TW201337266A - 利用生物標記診斷關節黏連脊椎炎之方法及組合物 - Google Patents
利用生物標記診斷關節黏連脊椎炎之方法及組合物 Download PDFInfo
- Publication number
- TW201337266A TW201337266A TW102119988A TW102119988A TW201337266A TW 201337266 A TW201337266 A TW 201337266A TW 102119988 A TW102119988 A TW 102119988A TW 102119988 A TW102119988 A TW 102119988A TW 201337266 A TW201337266 A TW 201337266A
- Authority
- TW
- Taiwan
- Prior art keywords
- content
- ctx
- biomarker
- treatment
- antibody
- Prior art date
Links
- 239000000090 biomarker Substances 0.000 title claims abstract description 296
- 206010002556 Ankylosing Spondylitis Diseases 0.000 title claims abstract 50
- 238000000034 method Methods 0.000 title abstract description 166
- 239000000203 mixture Substances 0.000 title description 39
- 239000000427 antigen Substances 0.000 claims abstract description 127
- 108091007433 antigens Proteins 0.000 claims abstract description 127
- 102000036639 antigens Human genes 0.000 claims abstract description 127
- 230000027455 binding Effects 0.000 claims abstract description 123
- 201000004595 synovitis Diseases 0.000 claims abstract description 119
- 230000011382 collagen catabolic process Effects 0.000 claims abstract description 77
- 238000011282 treatment Methods 0.000 claims description 147
- 235000001014 amino acid Nutrition 0.000 claims description 88
- 150000001413 amino acids Chemical class 0.000 claims description 81
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 70
- 101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 claims description 69
- 210000004027 cell Anatomy 0.000 claims description 60
- 108010016160 Matrix Metalloproteinase 3 Proteins 0.000 claims description 56
- 102000057041 human TNF Human genes 0.000 claims description 50
- 108060008682 Tumor Necrosis Factor Proteins 0.000 claims description 49
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 claims description 49
- 239000003814 drug Substances 0.000 claims description 49
- 229960002964 adalimumab Drugs 0.000 claims description 38
- 230000006378 damage Effects 0.000 claims description 38
- 102000000503 Collagen Type II Human genes 0.000 claims description 33
- 108010041390 Collagen Type II Proteins 0.000 claims description 33
- 108010074051 C-Reactive Protein Proteins 0.000 claims description 32
- 102100032752 C-reactive protein Human genes 0.000 claims description 32
- 201000002661 Spondylitis Diseases 0.000 claims description 31
- 210000002966 serum Anatomy 0.000 claims description 31
- 230000001225 therapeutic effect Effects 0.000 claims description 29
- 238000003556 assay Methods 0.000 claims description 26
- 210000002700 urine Anatomy 0.000 claims description 26
- 102000008186 Collagen Human genes 0.000 claims description 23
- 108010035532 Collagen Proteins 0.000 claims description 23
- 229920001436 collagen Polymers 0.000 claims description 23
- 101800001415 Bri23 peptide Proteins 0.000 claims description 21
- 101800000655 C-terminal peptide Proteins 0.000 claims description 21
- 102400000107 C-terminal peptide Human genes 0.000 claims description 21
- 206010058031 Joint adhesion Diseases 0.000 claims description 18
- 238000002360 preparation method Methods 0.000 claims description 17
- 238000002203 pretreatment Methods 0.000 claims description 14
- 235000004279 alanine Nutrition 0.000 claims description 13
- 230000002917 arthritic effect Effects 0.000 claims description 13
- 238000010494 dissociation reaction Methods 0.000 claims description 13
- 230000005593 dissociations Effects 0.000 claims description 13
- 238000006467 substitution reaction Methods 0.000 claims description 13
- 238000000338 in vitro Methods 0.000 claims description 12
- 239000002253 acid Substances 0.000 claims description 11
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 claims description 10
- 238000002965 ELISA Methods 0.000 claims description 8
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 claims description 8
- 230000003013 cytotoxicity Effects 0.000 claims description 8
- 231100000135 cytotoxicity Toxicity 0.000 claims description 8
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims description 7
- 229960001743 golimumab Drugs 0.000 claims description 6
- 230000004048 modification Effects 0.000 claims description 6
- 238000012986 modification Methods 0.000 claims description 6
- 229960002685 biotin Drugs 0.000 claims description 5
- 235000020958 biotin Nutrition 0.000 claims description 5
- 239000011616 biotin Substances 0.000 claims description 5
- 230000003115 biocidal effect Effects 0.000 claims description 4
- 230000017854 proteolysis Effects 0.000 claims description 4
- 125000003277 amino group Chemical group 0.000 claims description 3
- 230000000593 degrading effect Effects 0.000 claims description 3
- 230000036961 partial effect Effects 0.000 claims description 2
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 claims description 2
- 230000001988 toxicity Effects 0.000 claims description 2
- 231100000419 toxicity Toxicity 0.000 claims description 2
- 102000000422 Matrix Metalloproteinase 3 Human genes 0.000 claims 31
- 239000000825 pharmaceutical preparation Substances 0.000 claims 8
- 229940127557 pharmaceutical product Drugs 0.000 claims 8
- 238000006386 neutralization reaction Methods 0.000 claims 1
- 229940046728 tumor necrosis factor alpha inhibitor Drugs 0.000 abstract description 94
- 239000002452 tumor necrosis factor alpha inhibitor Substances 0.000 abstract description 59
- 108090000623 proteins and genes Proteins 0.000 description 100
- 239000012634 fragment Substances 0.000 description 97
- 208000001088 cerebrotendinous xanthomatosis Diseases 0.000 description 92
- 229940024606 amino acid Drugs 0.000 description 77
- 102100030416 Stromelysin-1 Human genes 0.000 description 54
- 108090000765 processed proteins & peptides Proteins 0.000 description 50
- 102000004169 proteins and genes Human genes 0.000 description 48
- 239000003795 chemical substances by application Substances 0.000 description 45
- 235000018102 proteins Nutrition 0.000 description 45
- 239000000523 sample Substances 0.000 description 42
- 206010003246 arthritis Diseases 0.000 description 38
- 108020004414 DNA Proteins 0.000 description 36
- 239000002451 tumor necrosis factor inhibitor Substances 0.000 description 35
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 31
- 101710108790 Stromelysin-1 Proteins 0.000 description 29
- VKUYLANQOAKALN-UHFFFAOYSA-N 2-[benzyl-(4-methoxyphenyl)sulfonylamino]-n-hydroxy-4-methylpentanamide Chemical group C1=CC(OC)=CC=C1S(=O)(=O)N(C(CC(C)C)C(=O)NO)CC1=CC=CC=C1 VKUYLANQOAKALN-UHFFFAOYSA-N 0.000 description 28
- 230000008355 cartilage degradation Effects 0.000 description 28
- 210000004602 germ cell Anatomy 0.000 description 28
- 239000013604 expression vector Substances 0.000 description 24
- 230000002485 urinary effect Effects 0.000 description 24
- 239000013598 vector Substances 0.000 description 23
- 108020004707 nucleic acids Proteins 0.000 description 22
- 102000039446 nucleic acids Human genes 0.000 description 22
- 150000007523 nucleic acids Chemical class 0.000 description 22
- 210000000845 cartilage Anatomy 0.000 description 21
- 239000003112 inhibitor Substances 0.000 description 21
- 102100040247 Tumor necrosis factor Human genes 0.000 description 19
- 206010061218 Inflammation Diseases 0.000 description 18
- 201000010099 disease Diseases 0.000 description 18
- 230000004054 inflammatory process Effects 0.000 description 18
- 108060003951 Immunoglobulin Proteins 0.000 description 17
- 208000006045 Spondylarthropathies Diseases 0.000 description 17
- 102000018358 immunoglobulin Human genes 0.000 description 17
- 239000008194 pharmaceutical composition Substances 0.000 description 17
- 238000003259 recombinant expression Methods 0.000 description 17
- 201000005671 spondyloarthropathy Diseases 0.000 description 17
- 229940124597 therapeutic agent Drugs 0.000 description 17
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 16
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 16
- 150000001875 compounds Chemical class 0.000 description 16
- 230000000694 effects Effects 0.000 description 16
- 239000013589 supplement Substances 0.000 description 16
- 238000002560 therapeutic procedure Methods 0.000 description 16
- 229940021182 non-steroidal anti-inflammatory drug Drugs 0.000 description 15
- 238000003752 polymerase chain reaction Methods 0.000 description 14
- 230000002829 reductive effect Effects 0.000 description 14
- 208000035475 disorder Diseases 0.000 description 13
- 230000014509 gene expression Effects 0.000 description 13
- 238000003199 nucleic acid amplification method Methods 0.000 description 13
- -1 polyethylene Polymers 0.000 description 13
- 239000000126 substance Substances 0.000 description 13
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 12
- 102000004127 Cytokines Human genes 0.000 description 12
- 108090000695 Cytokines Proteins 0.000 description 12
- 230000003321 amplification Effects 0.000 description 12
- 150000003384 small molecules Chemical class 0.000 description 12
- 210000001519 tissue Anatomy 0.000 description 12
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 11
- 241000219061 Rheum Species 0.000 description 11
- 239000003937 drug carrier Substances 0.000 description 11
- 229940068196 placebo Drugs 0.000 description 11
- 239000000902 placebo Substances 0.000 description 11
- 230000001105 regulatory effect Effects 0.000 description 11
- 239000000243 solution Substances 0.000 description 11
- 208000024891 symptom Diseases 0.000 description 11
- 201000001263 Psoriatic Arthritis Diseases 0.000 description 10
- 208000036824 Psoriatic arthropathy Diseases 0.000 description 10
- 238000006243 chemical reaction Methods 0.000 description 10
- 238000003018 immunoassay Methods 0.000 description 10
- 210000001503 joint Anatomy 0.000 description 10
- 230000004044 response Effects 0.000 description 10
- 102000004190 Enzymes Human genes 0.000 description 9
- 108090000790 Enzymes Proteins 0.000 description 9
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 9
- 102000002274 Matrix Metalloproteinases Human genes 0.000 description 9
- 108010000684 Matrix Metalloproteinases Proteins 0.000 description 9
- 230000007850 degeneration Effects 0.000 description 9
- 238000006731 degradation reaction Methods 0.000 description 9
- 238000001514 detection method Methods 0.000 description 9
- 230000009266 disease activity Effects 0.000 description 9
- 229940079593 drug Drugs 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- 238000009472 formulation Methods 0.000 description 9
- 229960000485 methotrexate Drugs 0.000 description 9
- 229920001223 polyethylene glycol Polymers 0.000 description 9
- 102000004196 processed proteins & peptides Human genes 0.000 description 9
- 208000002574 reactive arthritis Diseases 0.000 description 9
- 241000894007 species Species 0.000 description 9
- 206010003267 Arthritis reactive Diseases 0.000 description 8
- 208000012659 Joint disease Diseases 0.000 description 8
- 239000002202 Polyethylene glycol Substances 0.000 description 8
- 201000004681 Psoriasis Diseases 0.000 description 8
- 210000000988 bone and bone Anatomy 0.000 description 8
- 230000015556 catabolic process Effects 0.000 description 8
- 238000011161 development Methods 0.000 description 8
- 230000010076 replication Effects 0.000 description 8
- 239000013078 crystal Substances 0.000 description 7
- 239000003623 enhancer Substances 0.000 description 7
- OVBPIULPVIDEAO-LBPRGKRZSA-N folic acid Chemical compound C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-LBPRGKRZSA-N 0.000 description 7
- 230000006870 function Effects 0.000 description 7
- CGIGDMFJXJATDK-UHFFFAOYSA-N indomethacin Chemical compound CC1=C(CC(O)=O)C2=CC(OC)=CC=C2N1C(=O)C1=CC=C(Cl)C=C1 CGIGDMFJXJATDK-UHFFFAOYSA-N 0.000 description 7
- 229960000598 infliximab Drugs 0.000 description 7
- 238000004519 manufacturing process Methods 0.000 description 7
- 201000008482 osteoarthritis Diseases 0.000 description 7
- 230000001575 pathological effect Effects 0.000 description 7
- 210000002381 plasma Anatomy 0.000 description 7
- 108020004635 Complementary DNA Proteins 0.000 description 6
- 108010008165 Etanercept Proteins 0.000 description 6
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 6
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 6
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 108010076504 Protein Sorting Signals Proteins 0.000 description 6
- 108020004511 Recombinant DNA Proteins 0.000 description 6
- 238000010804 cDNA synthesis Methods 0.000 description 6
- 239000003153 chemical reaction reagent Substances 0.000 description 6
- 239000002299 complementary DNA Substances 0.000 description 6
- 239000000306 component Substances 0.000 description 6
- 230000003247 decreasing effect Effects 0.000 description 6
- 238000005516 engineering process Methods 0.000 description 6
- 210000002744 extracellular matrix Anatomy 0.000 description 6
- 108020001507 fusion proteins Proteins 0.000 description 6
- 102000037865 fusion proteins Human genes 0.000 description 6
- 230000006872 improvement Effects 0.000 description 6
- 238000001727 in vivo Methods 0.000 description 6
- 239000003550 marker Substances 0.000 description 6
- 108020004999 messenger RNA Proteins 0.000 description 6
- 239000002773 nucleotide Substances 0.000 description 6
- 125000003729 nucleotide group Chemical group 0.000 description 6
- 102000005962 receptors Human genes 0.000 description 6
- 108020003175 receptors Proteins 0.000 description 6
- 238000012216 screening Methods 0.000 description 6
- 239000007787 solid Substances 0.000 description 6
- 208000011231 Crohn disease Diseases 0.000 description 5
- 102000053602 DNA Human genes 0.000 description 5
- 108010087819 Fc receptors Proteins 0.000 description 5
- 102000009109 Fc receptors Human genes 0.000 description 5
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 5
- 206010023203 Joint destruction Diseases 0.000 description 5
- 206010052904 Musculoskeletal stiffness Diseases 0.000 description 5
- 208000025747 Rheumatic disease Diseases 0.000 description 5
- 108010090804 Streptavidin Proteins 0.000 description 5
- 125000000539 amino acid group Chemical group 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 5
- 239000003242 anti bacterial agent Substances 0.000 description 5
- 230000001588 bifunctional effect Effects 0.000 description 5
- MYSWGUAQZAJSOK-UHFFFAOYSA-N ciprofloxacin Chemical compound C12=CC(N3CCNCC3)=C(F)C=C2C(=O)C(C(=O)O)=CN1C1CC1 MYSWGUAQZAJSOK-UHFFFAOYSA-N 0.000 description 5
- 239000006185 dispersion Substances 0.000 description 5
- 229960000403 etanercept Drugs 0.000 description 5
- 238000007901 in situ hybridization Methods 0.000 description 5
- 208000015181 infectious disease Diseases 0.000 description 5
- 239000004615 ingredient Substances 0.000 description 5
- 230000003993 interaction Effects 0.000 description 5
- 125000005647 linker group Chemical group 0.000 description 5
- 230000001404 mediated effect Effects 0.000 description 5
- 238000002703 mutagenesis Methods 0.000 description 5
- 231100000350 mutagenesis Toxicity 0.000 description 5
- 230000003472 neutralizing effect Effects 0.000 description 5
- 239000000041 non-steroidal anti-inflammatory agent Substances 0.000 description 5
- 230000007310 pathophysiology Effects 0.000 description 5
- 229920001184 polypeptide Polymers 0.000 description 5
- 239000013615 primer Substances 0.000 description 5
- 230000000069 prophylactic effect Effects 0.000 description 5
- 238000003127 radioimmunoassay Methods 0.000 description 5
- 230000009467 reduction Effects 0.000 description 5
- 206010039073 rheumatoid arthritis Diseases 0.000 description 5
- 238000010561 standard procedure Methods 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 238000013518 transcription Methods 0.000 description 5
- 230000035897 transcription Effects 0.000 description 5
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 4
- RZVAJINKPMORJF-UHFFFAOYSA-N Acetaminophen Chemical compound CC(=O)NC1=CC=C(O)C=C1 RZVAJINKPMORJF-UHFFFAOYSA-N 0.000 description 4
- 102000014914 Carrier Proteins Human genes 0.000 description 4
- 208000022559 Inflammatory bowel disease Diseases 0.000 description 4
- UETNIIAIRMUTSM-UHFFFAOYSA-N Jacareubin Natural products CC1(C)OC2=CC3Oc4c(O)c(O)ccc4C(=O)C3C(=C2C=C1)O UETNIIAIRMUTSM-UHFFFAOYSA-N 0.000 description 4
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 4
- 238000000636 Northern blotting Methods 0.000 description 4
- 101710163270 Nuclease Proteins 0.000 description 4
- 208000002193 Pain Diseases 0.000 description 4
- 230000003110 anti-inflammatory effect Effects 0.000 description 4
- 229940088710 antibiotic agent Drugs 0.000 description 4
- 108091008324 binding proteins Proteins 0.000 description 4
- 230000004071 biological effect Effects 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 210000001124 body fluid Anatomy 0.000 description 4
- 239000010839 body fluid Substances 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 230000001684 chronic effect Effects 0.000 description 4
- 238000002648 combination therapy Methods 0.000 description 4
- 230000001419 dependent effect Effects 0.000 description 4
- 238000013461 design Methods 0.000 description 4
- 230000001627 detrimental effect Effects 0.000 description 4
- 239000003974 emollient agent Substances 0.000 description 4
- 235000019152 folic acid Nutrition 0.000 description 4
- 239000011724 folic acid Substances 0.000 description 4
- 230000002068 genetic effect Effects 0.000 description 4
- 230000036541 health Effects 0.000 description 4
- 229940048921 humira Drugs 0.000 description 4
- 238000009396 hybridization Methods 0.000 description 4
- JYGXADMDTFJGBT-VWUMJDOOSA-N hydrocortisone Chemical compound O=C1CC[C@]2(C)[C@H]3[C@@H](O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 JYGXADMDTFJGBT-VWUMJDOOSA-N 0.000 description 4
- 230000002757 inflammatory effect Effects 0.000 description 4
- 230000005764 inhibitory process Effects 0.000 description 4
- 238000002372 labelling Methods 0.000 description 4
- 238000012544 monitoring process Methods 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 230000007170 pathology Effects 0.000 description 4
- 230000006320 pegylation Effects 0.000 description 4
- 210000002706 plastid Anatomy 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- ZCCUUQDIBDJBTK-UHFFFAOYSA-N psoralen Chemical compound C1=C2OC(=O)C=CC2=CC2=C1OC=C2 ZCCUUQDIBDJBTK-UHFFFAOYSA-N 0.000 description 4
- YGSDEFSMJLZEOE-UHFFFAOYSA-N salicylic acid Chemical compound OC(=O)C1=CC=CC=C1O YGSDEFSMJLZEOE-UHFFFAOYSA-N 0.000 description 4
- 238000007920 subcutaneous administration Methods 0.000 description 4
- 229960001940 sulfasalazine Drugs 0.000 description 4
- NCEXYHBECQHGNR-QZQOTICOSA-N sulfasalazine Chemical compound C1=C(O)C(C(=O)O)=CC(\N=N\C=2C=CC(=CC=2)S(=O)(=O)NC=2N=CC=CC=2)=C1 NCEXYHBECQHGNR-QZQOTICOSA-N 0.000 description 4
- NCEXYHBECQHGNR-UHFFFAOYSA-N sulfasalazine Natural products C1=C(O)C(C(=O)O)=CC(N=NC=2C=CC(=CC=2)S(=O)(=O)NC=2N=CC=CC=2)=C1 NCEXYHBECQHGNR-UHFFFAOYSA-N 0.000 description 4
- 238000001890 transfection Methods 0.000 description 4
- 230000003612 virological effect Effects 0.000 description 4
- 238000001262 western blot Methods 0.000 description 4
- HVCOBJNICQPDBP-UHFFFAOYSA-N 3-[3-[3,5-dihydroxy-6-methyl-4-(3,4,5-trihydroxy-6-methyloxan-2-yl)oxyoxan-2-yl]oxydecanoyloxy]decanoic acid;hydrate Chemical compound O.OC1C(OC(CC(=O)OC(CCCCCCC)CC(O)=O)CCCCCCC)OC(C)C(O)C1OC1C(O)C(O)C(O)C(C)O1 HVCOBJNICQPDBP-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 208000006386 Bone Resorption Diseases 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- 229930186217 Glycolipid Natural products 0.000 description 3
- 108010061486 HLA-B27 Antigen Proteins 0.000 description 3
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 3
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 3
- 102100034343 Integrase Human genes 0.000 description 3
- 108090000978 Interleukin-4 Proteins 0.000 description 3
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 3
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 3
- 241000829100 Macaca mulatta polyomavirus 1 Species 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- OVBPIULPVIDEAO-UHFFFAOYSA-N N-Pteroyl-L-glutaminsaeure Natural products C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)NC(CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-UHFFFAOYSA-N 0.000 description 3
- 108091034117 Oligonucleotide Proteins 0.000 description 3
- 239000004698 Polyethylene Substances 0.000 description 3
- 108010067787 Proteoglycans Proteins 0.000 description 3
- 102000016611 Proteoglycans Human genes 0.000 description 3
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 3
- 108010022394 Threonine synthase Proteins 0.000 description 3
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 3
- 239000000556 agonist Substances 0.000 description 3
- LMEKQMALGUDUQG-UHFFFAOYSA-N azathioprine Chemical compound CN1C=NC([N+]([O-])=O)=C1SC1=NC=NC2=C1NC=N2 LMEKQMALGUDUQG-UHFFFAOYSA-N 0.000 description 3
- 229960002170 azathioprine Drugs 0.000 description 3
- 230000009286 beneficial effect Effects 0.000 description 3
- 230000024279 bone resorption Effects 0.000 description 3
- 239000000969 carrier Substances 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 239000007795 chemical reaction product Substances 0.000 description 3
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 3
- 230000000295 complement effect Effects 0.000 description 3
- 230000000875 corresponding effect Effects 0.000 description 3
- 229960001259 diclofenac Drugs 0.000 description 3
- DCOPUUMXTXDBNB-UHFFFAOYSA-N diclofenac Chemical compound OC(=O)CC1=CC=CC=C1NC1=C(Cl)C=CC=C1Cl DCOPUUMXTXDBNB-UHFFFAOYSA-N 0.000 description 3
- 102000004419 dihydrofolate reductase Human genes 0.000 description 3
- 230000009977 dual effect Effects 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 229960001347 fluocinolone acetonide Drugs 0.000 description 3
- FEBLZLNTKCEFIT-VSXGLTOVSA-N fluocinolone acetonide Chemical compound C1([C@@H](F)C2)=CC(=O)C=C[C@]1(C)[C@]1(F)[C@@H]2[C@@H]2C[C@H]3OC(C)(C)O[C@@]3(C(=O)CO)[C@@]2(C)C[C@@H]1O FEBLZLNTKCEFIT-VSXGLTOVSA-N 0.000 description 3
- 229960000304 folic acid Drugs 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 229960000905 indomethacin Drugs 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 238000001990 intravenous administration Methods 0.000 description 3
- 239000003446 ligand Substances 0.000 description 3
- 239000007937 lozenge Substances 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- VAOCPAMSLUNLGC-UHFFFAOYSA-N metronidazole Chemical compound CC1=NC=C([N+]([O-])=O)N1CCO VAOCPAMSLUNLGC-UHFFFAOYSA-N 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- CMWTZPSULFXXJA-VIFPVBQESA-N naproxen Chemical compound C1=C([C@H](C)C(O)=O)C=CC2=CC(OC)=CC=C21 CMWTZPSULFXXJA-VIFPVBQESA-N 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 239000013610 patient sample Substances 0.000 description 3
- 238000002823 phage display Methods 0.000 description 3
- 229920000573 polyethylene Polymers 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- XOFYZVNMUHMLCC-ZPOLXVRWSA-N prednisone Chemical compound O=C1C=C[C@]2(C)[C@H]3C(=O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 XOFYZVNMUHMLCC-ZPOLXVRWSA-N 0.000 description 3
- 229960004618 prednisone Drugs 0.000 description 3
- 238000001742 protein purification Methods 0.000 description 3
- 238000012207 quantitative assay Methods 0.000 description 3
- 238000003757 reverse transcription PCR Methods 0.000 description 3
- 238000010254 subcutaneous injection Methods 0.000 description 3
- 239000007929 subcutaneous injection Substances 0.000 description 3
- 208000011580 syndromic disease Diseases 0.000 description 3
- 238000013519 translation Methods 0.000 description 3
- 241000701161 unidentified adenovirus Species 0.000 description 3
- LJRDOKAZOAKLDU-UDXJMMFXSA-N (2s,3s,4r,5r,6r)-5-amino-2-(aminomethyl)-6-[(2r,3s,4r,5s)-5-[(1r,2r,3s,5r,6s)-3,5-diamino-2-[(2s,3r,4r,5s,6r)-3-amino-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-6-hydroxycyclohexyl]oxy-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl]oxyoxane-3,4-diol;sulfuric ac Chemical compound OS(O)(=O)=O.N[C@@H]1[C@@H](O)[C@H](O)[C@H](CN)O[C@@H]1O[C@H]1[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](N)C[C@@H](N)[C@@H]2O)O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O2)N)O[C@@H]1CO LJRDOKAZOAKLDU-UDXJMMFXSA-N 0.000 description 2
- PQMFVUNERGGBPG-UHFFFAOYSA-N (6-bromopyridin-2-yl)hydrazine Chemical compound NNC1=CC=CC(Br)=N1 PQMFVUNERGGBPG-UHFFFAOYSA-N 0.000 description 2
- VXGRJERITKFWPL-UHFFFAOYSA-N 4',5'-Dihydropsoralen Natural products C1=C2OC(=O)C=CC2=CC2=C1OCC2 VXGRJERITKFWPL-UHFFFAOYSA-N 0.000 description 2
- 206010069754 Acquired gene mutation Diseases 0.000 description 2
- 208000008035 Back Pain Diseases 0.000 description 2
- PTOAARAWEBMLNO-KVQBGUIXSA-N Cladribine Chemical compound C1=NC=2C(N)=NC(Cl)=NC=2N1[C@H]1C[C@H](O)[C@@H](CO)O1 PTOAARAWEBMLNO-KVQBGUIXSA-N 0.000 description 2
- 102000012422 Collagen Type I Human genes 0.000 description 2
- 108010022452 Collagen Type I Proteins 0.000 description 2
- 102000029816 Collagenase Human genes 0.000 description 2
- 108060005980 Collagenase Proteins 0.000 description 2
- 101150074155 DHFR gene Proteins 0.000 description 2
- 230000004544 DNA amplification Effects 0.000 description 2
- 239000003298 DNA probe Substances 0.000 description 2
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 2
- 229920002307 Dextran Polymers 0.000 description 2
- 102000005593 Endopeptidases Human genes 0.000 description 2
- 108010059378 Endopeptidases Proteins 0.000 description 2
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 2
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 2
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 2
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 2
- 102000012153 HLA-B27 Antigen Human genes 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 2
- 102000051628 Interleukin-1 receptor antagonist Human genes 0.000 description 2
- 108700021006 Interleukin-1 receptor antagonist Proteins 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- FQISKWAFAHGMGT-SGJOWKDISA-M Methylprednisolone sodium succinate Chemical compound [Na+].C([C@@]12C)=CC(=O)C=C1[C@@H](C)C[C@@H]1[C@@H]2[C@@H](O)C[C@]2(C)[C@@](O)(C(=O)COC(=O)CCC([O-])=O)CC[C@H]21 FQISKWAFAHGMGT-SGJOWKDISA-M 0.000 description 2
- 241001529936 Murinae Species 0.000 description 2
- 101100268066 Mus musculus Zap70 gene Proteins 0.000 description 2
- CMWTZPSULFXXJA-UHFFFAOYSA-N Naproxen Natural products C1=C(C(C)C(O)=O)C=CC2=CC(OC)=CC=C21 CMWTZPSULFXXJA-UHFFFAOYSA-N 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- XBDQKXXYIPTUBI-UHFFFAOYSA-M Propionate Chemical compound CCC([O-])=O XBDQKXXYIPTUBI-UHFFFAOYSA-M 0.000 description 2
- 239000013614 RNA sample Substances 0.000 description 2
- 102000006382 Ribonucleases Human genes 0.000 description 2
- 108010083644 Ribonucleases Proteins 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- QJJXYPPXXYFBGM-LFZNUXCKSA-N Tacrolimus Chemical compound C1C[C@@H](O)[C@H](OC)C[C@@H]1\C=C(/C)[C@@H]1[C@H](C)[C@@H](O)CC(=O)[C@H](CC=C)/C=C(C)/C[C@H](C)C[C@H](OC)[C@H]([C@H](C[C@H]2C)OC)O[C@@]2(O)C(=O)C(=O)N2CCCC[C@H]2C(=O)O1 QJJXYPPXXYFBGM-LFZNUXCKSA-N 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 2
- 102100033732 Tumor necrosis factor receptor superfamily member 1A Human genes 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 230000001154 acute effect Effects 0.000 description 2
- 230000009824 affinity maturation Effects 0.000 description 2
- 210000003423 ankle Anatomy 0.000 description 2
- 229940124599 anti-inflammatory drug Drugs 0.000 description 2
- 230000000692 anti-sense effect Effects 0.000 description 2
- 229960005475 antiinfective agent Drugs 0.000 description 2
- 239000004599 antimicrobial Substances 0.000 description 2
- 210000001188 articular cartilage Anatomy 0.000 description 2
- 210000000544 articulatio talocruralis Anatomy 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 2
- 229960000074 biopharmaceutical Drugs 0.000 description 2
- 239000004327 boric acid Substances 0.000 description 2
- 239000001506 calcium phosphate Substances 0.000 description 2
- 229910000389 calcium phosphate Inorganic materials 0.000 description 2
- 235000011010 calcium phosphates Nutrition 0.000 description 2
- 201000011510 cancer Diseases 0.000 description 2
- 230000008422 cartilage matrix degradation Effects 0.000 description 2
- 230000020411 cell activation Effects 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 229960003405 ciprofloxacin Drugs 0.000 description 2
- AGOYDEPGAOXOCK-KCBOHYOISA-N clarithromycin Chemical compound O([C@@H]1[C@@H](C)C(=O)O[C@@H]([C@@]([C@H](O)[C@@H](C)C(=O)[C@H](C)C[C@](C)([C@H](O[C@H]2[C@@H]([C@H](C[C@@H](C)O2)N(C)C)O)[C@H]1C)OC)(C)O)CC)[C@H]1C[C@@](C)(OC)[C@@H](O)[C@H](C)O1 AGOYDEPGAOXOCK-KCBOHYOISA-N 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 229960001214 clofibrate Drugs 0.000 description 2
- KNHUKKLJHYUCFP-UHFFFAOYSA-N clofibrate Chemical compound CCOC(=O)C(C)(C)OC1=CC=C(Cl)C=C1 KNHUKKLJHYUCFP-UHFFFAOYSA-N 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 229960002424 collagenase Drugs 0.000 description 2
- 238000012875 competitive assay Methods 0.000 description 2
- 238000013270 controlled release Methods 0.000 description 2
- 239000003246 corticosteroid Substances 0.000 description 2
- 229960001334 corticosteroids Drugs 0.000 description 2
- RMRCNWBMXRMIRW-BYFNXCQMSA-M cyanocobalamin Chemical compound N#C[Co+]N([C@]1([H])[C@H](CC(N)=O)[C@]\2(CCC(=O)NC[C@H](C)OP(O)(=O)OC3[C@H]([C@H](O[C@@H]3CO)N3C4=CC(C)=C(C)C=C4N=C3)O)C)C/2=C(C)\C([C@H](C/2(C)C)CCC(N)=O)=N\C\2=C\C([C@H]([C@@]/2(CC(N)=O)C)CCC(N)=O)=N\C\2=C(C)/C2=N[C@]1(C)[C@@](C)(CC(N)=O)[C@@H]2CCC(N)=O RMRCNWBMXRMIRW-BYFNXCQMSA-M 0.000 description 2
- 238000003745 diagnosis Methods 0.000 description 2
- 239000002612 dispersion medium Substances 0.000 description 2
- 239000012636 effector Substances 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 208000037902 enteropathy Diseases 0.000 description 2
- 230000003628 erosive effect Effects 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 229960000890 hydrocortisone Drugs 0.000 description 2
- XXSMGPRMXLTPCZ-UHFFFAOYSA-N hydroxychloroquine Chemical compound ClC1=CC=C2C(NC(C)CCCN(CCO)CC)=CC=NC2=C1 XXSMGPRMXLTPCZ-UHFFFAOYSA-N 0.000 description 2
- 229960004171 hydroxychloroquine Drugs 0.000 description 2
- 230000003053 immunization Effects 0.000 description 2
- 238000002649 immunization Methods 0.000 description 2
- 238000010166 immunofluorescence Methods 0.000 description 2
- 229940072221 immunoglobulins Drugs 0.000 description 2
- 208000027866 inflammatory disease Diseases 0.000 description 2
- 238000001802 infusion Methods 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 208000028774 intestinal disease Diseases 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- 239000007951 isotonicity adjuster Substances 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 230000004060 metabolic process Effects 0.000 description 2
- 229960000282 metronidazole Drugs 0.000 description 2
- 239000002480 mineral oil Substances 0.000 description 2
- 235000010446 mineral oil Nutrition 0.000 description 2
- HPNSFSBZBAHARI-RUDMXATFSA-N mycophenolic acid Chemical compound OC1=C(C\C=C(/C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-RUDMXATFSA-N 0.000 description 2
- 229960002009 naproxen Drugs 0.000 description 2
- 210000000056 organ Anatomy 0.000 description 2
- FJKROLUGYXJWQN-UHFFFAOYSA-N papa-hydroxy-benzoic acid Natural products OC(=O)C1=CC=C(O)C=C1 FJKROLUGYXJWQN-UHFFFAOYSA-N 0.000 description 2
- 229960001639 penicillamine Drugs 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- KASDHRXLYQOAKZ-ZPSXYTITSA-N pimecrolimus Chemical compound C/C([C@H]1OC(=O)[C@@H]2CCCCN2C(=O)C(=O)[C@]2(O)O[C@@H]([C@H](C[C@H]2C)OC)[C@@H](OC)C[C@@H](C)C/C(C)=C/[C@H](C(C[C@H](O)[C@H]1C)=O)CC)=C\[C@@H]1CC[C@@H](Cl)[C@H](OC)C1 KASDHRXLYQOAKZ-ZPSXYTITSA-N 0.000 description 2
- 229960005330 pimecrolimus Drugs 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- ZAHRKKWIAAJSAO-UHFFFAOYSA-N rapamycin Natural products COCC(O)C(=C/C(C)C(=O)CC(OC(=O)C1CCCCN1C(=O)C(=O)C2(O)OC(CC(OC)C(=CC=CC=CC(C)CC(C)C(=O)C)C)CCC2C)C(C)CC3CCC(O)C(C3)OC)C ZAHRKKWIAAJSAO-UHFFFAOYSA-N 0.000 description 2
- 238000003753 real-time PCR Methods 0.000 description 2
- 229940116176 remicade Drugs 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 229960004889 salicylic acid Drugs 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 238000009097 single-agent therapy Methods 0.000 description 2
- 229960002930 sirolimus Drugs 0.000 description 2
- QFJCIRLUMZQUOT-HPLJOQBZSA-N sirolimus Chemical compound C1C[C@@H](O)[C@H](OC)C[C@@H]1C[C@@H](C)[C@H]1OC(=O)[C@@H]2CCCCN2C(=O)C(=O)[C@](O)(O2)[C@H](C)CC[C@H]2C[C@H](OC)/C(C)=C/C=C/C=C/[C@@H](C)C[C@@H](C)C(=O)[C@H](OC)[C@H](O)/C(C)=C/[C@@H](C)C(=O)C1 QFJCIRLUMZQUOT-HPLJOQBZSA-N 0.000 description 2
- 238000002741 site-directed mutagenesis Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 230000037439 somatic mutation Effects 0.000 description 2
- 238000012409 standard PCR amplification Methods 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 230000002195 synergetic effect Effects 0.000 description 2
- 210000001179 synovial fluid Anatomy 0.000 description 2
- 210000001258 synovial membrane Anatomy 0.000 description 2
- 229940033663 thimerosal Drugs 0.000 description 2
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 2
- 238000004809 thin layer chromatography Methods 0.000 description 2
- UPSPUYADGBWSHF-UHFFFAOYSA-N tolmetin Chemical compound C1=CC(C)=CC=C1C(=O)C1=CC=C(CC(O)=O)N1C UPSPUYADGBWSHF-UHFFFAOYSA-N 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 230000009261 transgenic effect Effects 0.000 description 2
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 2
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- 239000013603 viral vector Substances 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 229920003169 water-soluble polymer Polymers 0.000 description 2
- 230000003442 weekly effect Effects 0.000 description 2
- RJNRORZRFGUAKL-ADMBVFOFSA-N (1r)-1-[(3ar,5r,6s,6ar)-6-[3-(dimethylamino)propoxy]-2,2-dimethyl-3a,5,6,6a-tetrahydrofuro[2,3-d][1,3]dioxol-5-yl]ethane-1,2-diol;hydrochloride Chemical compound Cl.O1C(C)(C)O[C@@H]2[C@@H](OCCCN(C)C)[C@@H]([C@H](O)CO)O[C@@H]21 RJNRORZRFGUAKL-ADMBVFOFSA-N 0.000 description 1
- XMAYWYJOQHXEEK-OZXSUGGESA-N (2R,4S)-ketoconazole Chemical compound C1CN(C(=O)C)CCN1C(C=C1)=CC=C1OC[C@@H]1O[C@@](CN2C=NC=C2)(C=2C(=CC(Cl)=CC=2)Cl)OC1 XMAYWYJOQHXEEK-OZXSUGGESA-N 0.000 description 1
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- OTHYPAMNTUGKDK-UHFFFAOYSA-N (3-acetylphenyl) acetate Chemical compound CC(=O)OC1=CC=CC(C(C)=O)=C1 OTHYPAMNTUGKDK-UHFFFAOYSA-N 0.000 description 1
- VEEGZPWAAPPXRB-BJMVGYQFSA-N (3e)-3-(1h-imidazol-5-ylmethylidene)-1h-indol-2-one Chemical compound O=C1NC2=CC=CC=C2\C1=C/C1=CN=CN1 VEEGZPWAAPPXRB-BJMVGYQFSA-N 0.000 description 1
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 1
- OJHZNMVJJKMFGX-RNWHKREASA-N (4r,4ar,7ar,12bs)-9-methoxy-3-methyl-1,2,4,4a,5,6,7a,13-octahydro-4,12-methanobenzofuro[3,2-e]isoquinoline-7-one;2,3-dihydroxybutanedioic acid Chemical compound OC(=O)C(O)C(O)C(O)=O.O=C([C@@H]1O2)CC[C@H]3[C@]4([H])N(C)CC[C@]13C1=C2C(OC)=CC=C1C4 OJHZNMVJJKMFGX-RNWHKREASA-N 0.000 description 1
- DKSZLDSPXIWGFO-BLOJGBSASA-N (4r,4ar,7s,7ar,12bs)-9-methoxy-3-methyl-2,4,4a,7,7a,13-hexahydro-1h-4,12-methanobenzofuro[3,2-e]isoquinoline-7-ol;phosphoric acid;hydrate Chemical compound O.OP(O)(O)=O.OP(O)(O)=O.C([C@H]1[C@H](N(CC[C@@]112)C)C3)=C[C@H](O)[C@@H]1OC1=C2C3=CC=C1OC.C([C@H]1[C@H](N(CC[C@@]112)C)C3)=C[C@H](O)[C@@H]1OC1=C2C3=CC=C1OC DKSZLDSPXIWGFO-BLOJGBSASA-N 0.000 description 1
- YCIHPQHVWDULOY-FMZCEJRJSA-N (4s,4as,5as,6s,12ar)-4-(dimethylamino)-1,6,10,11,12a-pentahydroxy-6-methyl-3,12-dioxo-4,4a,5,5a-tetrahydrotetracene-2-carboxamide;hydrochloride Chemical compound Cl.C1=CC=C2[C@](O)(C)[C@H]3C[C@H]4[C@H](N(C)C)C(=O)C(C(N)=O)=C(O)[C@@]4(O)C(=O)C3=C(O)C2=C1O YCIHPQHVWDULOY-FMZCEJRJSA-N 0.000 description 1
- QUPFKBITVLIQNA-KPKJPENVSA-N (5e)-2-sulfanylidene-5-[[5-[3-(trifluoromethyl)phenyl]furan-2-yl]methylidene]-1,3-thiazolidin-4-one Chemical compound FC(F)(F)C1=CC=CC(C=2OC(\C=C\3C(NC(=S)S/3)=O)=CC=2)=C1 QUPFKBITVLIQNA-KPKJPENVSA-N 0.000 description 1
- HMLGSIZOMSVISS-ONJSNURVSA-N (7r)-7-[[(2z)-2-(2-amino-1,3-thiazol-4-yl)-2-(2,2-dimethylpropanoyloxymethoxyimino)acetyl]amino]-3-ethenyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid Chemical compound N([C@@H]1C(N2C(=C(C=C)CSC21)C(O)=O)=O)C(=O)\C(=N/OCOC(=O)C(C)(C)C)C1=CSC(N)=N1 HMLGSIZOMSVISS-ONJSNURVSA-N 0.000 description 1
- WHTVZRBIWZFKQO-AWEZNQCLSA-N (S)-chloroquine Chemical compound ClC1=CC=C2C(N[C@@H](C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-AWEZNQCLSA-N 0.000 description 1
- VZXTWGWHSMCWGA-UHFFFAOYSA-N 1,3,5-triazine-2,4-diamine Chemical compound NC1=NC=NC(N)=N1 VZXTWGWHSMCWGA-UHFFFAOYSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- UEJJHQNACJXSKW-UHFFFAOYSA-N 2-(2,6-dioxopiperidin-3-yl)-1H-isoindole-1,3(2H)-dione Chemical compound O=C1C2=CC=CC=C2C(=O)N1C1CCC(=O)NC1=O UEJJHQNACJXSKW-UHFFFAOYSA-N 0.000 description 1
- VTAKZNRDSPNOAU-UHFFFAOYSA-M 2-(chloromethyl)oxirane;hydron;prop-2-en-1-amine;n-prop-2-enyldecan-1-amine;trimethyl-[6-(prop-2-enylamino)hexyl]azanium;dichloride Chemical compound Cl.[Cl-].NCC=C.ClCC1CO1.CCCCCCCCCCNCC=C.C[N+](C)(C)CCCCCCNCC=C VTAKZNRDSPNOAU-UHFFFAOYSA-M 0.000 description 1
- CVOFKRWYWCSDMA-UHFFFAOYSA-N 2-chloro-n-(2,6-diethylphenyl)-n-(methoxymethyl)acetamide;2,6-dinitro-n,n-dipropyl-4-(trifluoromethyl)aniline Chemical compound CCC1=CC=CC(CC)=C1N(COC)C(=O)CCl.CCCN(CCC)C1=C([N+]([O-])=O)C=C(C(F)(F)F)C=C1[N+]([O-])=O CVOFKRWYWCSDMA-UHFFFAOYSA-N 0.000 description 1
- NBUHTTJGQKIBMR-UHFFFAOYSA-N 4,6-dimethylpyrimidin-5-amine Chemical compound CC1=NC=NC(C)=C1N NBUHTTJGQKIBMR-UHFFFAOYSA-N 0.000 description 1
- IMPPGHMHELILKG-UHFFFAOYSA-N 4-ethoxyaniline Chemical compound CCOC1=CC=C(N)C=C1 IMPPGHMHELILKG-UHFFFAOYSA-N 0.000 description 1
- SUBDBMMJDZJVOS-UHFFFAOYSA-N 5-methoxy-2-{[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]sulfinyl}-1H-benzimidazole Chemical compound N=1C2=CC(OC)=CC=C2NC=1S(=O)CC1=NC=C(C)C(OC)=C1C SUBDBMMJDZJVOS-UHFFFAOYSA-N 0.000 description 1
- 102100026802 72 kDa type IV collagenase Human genes 0.000 description 1
- 101710151806 72 kDa type IV collagenase Proteins 0.000 description 1
- 239000005541 ACE inhibitor Substances 0.000 description 1
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
- 241000251468 Actinopterygii Species 0.000 description 1
- 102000007469 Actins Human genes 0.000 description 1
- 108010085238 Actins Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 108700028369 Alleles Proteins 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 102000005590 Anaphylatoxin C5a Receptor Human genes 0.000 description 1
- 108010059426 Anaphylatoxin C5a Receptor Proteins 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 206010003253 Arthritis enteropathic Diseases 0.000 description 1
- 208000036487 Arthropathies Diseases 0.000 description 1
- BSYNRYMUTXBXSQ-UHFFFAOYSA-N Aspirin Chemical compound CC(=O)OC1=CC=CC=C1C(O)=O BSYNRYMUTXBXSQ-UHFFFAOYSA-N 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 208000035143 Bacterial infection Diseases 0.000 description 1
- 206010051728 Bone erosion Diseases 0.000 description 1
- VOVIALXJUBGFJZ-KWVAZRHASA-N Budesonide Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@@H]2[C@@H]1[C@@H]1C[C@H]3OC(CCC)O[C@@]3(C(=O)CO)[C@@]1(C)C[C@@H]2O VOVIALXJUBGFJZ-KWVAZRHASA-N 0.000 description 1
- 102100035875 C-C chemokine receptor type 5 Human genes 0.000 description 1
- 101710149870 C-C chemokine receptor type 5 Proteins 0.000 description 1
- 102100025074 C-C chemokine receptor-like 2 Human genes 0.000 description 1
- 102100028990 C-X-C chemokine receptor type 3 Human genes 0.000 description 1
- 241000589876 Campylobacter Species 0.000 description 1
- 108090000426 Caspase-1 Proteins 0.000 description 1
- 241000606161 Chlamydia Species 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 1
- 229920001268 Cholestyramine Polymers 0.000 description 1
- 101000573882 Coccidioides posadasii (strain C735) Neutral protease 2 homolog MEP3 Proteins 0.000 description 1
- 206010009900 Colitis ulcerative Diseases 0.000 description 1
- 102100027995 Collagenase 3 Human genes 0.000 description 1
- 108050005238 Collagenase 3 Proteins 0.000 description 1
- 206010010741 Conjunctivitis Diseases 0.000 description 1
- 239000004971 Cross linker Substances 0.000 description 1
- 102000001493 Cyclophilins Human genes 0.000 description 1
- 108010068682 Cyclophilins Proteins 0.000 description 1
- CMSMOCZEIVJLDB-UHFFFAOYSA-N Cyclophosphamide Chemical compound ClCCN(CCCl)P1(=O)NCCCO1 CMSMOCZEIVJLDB-UHFFFAOYSA-N 0.000 description 1
- PMATZTZNYRCHOR-CGLBZJNRSA-N Cyclosporin A Chemical compound CC[C@@H]1NC(=O)[C@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O PMATZTZNYRCHOR-CGLBZJNRSA-N 0.000 description 1
- 108010036949 Cyclosporine Proteins 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- 102000012410 DNA Ligases Human genes 0.000 description 1
- 108010061982 DNA Ligases Proteins 0.000 description 1
- 108020003215 DNA Probes Proteins 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 238000012270 DNA recombination Methods 0.000 description 1
- 101100481408 Danio rerio tie2 gene Proteins 0.000 description 1
- 241001232464 Delma Species 0.000 description 1
- 206010061818 Disease progression Diseases 0.000 description 1
- QXNVGIXVLWOKEQ-UHFFFAOYSA-N Disodium Chemical compound [Na][Na] QXNVGIXVLWOKEQ-UHFFFAOYSA-N 0.000 description 1
- 108010024212 E-Selectin Proteins 0.000 description 1
- 102100023471 E-selectin Human genes 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- JOYRKODLDBILNP-UHFFFAOYSA-N Ethyl urethane Chemical compound CCOC(N)=O JOYRKODLDBILNP-UHFFFAOYSA-N 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 102000016359 Fibronectins Human genes 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- WJOHZNCJWYWUJD-IUGZLZTKSA-N Fluocinonide Chemical compound C1([C@@H](F)C2)=CC(=O)C=C[C@]1(C)[C@]1(F)[C@@H]2[C@@H]2C[C@H]3OC(C)(C)O[C@@]3(C(=O)COC(=O)C)[C@@]2(C)C[C@@H]1O WJOHZNCJWYWUJD-IUGZLZTKSA-N 0.000 description 1
- POPFMWWJOGLOIF-XWCQMRHXSA-N Flurandrenolide Chemical compound C1([C@@H](F)C2)=CC(=O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2C[C@H]3OC(C)(C)O[C@@]3(C(=O)CO)[C@@]2(C)C[C@@H]1O POPFMWWJOGLOIF-XWCQMRHXSA-N 0.000 description 1
- 206010017533 Fungal infection Diseases 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 102000013382 Gelatinases Human genes 0.000 description 1
- 108010026132 Gelatinases Proteins 0.000 description 1
- 102000006395 Globulins Human genes 0.000 description 1
- 108010044091 Globulins Proteins 0.000 description 1
- 108090000079 Glucocorticoid Receptors Proteins 0.000 description 1
- 102100033417 Glucocorticoid receptor Human genes 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 102100031181 Glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 229920002683 Glycosaminoglycan Polymers 0.000 description 1
- 208000009329 Graft vs Host Disease Diseases 0.000 description 1
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 101000798902 Homo sapiens Atypical chemokine receptor 4 Proteins 0.000 description 1
- 101000916050 Homo sapiens C-X-C chemokine receptor type 3 Proteins 0.000 description 1
- 101000917826 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor II-a Proteins 0.000 description 1
- 101000917824 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor II-b Proteins 0.000 description 1
- 101000990915 Homo sapiens Stromelysin-1 Proteins 0.000 description 1
- 108010091358 Hypoxanthine Phosphoribosyltransferase Proteins 0.000 description 1
- 102000018251 Hypoxanthine Phosphoribosyltransferase Human genes 0.000 description 1
- HEFNNWSXXWATRW-UHFFFAOYSA-N Ibuprofen Chemical compound CC(C)CC1=CC=C(C(C)C(O)=O)C=C1 HEFNNWSXXWATRW-UHFFFAOYSA-N 0.000 description 1
- 108010041012 Integrin alpha4 Proteins 0.000 description 1
- 108010064593 Intercellular Adhesion Molecule-1 Proteins 0.000 description 1
- 102100037877 Intercellular adhesion molecule 1 Human genes 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 102100026018 Interleukin-1 receptor antagonist protein Human genes 0.000 description 1
- 101710144554 Interleukin-1 receptor antagonist protein Proteins 0.000 description 1
- 102100023533 Interleukin-1 receptor-associated kinase 4 Human genes 0.000 description 1
- 101710199010 Interleukin-1 receptor-associated kinase 4 Proteins 0.000 description 1
- 102000003815 Interleukin-11 Human genes 0.000 description 1
- 108090000177 Interleukin-11 Proteins 0.000 description 1
- 108090000176 Interleukin-13 Proteins 0.000 description 1
- 102000003816 Interleukin-13 Human genes 0.000 description 1
- 102000013691 Interleukin-17 Human genes 0.000 description 1
- 108050003558 Interleukin-17 Proteins 0.000 description 1
- 108010002350 Interleukin-2 Proteins 0.000 description 1
- 206010022678 Intestinal infections Diseases 0.000 description 1
- 206010023230 Joint stiffness Diseases 0.000 description 1
- 208000003947 Knee Osteoarthritis Diseases 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- 108010092694 L-Selectin Proteins 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- 102000016551 L-selectin Human genes 0.000 description 1
- 102000007547 Laminin Human genes 0.000 description 1
- 108010085895 Laminin Proteins 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- GSDSWSVVBLHKDQ-JTQLQIEISA-N Levofloxacin Chemical compound C([C@@H](N1C2=C(C(C(C(O)=O)=C1)=O)C=C1F)C)OC2=C1N1CCN(C)CC1 GSDSWSVVBLHKDQ-JTQLQIEISA-N 0.000 description 1
- 102100029204 Low affinity immunoglobulin gamma Fc region receptor II-a Human genes 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 102000055008 Matrilin Proteins Human genes 0.000 description 1
- 108010072582 Matrilin Proteins Proteins 0.000 description 1
- 102000000380 Matrix Metalloproteinase 1 Human genes 0.000 description 1
- 108010016113 Matrix Metalloproteinase 1 Proteins 0.000 description 1
- 102100030412 Matrix metalloproteinase-9 Human genes 0.000 description 1
- 108010015302 Matrix metalloproteinase-9 Proteins 0.000 description 1
- SBDNJUWAMKYJOX-UHFFFAOYSA-N Meclofenamic Acid Chemical compound CC1=CC=C(Cl)C(NC=2C(=CC=CC=2)C(O)=O)=C1Cl SBDNJUWAMKYJOX-UHFFFAOYSA-N 0.000 description 1
- ZRVUJXDFFKFLMG-UHFFFAOYSA-N Meloxicam Chemical compound OC=1C2=CC=CC=C2S(=O)(=O)N(C)C=1C(=O)NC1=NC=C(C)S1 ZRVUJXDFFKFLMG-UHFFFAOYSA-N 0.000 description 1
- 102000005741 Metalloproteases Human genes 0.000 description 1
- 108010006035 Metalloproteases Proteins 0.000 description 1
- QXKHYNVANLEOEG-UHFFFAOYSA-N Methoxsalen Chemical compound C1=CC(=O)OC2=C1C=C1C=COC1=C2OC QXKHYNVANLEOEG-UHFFFAOYSA-N 0.000 description 1
- 108060004795 Methyltransferase Proteins 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 101100481410 Mus musculus Tek gene Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 241000238367 Mya arenaria Species 0.000 description 1
- 208000000112 Myalgia Diseases 0.000 description 1
- 208000031888 Mycoses Diseases 0.000 description 1
- 241001045988 Neogene Species 0.000 description 1
- 102100030411 Neutrophil collagenase Human genes 0.000 description 1
- 101710118230 Neutrophil collagenase Proteins 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- ZCQWOFVYLHDMMC-UHFFFAOYSA-N Oxazole Chemical compound C1=COC=N1 ZCQWOFVYLHDMMC-UHFFFAOYSA-N 0.000 description 1
- 102100037602 P2X purinoceptor 7 Human genes 0.000 description 1
- 101710189965 P2X purinoceptor 7 Proteins 0.000 description 1
- 229930040373 Paraformaldehyde Natural products 0.000 description 1
- 208000030852 Parasitic disease Diseases 0.000 description 1
- 235000019483 Peanut oil Nutrition 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 229920002732 Polyanhydride Polymers 0.000 description 1
- 229920000148 Polycarbophil calcium Polymers 0.000 description 1
- 229920000954 Polyglycolide Polymers 0.000 description 1
- 229920001710 Polyorthoester Polymers 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 108020004518 RNA Probes Proteins 0.000 description 1
- 238000002123 RNA extraction Methods 0.000 description 1
- 239000003391 RNA probe Substances 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 208000033464 Reiter syndrome Diseases 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 206010040047 Sepsis Diseases 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 208000019802 Sexually transmitted disease Diseases 0.000 description 1
- 208000007156 Spondylarthritis Diseases 0.000 description 1
- 208000005718 Stomach Neoplasms Diseases 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 206010052779 Transplant rejections Diseases 0.000 description 1
- 206010066901 Treatment failure Diseases 0.000 description 1
- 101710187743 Tumor necrosis factor receptor superfamily member 1A Proteins 0.000 description 1
- 201000006704 Ulcerative Colitis Diseases 0.000 description 1
- 108091008605 VEGF receptors Proteins 0.000 description 1
- 229940124674 VEGF-R inhibitor Drugs 0.000 description 1
- 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 description 1
- 102000009484 Vascular Endothelial Growth Factor Receptors Human genes 0.000 description 1
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 1
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 229930003316 Vitamin D Natural products 0.000 description 1
- QYSXJUFSXHHAJI-XFEUOLMDSA-N Vitamin D3 Natural products C1(/[C@@H]2CC[C@@H]([C@]2(CCC1)C)[C@H](C)CCCC(C)C)=C/C=C1\C[C@@H](O)CCC1=C QYSXJUFSXHHAJI-XFEUOLMDSA-N 0.000 description 1
- 238000002441 X-ray diffraction Methods 0.000 description 1
- PCWZKQSKUXXDDJ-UHFFFAOYSA-N Xanthotoxin Natural products COCc1c2OC(=O)C=Cc2cc3ccoc13 PCWZKQSKUXXDDJ-UHFFFAOYSA-N 0.000 description 1
- 241000607734 Yersinia <bacteria> Species 0.000 description 1
- 241000212749 Zesius chrysomallus Species 0.000 description 1
- 102000036861 Zinc-dependent endopeptidases Human genes 0.000 description 1
- 108091006982 Zinc-dependent endopeptidases Proteins 0.000 description 1
- OGQICQVSFDPSEI-UHFFFAOYSA-N Zorac Chemical compound N1=CC(C(=O)OCC)=CC=C1C#CC1=CC=C(SCCC2(C)C)C2=C1 OGQICQVSFDPSEI-UHFFFAOYSA-N 0.000 description 1
- HOBWAPHTEJGALG-JKCMADFCSA-N [(1r,5s)-8-methyl-8-azoniabicyclo[3.2.1]octan-3-yl] 3-hydroxy-2-phenylpropanoate;sulfate Chemical compound [O-]S([O-])(=O)=O.C([C@H]1CC[C@@H](C2)[NH+]1C)C2OC(=O)C(CO)C1=CC=CC=C1.C([C@H]1CC[C@@H](C2)[NH+]1C)C2OC(=O)C(CO)C1=CC=CC=C1 HOBWAPHTEJGALG-JKCMADFCSA-N 0.000 description 1
- SXEHKFHPFVVDIR-UHFFFAOYSA-N [4-(4-hydrazinylphenyl)phenyl]hydrazine Chemical compound C1=CC(NN)=CC=C1C1=CC=C(NN)C=C1 SXEHKFHPFVVDIR-UHFFFAOYSA-N 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000003070 absorption delaying agent Substances 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 229960001138 acetylsalicylic acid Drugs 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 229960005339 acitretin Drugs 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 229960002459 alefacept Drugs 0.000 description 1
- JMLGXYWHNOKLBE-HOTXNYTESA-A alicaforsen sodium Chemical compound [Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](COP([O-])(=S)O[C@@H]2[C@H](O[C@H](C2)N2C(N=C(N)C=C2)=O)COP([O-])(=S)O[C@@H]2[C@H](O[C@H](C2)N2C3=C(C(NC(N)=N3)=O)N=C2)COP([O-])(=S)O[C@@H]2[C@H](O[C@H](C2)N2C3=NC=NC(N)=C3N=C2)COP([O-])(=S)O[C@@H]2[C@H](O[C@H](C2)N2C3=NC=NC(N)=C3N=C2)COP([O-])(=S)O[C@@H]2[C@H](O[C@H](C2)N2C(N=C(N)C=C2)=O)COP([O-])(=S)O[C@@H]2[C@H](O[C@H](C2)N2C(N=C(N)C=C2)=O)COP([O-])(=S)O[C@@H]2[C@H](O[C@H](C2)N2C(N=C(N)C=C2)=O)COP([O-])(=S)O[C@@H]2[C@H](O[C@H](C2)N2C3=C(C(NC(N)=N3)=O)N=C2)CO)[C@@H](OP([O-])(=S)OC[C@@H]2[C@H](C[C@@H](O2)N2C3=C(C(NC(N)=N3)=O)N=C2)OP([O-])(=S)OC[C@@H]2[C@H](C[C@@H](O2)N2C3=C(C(NC(N)=N3)=O)N=C2)OP([O-])(=S)OC[C@@H]2[C@H](C[C@@H](O2)N2C(N=C(N)C=C2)=O)OP([O-])(=S)OC[C@@H]2[C@H](C[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)OP([O-])(=S)OC[C@@H]2[C@H](C[C@@H](O2)N2C(NC(=O)C(C)=C2)=O)OP([O-])(=S)OC[C@@H]2[C@H](C[C@@H](O2)N2C(N=C(N)C=C2)=O)OP([O-])(=S)OC[C@@H]2[C@H](C[C@@H](O2)N2C(N=C(N)C=C2)=O)OP([O-])(=S)OC[C@@H]2[C@H](C[C@@H](O2)N2C3=C(C(NC(N)=N3)=O)N=C2)OP([O-])(=S)OC[C@@H]2[C@H](C[C@@H](O2)N2C(NC(=O)C(C)=C2)=O)OP([O-])(=S)OC[C@@H]2[C@H](C[C@@H](O2)N2C(N=C(N)C=C2)=O)OP([O-])(=S)OC[C@@H]2[C@H](C[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)C1 JMLGXYWHNOKLBE-HOTXNYTESA-A 0.000 description 1
- 238000005804 alkylation reaction Methods 0.000 description 1
- IHUNBGSDBOWDMA-AQFIFDHZSA-N all-trans-acitretin Chemical compound COC1=CC(C)=C(\C=C\C(\C)=C\C=C\C(\C)=C\C(O)=O)C(C)=C1C IHUNBGSDBOWDMA-AQFIFDHZSA-N 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 229960004238 anakinra Drugs 0.000 description 1
- 230000033115 angiogenesis Effects 0.000 description 1
- 239000004037 angiogenesis inhibitor Substances 0.000 description 1
- 229940121369 angiogenesis inhibitor Drugs 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 239000005557 antagonist Substances 0.000 description 1
- NUZWLKWWNNJHPT-UHFFFAOYSA-N anthralin Chemical compound C1C2=CC=CC(O)=C2C(=O)C2=C1C=CC=C2O NUZWLKWWNNJHPT-UHFFFAOYSA-N 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000003092 anti-cytokine Effects 0.000 description 1
- 239000002260 anti-inflammatory agent Substances 0.000 description 1
- 230000001494 anti-thymocyte effect Effects 0.000 description 1
- 230000009830 antibody antigen interaction Effects 0.000 description 1
- 239000003429 antifungal agent Substances 0.000 description 1
- 229940121375 antifungal agent Drugs 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000003443 antiviral agent Substances 0.000 description 1
- 239000002249 anxiolytic agent Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 229960002028 atropine sulfate Drugs 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- AUJRCFUBUPVWSZ-XTZHGVARSA-M auranofin Chemical compound CCP(CC)(CC)=[Au]S[C@@H]1O[C@H](COC(C)=O)[C@@H](OC(C)=O)[C@H](OC(C)=O)[C@H]1OC(C)=O AUJRCFUBUPVWSZ-XTZHGVARSA-M 0.000 description 1
- 229960005207 auranofin Drugs 0.000 description 1
- 230000002886 autophagic effect Effects 0.000 description 1
- QQOBRRFOVWGIMD-OJAKKHQRSA-N azaribine Chemical compound CC(=O)O[C@@H]1[C@H](OC(C)=O)[C@@H](COC(=O)C)O[C@H]1N1C(=O)NC(=O)C=N1 QQOBRRFOVWGIMD-OJAKKHQRSA-N 0.000 description 1
- 229950010054 azaribine Drugs 0.000 description 1
- 229960004099 azithromycin Drugs 0.000 description 1
- MQTOSJVFKKJCRP-BICOPXKESA-N azithromycin Chemical compound O([C@@H]1[C@@H](C)C(=O)O[C@@H]([C@@]([C@H](O)[C@@H](C)N(C)C[C@H](C)C[C@@](C)(O)[C@H](O[C@H]2[C@@H]([C@H](C[C@@H](C)O2)N(C)C)O)[C@H]1C)(C)O)CC)[C@H]1C[C@@](C)(OC)[C@@H](O)[C@H](C)O1 MQTOSJVFKKJCRP-BICOPXKESA-N 0.000 description 1
- 208000022362 bacterial infectious disease Diseases 0.000 description 1
- 229960000560 balsalazide disodium Drugs 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 229960002537 betamethasone Drugs 0.000 description 1
- UREBDLICKHMUKA-DVTGEIKXSA-N betamethasone Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@]2(F)[C@@H]1[C@@H]1C[C@H](C)[C@@](C(=O)CO)(O)[C@@]1(C)C[C@@H]2O UREBDLICKHMUKA-DVTGEIKXSA-N 0.000 description 1
- 229960001102 betamethasone dipropionate Drugs 0.000 description 1
- CIWBQSYVNNPZIQ-XYWKZLDCSA-N betamethasone dipropionate Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@]2(F)[C@@H]1[C@@H]1C[C@H](C)[C@@](C(=O)COC(=O)CC)(OC(=O)CC)[C@@]1(C)C[C@@H]2O CIWBQSYVNNPZIQ-XYWKZLDCSA-N 0.000 description 1
- 229960004311 betamethasone valerate Drugs 0.000 description 1
- SNHRLVCMMWUAJD-SUYDQAKGSA-N betamethasone valerate Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@]2(F)[C@@H]1[C@@H]1C[C@H](C)[C@@](C(=O)CO)(OC(=O)CCCC)[C@@]1(C)C[C@@H]2O SNHRLVCMMWUAJD-SUYDQAKGSA-N 0.000 description 1
- 229940087430 biaxin Drugs 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 238000010256 biochemical assay Methods 0.000 description 1
- 229920000249 biocompatible polymer Polymers 0.000 description 1
- 238000006065 biodegradation reaction Methods 0.000 description 1
- 230000008436 biogenesis Effects 0.000 description 1
- 239000003124 biologic agent Substances 0.000 description 1
- 239000012472 biological sample Substances 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- 239000012503 blood component Substances 0.000 description 1
- 238000009534 blood test Methods 0.000 description 1
- 230000008416 bone turnover Effects 0.000 description 1
- 239000006189 buccal tablet Substances 0.000 description 1
- 229960004436 budesonide Drugs 0.000 description 1
- DQXBYHZEEUGOBF-UHFFFAOYSA-N but-3-enoic acid;ethene Chemical compound C=C.OC(=O)CC=C DQXBYHZEEUGOBF-UHFFFAOYSA-N 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 229960002882 calcipotriol Drugs 0.000 description 1
- LWQQLNNNIPYSNX-UROSTWAQSA-N calcipotriol Chemical compound C1([C@H](O)/C=C/[C@@H](C)[C@@H]2[C@]3(CCCC(/[C@@H]3CC2)=C\C=C\2C([C@@H](O)C[C@H](O)C/2)=C)C)CC1 LWQQLNNNIPYSNX-UROSTWAQSA-N 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 238000005251 capillar electrophoresis Methods 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 239000004359 castor oil Substances 0.000 description 1
- 235000019438 castor oil Nutrition 0.000 description 1
- 229960000590 celecoxib Drugs 0.000 description 1
- RZEKVGVHFLEQIL-UHFFFAOYSA-N celecoxib Chemical compound C1=CC(C)=CC=C1C1=CC(C(F)(F)F)=NN1C1=CC=C(S(N)(=O)=O)C=C1 RZEKVGVHFLEQIL-UHFFFAOYSA-N 0.000 description 1
- 210000003850 cellular structure Anatomy 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 229960003115 certolizumab pegol Drugs 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- CKMOQBVBEGCJGW-UHFFFAOYSA-L chembl1200760 Chemical compound [Na+].[Na+].C1=C(C([O-])=O)C(O)=CC=C1N=NC1=CC=C(C(=O)NCCC([O-])=O)C=C1 CKMOQBVBEGCJGW-UHFFFAOYSA-L 0.000 description 1
- 239000013043 chemical agent Substances 0.000 description 1
- 238000012412 chemical coupling Methods 0.000 description 1
- 238000010382 chemical cross-linking Methods 0.000 description 1
- 229960004630 chlorambucil Drugs 0.000 description 1
- JCKYGMPEJWAADB-UHFFFAOYSA-N chlorambucil Chemical compound OC(=O)CCCC1=CC=C(N(CCCl)CCCl)C=C1 JCKYGMPEJWAADB-UHFFFAOYSA-N 0.000 description 1
- 229960003677 chloroquine Drugs 0.000 description 1
- WHTVZRBIWZFKQO-UHFFFAOYSA-N chloroquine Natural products ClC1=CC=C2C(NC(C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-UHFFFAOYSA-N 0.000 description 1
- 210000001612 chondrocyte Anatomy 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000003593 chromogenic compound Substances 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 208000037976 chronic inflammation Diseases 0.000 description 1
- 208000037893 chronic inflammatory disorder Diseases 0.000 description 1
- 229960001265 ciclosporin Drugs 0.000 description 1
- 229940088516 cipro Drugs 0.000 description 1
- DIOIOSKKIYDRIQ-UHFFFAOYSA-N ciprofloxacin hydrochloride Chemical compound Cl.C12=CC(N3CCNCC3)=C(F)C=C2C(=O)C(C(=O)O)=CN1C1CC1 DIOIOSKKIYDRIQ-UHFFFAOYSA-N 0.000 description 1
- 229960001229 ciprofloxacin hydrochloride Drugs 0.000 description 1
- 229960002436 cladribine Drugs 0.000 description 1
- 229960002626 clarithromycin Drugs 0.000 description 1
- 229960004703 clobetasol propionate Drugs 0.000 description 1
- CBGUOGMQLZIXBE-XGQKBEPLSA-N clobetasol propionate Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@]2(F)[C@@H]1[C@@H]1C[C@H](C)[C@@](C(=O)CCl)(OC(=O)CC)[C@@]1(C)C[C@@H]2O CBGUOGMQLZIXBE-XGQKBEPLSA-N 0.000 description 1
- 229960001357 clocortolone pivalate Drugs 0.000 description 1
- SXYZQZLHAIHKKY-GSTUPEFVSA-N clocortolone pivalate Chemical compound C1([C@@H](F)C2)=CC(=O)C=C[C@]1(C)[C@]1(Cl)[C@@H]2[C@@H]2C[C@@H](C)[C@H](C(=O)COC(=O)C(C)(C)C)[C@@]2(C)C[C@@H]1O SXYZQZLHAIHKKY-GSTUPEFVSA-N 0.000 description 1
- 239000003245 coal Substances 0.000 description 1
- 239000011280 coal tar Substances 0.000 description 1
- 229940053219 coal tar / salicylic acid Drugs 0.000 description 1
- 229940062807 coal tar / salicylic acid / sulfur Drugs 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 229960004415 codeine phosphate Drugs 0.000 description 1
- 238000010835 comparative analysis Methods 0.000 description 1
- 102000006834 complement receptors Human genes 0.000 description 1
- 108010047295 complement receptors Proteins 0.000 description 1
- 238000002591 computed tomography Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 238000010219 correlation analysis Methods 0.000 description 1
- 230000001054 cortical effect Effects 0.000 description 1
- FZCHYNWYXKICIO-FZNHGJLXSA-N cortisol 17-valerate Chemical compound C1CC2=CC(=O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@@](C(=O)CO)(OC(=O)CCCC)[C@@]1(C)C[C@@H]2O FZCHYNWYXKICIO-FZNHGJLXSA-N 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 229940111134 coxibs Drugs 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 229960002104 cyanocobalamin Drugs 0.000 description 1
- 235000000639 cyanocobalamin Nutrition 0.000 description 1
- 239000011666 cyanocobalamin Substances 0.000 description 1
- 125000004956 cyclohexylene group Chemical group 0.000 description 1
- FNIATMYXUPOJRW-UHFFFAOYSA-N cyclohexylidene Chemical class [C]1CCCCC1 FNIATMYXUPOJRW-UHFFFAOYSA-N 0.000 description 1
- 239000003255 cyclooxygenase 2 inhibitor Substances 0.000 description 1
- 229960004397 cyclophosphamide Drugs 0.000 description 1
- 229930182912 cyclosporin Natural products 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 230000000093 cytochemical effect Effects 0.000 description 1
- 229940127089 cytotoxic agent Drugs 0.000 description 1
- 239000002254 cytotoxic agent Substances 0.000 description 1
- 231100000599 cytotoxic agent Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000003412 degenerative effect Effects 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- 238000000326 densiometry Methods 0.000 description 1
- 229960003662 desonide Drugs 0.000 description 1
- WBGKWQHBNHJJPZ-LECWWXJVSA-N desonide Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@@H]2[C@@H]1[C@@H]1C[C@H]3OC(C)(C)O[C@@]3(C(=O)CO)[C@@]1(C)C[C@@H]2O WBGKWQHBNHJJPZ-LECWWXJVSA-N 0.000 description 1
- 229960002593 desoximetasone Drugs 0.000 description 1
- VWVSBHGCDBMOOT-IIEHVVJPSA-N desoximetasone Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@]2(F)[C@@H]1[C@@H]1C[C@@H](C)[C@H](C(=O)CO)[C@@]1(C)C[C@@H]2O VWVSBHGCDBMOOT-IIEHVVJPSA-N 0.000 description 1
- 230000006866 deterioration Effects 0.000 description 1
- 229960004193 dextropropoxyphene Drugs 0.000 description 1
- XLMALTXPSGQGBX-GCJKJVERSA-N dextropropoxyphene Chemical compound C([C@](OC(=O)CC)([C@H](C)CN(C)C)C=1C=CC=CC=1)C1=CC=CC=C1 XLMALTXPSGQGBX-GCJKJVERSA-N 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 229960003529 diazepam Drugs 0.000 description 1
- AAOVKJBEBIDNHE-UHFFFAOYSA-N diazepam Chemical compound N=1CC(=O)N(C)C2=CC=C(Cl)C=C2C=1C1=CC=CC=C1 AAOVKJBEBIDNHE-UHFFFAOYSA-N 0.000 description 1
- KPHWPUGNDIVLNH-UHFFFAOYSA-M diclofenac sodium Chemical compound [Na+].[O-]C(=O)CC1=CC=CC=C1NC1=C(Cl)C=CC=C1Cl KPHWPUGNDIVLNH-UHFFFAOYSA-M 0.000 description 1
- 235000005911 diet Nutrition 0.000 description 1
- 230000037213 diet Effects 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 229960002124 diflorasone diacetate Drugs 0.000 description 1
- BOBLHFUVNSFZPJ-JOYXJVLSSA-N diflorasone diacetate Chemical compound C1([C@@H](F)C2)=CC(=O)C=C[C@]1(C)[C@]1(F)[C@@H]2[C@@H]2C[C@H](C)[C@@](C(=O)COC(C)=O)(OC(C)=O)[C@@]2(C)C[C@@H]1O BOBLHFUVNSFZPJ-JOYXJVLSSA-N 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 150000002009 diols Chemical class 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 230000005750 disease progression Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 229960002311 dithranol Drugs 0.000 description 1
- 238000012377 drug delivery Methods 0.000 description 1
- 208000001848 dysentery Diseases 0.000 description 1
- 229960000284 efalizumab Drugs 0.000 description 1
- 235000013601 eggs Nutrition 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 229940073621 enbrel Drugs 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 229940066758 endopeptidases Drugs 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 239000005038 ethylene vinyl acetate Substances 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000005713 exacerbation Effects 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 229940063190 flagyl Drugs 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 229960004511 fludroxycortide Drugs 0.000 description 1
- 229960004369 flufenamic acid Drugs 0.000 description 1
- LPEPZBJOKDYZAD-UHFFFAOYSA-N flufenamic acid Chemical compound OC(=O)C1=CC=CC=C1NC1=CC=CC(C(F)(F)F)=C1 LPEPZBJOKDYZAD-UHFFFAOYSA-N 0.000 description 1
- 229960000785 fluocinonide Drugs 0.000 description 1
- 229960002714 fluticasone Drugs 0.000 description 1
- MGNNYOODZCAHBA-GQKYHHCASA-N fluticasone Chemical compound C1([C@@H](F)C2)=CC(=O)C=C[C@]1(C)[C@]1(F)[C@@H]2[C@@H]2C[C@@H](C)[C@@](C(=O)SCF)(O)[C@@]2(C)C[C@@H]1O MGNNYOODZCAHBA-GQKYHHCASA-N 0.000 description 1
- 229960000289 fluticasone propionate Drugs 0.000 description 1
- WMWTYOKRWGGJOA-CENSZEJFSA-N fluticasone propionate Chemical compound C1([C@@H](F)C2)=CC(=O)C=C[C@]1(C)[C@]1(F)[C@@H]2[C@@H]2C[C@@H](C)[C@@](C(=O)SCF)(OC(=O)CC)[C@@]2(C)C[C@@H]1O WMWTYOKRWGGJOA-CENSZEJFSA-N 0.000 description 1
- 229940014144 folate Drugs 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 206010017758 gastric cancer Diseases 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 239000007903 gelatin capsule Substances 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 230000000762 glandular Effects 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 1
- ZEMPKEQAKRGZGQ-XOQCFJPHSA-N glycerol triricinoleate Natural products CCCCCC[C@@H](O)CC=CCCCCCCCC(=O)OC[C@@H](COC(=O)CCCCCCCC=CC[C@@H](O)CCCCCC)OC(=O)CCCCCCCC=CC[C@H](O)CCCCCC ZEMPKEQAKRGZGQ-XOQCFJPHSA-N 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 239000010931 gold Substances 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- 208000024908 graft versus host disease Diseases 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- ZRALSGWEFCBTJO-UHFFFAOYSA-O guanidinium Chemical compound NC(N)=[NH2+] ZRALSGWEFCBTJO-UHFFFAOYSA-O 0.000 description 1
- 230000009931 harmful effect Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229960002764 hydrocodone bitartrate Drugs 0.000 description 1
- 229960000631 hydrocortisone valerate Drugs 0.000 description 1
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 description 1
- 229960001550 hyoscyamine sulfate Drugs 0.000 description 1
- 229960001680 ibuprofen Drugs 0.000 description 1
- HIFJCPQKFCZDDL-ACWOEMLNSA-N iloprost Chemical compound C1\C(=C/CCCC(O)=O)C[C@@H]2[C@@H](/C=C/[C@@H](O)C(C)CC#CC)[C@H](O)C[C@@H]21 HIFJCPQKFCZDDL-ACWOEMLNSA-N 0.000 description 1
- 229960002240 iloprost Drugs 0.000 description 1
- 238000003365 immunocytochemistry Methods 0.000 description 1
- 230000000951 immunodiffusion Effects 0.000 description 1
- 238000000760 immunoelectrophoresis Methods 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 238000002991 immunohistochemical analysis Methods 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 238000010324 immunological assay Methods 0.000 description 1
- 239000002955 immunomodulating agent Substances 0.000 description 1
- 229940121354 immunomodulator Drugs 0.000 description 1
- 230000002584 immunomodulator Effects 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 239000003547 immunosorbent Substances 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 238000005462 in vivo assay Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 229940089536 indocin Drugs 0.000 description 1
- 239000003701 inert diluent Substances 0.000 description 1
- 230000004968 inflammatory condition Effects 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 229940102223 injectable solution Drugs 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 230000015788 innate immune response Effects 0.000 description 1
- 229960003130 interferon gamma Drugs 0.000 description 1
- 229940074383 interleukin-11 Drugs 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- SZVJSHCCFOBDDC-UHFFFAOYSA-N iron(II,III) oxide Inorganic materials O=[Fe]O[Fe]O[Fe]=O SZVJSHCCFOBDDC-UHFFFAOYSA-N 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 230000007794 irritation Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 238000011901 isothermal amplification Methods 0.000 description 1
- 150000002540 isothiocyanates Chemical class 0.000 description 1
- 230000000155 isotopic effect Effects 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 230000009916 joint effect Effects 0.000 description 1
- 208000018937 joint inflammation Diseases 0.000 description 1
- 229960004125 ketoconazole Drugs 0.000 description 1
- 229940054136 kineret Drugs 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 229960000681 leflunomide Drugs 0.000 description 1
- VHOGYURTWQBHIL-UHFFFAOYSA-N leflunomide Chemical compound O1N=CC(C(=O)NC=2C=CC(=CC=2)C(F)(F)F)=C1C VHOGYURTWQBHIL-UHFFFAOYSA-N 0.000 description 1
- 229960003376 levofloxacin Drugs 0.000 description 1
- 238000007834 ligase chain reaction Methods 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000008297 liquid dosage form Substances 0.000 description 1
- 239000006193 liquid solution Substances 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 229960002983 loperamide hydrochloride Drugs 0.000 description 1
- PGYPOBZJRVSMDS-UHFFFAOYSA-N loperamide hydrochloride Chemical compound Cl.C=1C=CC=CC=1C(C=1C=CC=CC=1)(C(=O)N(C)C)CCN(CC1)CCC1(O)C1=CC=C(Cl)C=C1 PGYPOBZJRVSMDS-UHFFFAOYSA-N 0.000 description 1
- 230000001926 lymphatic effect Effects 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 108010026228 mRNA guanylyltransferase Proteins 0.000 description 1
- 238000002595 magnetic resonance imaging Methods 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 238000001840 matrix-assisted laser desorption--ionisation time-of-flight mass spectrometry Methods 0.000 description 1
- 229960003803 meclofenamic acid Drugs 0.000 description 1
- 229960001929 meloxicam Drugs 0.000 description 1
- 229940051129 meperidine hydrochloride Drugs 0.000 description 1
- KBOPZPXVLCULAV-UHFFFAOYSA-N mesalamine Chemical compound NC1=CC=C(O)C(C(O)=O)=C1 KBOPZPXVLCULAV-UHFFFAOYSA-N 0.000 description 1
- 229960004963 mesalazine Drugs 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 229960004469 methoxsalen Drugs 0.000 description 1
- 229960004584 methylprednisolone Drugs 0.000 description 1
- 229960001293 methylprednisolone acetate Drugs 0.000 description 1
- PLBHSZGDDKCEHR-LFYFAGGJSA-N methylprednisolone acetate Chemical compound C([C@@]12C)=CC(=O)C=C1[C@@H](C)C[C@@H]1[C@@H]2[C@@H](O)C[C@]2(C)[C@@](O)(C(=O)COC(C)=O)CC[C@H]21 PLBHSZGDDKCEHR-LFYFAGGJSA-N 0.000 description 1
- 229960000334 methylprednisolone sodium succinate Drugs 0.000 description 1
- HPNSFSBZBAHARI-UHFFFAOYSA-N micophenolic acid Natural products OC1=C(CC=C(C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-UHFFFAOYSA-N 0.000 description 1
- 239000004530 micro-emulsion Substances 0.000 description 1
- 238000010208 microarray analysis Methods 0.000 description 1
- 239000011859 microparticle Substances 0.000 description 1
- 239000004005 microsphere Substances 0.000 description 1
- 229960002853 midazolam hydrochloride Drugs 0.000 description 1
- PLYSCVSCYOQVRP-UHFFFAOYSA-N midazolam hydrochloride Chemical compound Cl.C12=CC(Cl)=CC=C2N2C(C)=NC=C2CN=C1C1=CC=CC=C1F PLYSCVSCYOQVRP-UHFFFAOYSA-N 0.000 description 1
- DYKFCLLONBREIL-KVUCHLLUSA-N minocycline Chemical compound C([C@H]1C2)C3=C(N(C)C)C=CC(O)=C3C(=O)C1=C(O)[C@@]1(O)[C@@H]2[C@H](N(C)C)C(O)=C(C(N)=O)C1=O DYKFCLLONBREIL-KVUCHLLUSA-N 0.000 description 1
- 229960004023 minocycline Drugs 0.000 description 1
- ZAHQPTJLOCWVPG-UHFFFAOYSA-N mitoxantrone dihydrochloride Chemical compound Cl.Cl.O=C1C2=C(O)C=CC(O)=C2C(=O)C2=C1C(NCCNCCO)=CC=C2NCCNCCO ZAHQPTJLOCWVPG-UHFFFAOYSA-N 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000003020 moisturizing effect Effects 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 229960002744 mometasone furoate Drugs 0.000 description 1
- WOFMFGQZHJDGCX-ZULDAHANSA-N mometasone furoate Chemical compound O([C@]1([C@@]2(C)C[C@H](O)[C@]3(Cl)[C@@]4(C)C=CC(=O)C=C4CC[C@H]3[C@@H]2C[C@H]1C)C(=O)CCl)C(=O)C1=CC=CO1 WOFMFGQZHJDGCX-ZULDAHANSA-N 0.000 description 1
- 230000009854 mucosal lesion Effects 0.000 description 1
- 229960000951 mycophenolic acid Drugs 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 229940090008 naprosyn Drugs 0.000 description 1
- 229960005027 natalizumab Drugs 0.000 description 1
- 101150091879 neo gene Proteins 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 238000007899 nucleic acid hybridization Methods 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- KQYWQOXTZUHYEF-UHFFFAOYSA-N octanedioic acid;pyrrolidine-2,5-dione Chemical compound O=C1CCC(=O)N1.O=C1CCC(=O)N1.OC(=O)CCCCCCC(O)=O KQYWQOXTZUHYEF-UHFFFAOYSA-N 0.000 description 1
- 229940046166 oligodeoxynucleotide Drugs 0.000 description 1
- 229960000381 omeprazole Drugs 0.000 description 1
- 230000014207 opsonization Effects 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 229960004534 orgotein Drugs 0.000 description 1
- 108010070915 orgotein Proteins 0.000 description 1
- MUZQPDBAOYKNLO-RKXJKUSZSA-N oxycodone hydrochloride Chemical compound [H+].[Cl-].O=C([C@@H]1O2)CC[C@@]3(O)[C@H]4CC5=CC=C(OC)C2=C5[C@@]13CCN4C MUZQPDBAOYKNLO-RKXJKUSZSA-N 0.000 description 1
- 229960005489 paracetamol Drugs 0.000 description 1
- 239000012188 paraffin wax Substances 0.000 description 1
- 230000003071 parasitic effect Effects 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 239000000312 peanut oil Substances 0.000 description 1
- 210000004197 pelvis Anatomy 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 239000003208 petroleum Substances 0.000 description 1
- 230000008782 phagocytosis Effects 0.000 description 1
- 239000008177 pharmaceutical agent Substances 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 229960002895 phenylbutazone Drugs 0.000 description 1
- VYMDGNCVAMGZFE-UHFFFAOYSA-N phenylbutazonum Chemical compound O=C1C(CCCC)C(=O)N(C=2C=CC=CC=2)N1C1=CC=CC=C1 VYMDGNCVAMGZFE-UHFFFAOYSA-N 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- 239000002587 phosphodiesterase IV inhibitor Substances 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 238000001126 phototherapy Methods 0.000 description 1
- 230000035479 physiological effects, processes and functions Effects 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 229960002702 piroxicam Drugs 0.000 description 1
- QYSPLQLAKJAUJT-UHFFFAOYSA-N piroxicam Chemical compound OC=1C2=CC=CC=C2S(=O)(=O)N(C)C=1C(=O)NC1=CC=CC=N1 QYSPLQLAKJAUJT-UHFFFAOYSA-N 0.000 description 1
- 230000033885 plasminogen activation Effects 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920001200 poly(ethylene-vinyl acetate) Polymers 0.000 description 1
- 229920000747 poly(lactic acid) Polymers 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229950005134 polycarbophil Drugs 0.000 description 1
- 239000004633 polyglycolic acid Substances 0.000 description 1
- 229920002704 polyhistidine Polymers 0.000 description 1
- 239000004626 polylactic acid Substances 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 229920006324 polyoxymethylene Polymers 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 231100000683 possible toxicity Toxicity 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- DQKXQSGTHWVTAD-UHFFFAOYSA-N pramocaine Chemical compound C1=CC(OCCCC)=CC=C1OCCCN1CCOCC1 DQKXQSGTHWVTAD-UHFFFAOYSA-N 0.000 description 1
- 229960001896 pramocaine Drugs 0.000 description 1
- 229940071643 prefilled syringe Drugs 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000000750 progressive effect Effects 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000009465 prokaryotic expression Effects 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- XXPDBLUZJRXNNZ-UHFFFAOYSA-N promethazine hydrochloride Chemical compound Cl.C1=CC=C2N(CC(C)N(C)C)C3=CC=CC=C3SC2=C1 XXPDBLUZJRXNNZ-UHFFFAOYSA-N 0.000 description 1
- 229960002244 promethazine hydrochloride Drugs 0.000 description 1
- QQONPFPTGQHPMA-UHFFFAOYSA-N propylene Natural products CC=C QQONPFPTGQHPMA-UHFFFAOYSA-N 0.000 description 1
- 125000004805 propylene group Chemical group [H]C([H])([H])C([H])([*:1])C([H])([H])[*:2] 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 238000012113 quantitative test Methods 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000002601 radiography Methods 0.000 description 1
- 238000001959 radiotherapy Methods 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 238000007634 remodeling Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 150000004492 retinoid derivatives Chemical class 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 230000000552 rheumatic effect Effects 0.000 description 1
- 201000003068 rheumatic fever Diseases 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 229920002477 rna polymer Polymers 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 229960002530 sargramostim Drugs 0.000 description 1
- 108010038379 sargramostim Proteins 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 239000008299 semisolid dosage form Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 230000000405 serological effect Effects 0.000 description 1
- 230000001568 sexual effect Effects 0.000 description 1
- 239000002453 shampoo Substances 0.000 description 1
- 201000009890 sinusitis Diseases 0.000 description 1
- 239000000344 soap Substances 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 229960003339 sodium phosphate Drugs 0.000 description 1
- 239000007909 solid dosage form Substances 0.000 description 1
- 230000000392 somatic effect Effects 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 230000003637 steroidlike Effects 0.000 description 1
- 201000011549 stomach cancer Diseases 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 210000005065 subchondral bone plate Anatomy 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 229960005404 sulfamethoxazole Drugs 0.000 description 1
- MLKXDPUZXIRXEP-MFOYZWKCSA-N sulindac Chemical compound CC1=C(CC(O)=O)C2=CC(F)=CC=C2\C1=C/C1=CC=C(S(C)=O)C=C1 MLKXDPUZXIRXEP-MFOYZWKCSA-N 0.000 description 1
- JLKIGFTWXXRPMT-UHFFFAOYSA-N sulphamethoxazole Chemical compound O1C(C)=CC(NS(=O)(=O)C=2C=CC(N)=CC=2)=N1 JLKIGFTWXXRPMT-UHFFFAOYSA-N 0.000 description 1
- 229910021653 sulphate ion Inorganic materials 0.000 description 1
- 230000000475 sunscreen effect Effects 0.000 description 1
- 239000000516 sunscreening agent Substances 0.000 description 1
- 239000000829 suppository Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 230000002459 sustained effect Effects 0.000 description 1
- 238000013268 sustained release Methods 0.000 description 1
- 210000004243 sweat Anatomy 0.000 description 1
- 230000000946 synaptic effect Effects 0.000 description 1
- 230000008409 synovial inflammation Effects 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 229960001967 tacrolimus Drugs 0.000 description 1
- QJJXYPPXXYFBGM-SHYZHZOCSA-N tacrolimus Natural products CO[C@H]1C[C@H](CC[C@@H]1O)C=C(C)[C@H]2OC(=O)[C@H]3CCCCN3C(=O)C(=O)[C@@]4(O)O[C@@H]([C@H](C[C@H]4C)OC)[C@@H](C[C@H](C)CC(=C[C@@H](CC=C)C(=O)C[C@H](O)[C@H]2C)C)OC QJJXYPPXXYFBGM-SHYZHZOCSA-N 0.000 description 1
- 239000011269 tar Substances 0.000 description 1
- 229960000565 tazarotene Drugs 0.000 description 1
- 210000002435 tendon Anatomy 0.000 description 1
- LXIKEPCNDFVJKC-QXMHVHEDSA-N tenidap Chemical compound C12=CC(Cl)=CC=C2N(C(=O)N)C(=O)\C1=C(/O)C1=CC=CS1 LXIKEPCNDFVJKC-QXMHVHEDSA-N 0.000 description 1
- 229960003676 tenidap Drugs 0.000 description 1
- TUGDLVFMIQZYPA-UHFFFAOYSA-N tetracopper;tetrazinc Chemical compound [Cu+2].[Cu+2].[Cu+2].[Cu+2].[Zn+2].[Zn+2].[Zn+2].[Zn+2] TUGDLVFMIQZYPA-UHFFFAOYSA-N 0.000 description 1
- 229960004989 tetracycline hydrochloride Drugs 0.000 description 1
- 229960003433 thalidomide Drugs 0.000 description 1
- RYYWUUFWQRZTIU-UHFFFAOYSA-K thiophosphate Chemical compound [O-]P([O-])([O-])=S RYYWUUFWQRZTIU-UHFFFAOYSA-K 0.000 description 1
- 210000002303 tibia Anatomy 0.000 description 1
- 229960001017 tolmetin Drugs 0.000 description 1
- 229940125379 topical corticosteroid Drugs 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- GYDJEQRTZSCIOI-LJGSYFOKSA-N tranexamic acid Chemical compound NC[C@H]1CC[C@H](C(O)=O)CC1 GYDJEQRTZSCIOI-LJGSYFOKSA-N 0.000 description 1
- 229960000401 tranexamic acid Drugs 0.000 description 1
- 238000011830 transgenic mouse model Methods 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 238000011277 treatment modality Methods 0.000 description 1
- 229960002117 triamcinolone acetonide Drugs 0.000 description 1
- YNDXUCZADRHECN-JNQJZLCISA-N triamcinolone acetonide Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@]2(F)[C@@H]1[C@@H]1C[C@H]3OC(C)(C)O[C@@]3(C(=O)CO)[C@@]1(C)C[C@@H]2O YNDXUCZADRHECN-JNQJZLCISA-N 0.000 description 1
- KVSKGMLNBAPGKH-UHFFFAOYSA-N tribromosalicylanilide Chemical compound OC1=C(Br)C=C(Br)C=C1C(=O)NC1=CC=C(Br)C=C1 KVSKGMLNBAPGKH-UHFFFAOYSA-N 0.000 description 1
- 229950001807 tribromsalan Drugs 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- 229960001082 trimethoprim Drugs 0.000 description 1
- IEDVJHCEMCRBQM-UHFFFAOYSA-N trimethoprim Chemical compound COC1=C(OC)C(OC)=CC(CC=2C(=NC(N)=NC=2)N)=C1 IEDVJHCEMCRBQM-UHFFFAOYSA-N 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 229950008396 ulobetasol propionate Drugs 0.000 description 1
- BDSYKGHYMJNPAB-LICBFIPMSA-N ulobetasol propionate Chemical compound C1([C@@H](F)C2)=CC(=O)C=C[C@]1(C)[C@]1(F)[C@@H]2[C@@H]2C[C@H](C)[C@@](C(=O)CCl)(OC(=O)CC)[C@@]2(C)C[C@@H]1O BDSYKGHYMJNPAB-LICBFIPMSA-N 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 229940045136 urea Drugs 0.000 description 1
- 208000000143 urethritis Diseases 0.000 description 1
- 238000001291 vacuum drying Methods 0.000 description 1
- 229940124676 vascular endothelial growth factor receptor Drugs 0.000 description 1
- 239000002525 vasculotropin inhibitor Substances 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 108700026220 vif Genes Proteins 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
- 235000019166 vitamin D Nutrition 0.000 description 1
- 239000011710 vitamin D Substances 0.000 description 1
- 150000003710 vitamin D derivatives Chemical class 0.000 description 1
- 229940046008 vitamin d Drugs 0.000 description 1
- 229940063674 voltaren Drugs 0.000 description 1
- 235000012431 wafers Nutrition 0.000 description 1
- 238000009736 wetting Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
- MWLSOWXNZPKENC-SSDOTTSWSA-N zileuton Chemical compound C1=CC=C2SC([C@H](N(O)C(N)=O)C)=CC2=C1 MWLSOWXNZPKENC-SSDOTTSWSA-N 0.000 description 1
- 229960005332 zileuton Drugs 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12M—APPARATUS FOR ENZYMOLOGY OR MICROBIOLOGY; APPARATUS FOR CULTURING MICROORGANISMS FOR PRODUCING BIOMASS, FOR GROWING CELLS OR FOR OBTAINING FERMENTATION OR METABOLIC PRODUCTS, i.e. BIOREACTORS OR FERMENTERS
- C12M3/00—Tissue, human, animal or plant cell, or virus culture apparatus
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6887—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids from muscle, cartilage or connective tissue
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin, cold insoluble globulin [CIG]
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/10—Musculoskeletal or connective tissue disorders
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/52—Predicting or monitoring the response to treatment, e.g. for selection of therapy based on assay results in personalised medicine; Prognosis
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Biomedical Technology (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- General Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Cell Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Microbiology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Food Science & Technology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Physical Education & Sports Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Virology (AREA)
- Sustainable Development (AREA)
- Veterinary Medicine (AREA)
- Rheumatology (AREA)
- General Engineering & Computer Science (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Biophysics (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US73244405P | 2005-11-01 | 2005-11-01 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| TW201337266A true TW201337266A (zh) | 2013-09-16 |
Family
ID=38327823
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| TW102119988A TW201337266A (zh) | 2005-11-01 | 2006-10-31 | 利用生物標記診斷關節黏連脊椎炎之方法及組合物 |
| TW095140333A TWI424161B (zh) | 2005-11-01 | 2006-10-31 | 利用生物標記診斷關節黏連脊椎炎之方法及組合物 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| TW095140333A TWI424161B (zh) | 2005-11-01 | 2006-10-31 | 利用生物標記診斷關節黏連脊椎炎之方法及組合物 |
Country Status (21)
| Country | Link |
|---|---|
| US (2) | US7919264B2 (enExample) |
| EP (2) | EP1948235B1 (enExample) |
| JP (4) | JP5198277B2 (enExample) |
| KR (2) | KR20140012160A (enExample) |
| CN (2) | CN101663048A (enExample) |
| AU (1) | AU2006337105B2 (enExample) |
| BR (1) | BRPI0618085A2 (enExample) |
| CA (1) | CA2626804A1 (enExample) |
| DK (1) | DK1948235T3 (enExample) |
| ES (1) | ES2431643T3 (enExample) |
| HR (1) | HRP20131112T1 (enExample) |
| IL (2) | IL190964A0 (enExample) |
| NZ (3) | NZ608431A (enExample) |
| PL (1) | PL1948235T3 (enExample) |
| PT (1) | PT1948235E (enExample) |
| RS (1) | RS53055B (enExample) |
| RU (2) | RU2438704C2 (enExample) |
| SG (1) | SG169361A1 (enExample) |
| SI (1) | SI1948235T1 (enExample) |
| TW (2) | TW201337266A (enExample) |
| WO (1) | WO2007089303A2 (enExample) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TWI671761B (zh) * | 2017-05-01 | 2019-09-11 | 臺中榮民總醫院 | 脊椎關節炎患者疾病活動度電子病歷管理系統 |
Families Citing this family (96)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6090382A (en) * | 1996-02-09 | 2000-07-18 | Basf Aktiengesellschaft | Human antibodies that bind human TNFα |
| BRPI9707379B8 (pt) * | 1996-02-09 | 2015-07-07 | Abbvie Biotechnology Ltd | Composições farmacêuticas compreendendo anticorpo humano recombinante geneticamente engenheirado, e anticorpo humano recombinante geneticamente engenheirado. |
| CA2817619A1 (en) | 2001-06-08 | 2002-12-08 | Abbott Laboratories (Bermuda) Ltd. | Methods of administering anti-tnf.alpha. antibodies |
| US20040009172A1 (en) * | 2002-04-26 | 2004-01-15 | Steven Fischkoff | Use of anti-TNFalpha antibodies and another drug |
| US20090280065A1 (en) * | 2006-04-10 | 2009-11-12 | Willian Mary K | Uses and Compositions for Treatment of Psoriasis |
| CA2493067A1 (en) * | 2002-07-19 | 2004-01-29 | Abbott Biotechnology Ltd. | Treatment of tnf.alpha. related disorders |
| US20040033228A1 (en) | 2002-08-16 | 2004-02-19 | Hans-Juergen Krause | Formulation of human antibodies for treating TNF-alpha associated disorders |
| MY150740A (en) * | 2002-10-24 | 2014-02-28 | Abbvie Biotechnology Ltd | Low dose methods for treating disorders in which tnf? activity is detrimental |
| TW201705980A (zh) | 2004-04-09 | 2017-02-16 | 艾伯維生物技術有限責任公司 | 用於治療ＴＮＦα相關失調症之多重可變劑量療法 |
| GB0414054D0 (en) | 2004-06-23 | 2004-07-28 | Owen Mumford Ltd | Improvements relating to automatic injection devices |
| US20060083741A1 (en) * | 2004-10-08 | 2006-04-20 | Hoffman Rebecca S | Treatment of respiratory syncytial virus (RSV) infection |
| JP5757495B2 (ja) | 2005-05-16 | 2015-07-29 | アッヴィ バイオテクノロジー リミテッド | びらん性多発性関節炎の治療のためのｔｎｆ阻害剤の使用 |
| US8874477B2 (en) | 2005-10-04 | 2014-10-28 | Steven Mark Hoffberg | Multifactorial optimization system and method |
| JP5198277B2 (ja) | 2005-11-01 | 2013-05-15 | アボツト・バイオテクノロジー・リミテツド | バイオマーカーを用いて強直性脊椎炎を診断するための方法及び組成物 |
| EP2738179A1 (en) | 2006-04-05 | 2014-06-04 | AbbVie Biotechnology Ltd | Antibody purification |
| US20080118496A1 (en) * | 2006-04-10 | 2008-05-22 | Medich John R | Uses and compositions for treatment of juvenile rheumatoid arthritis |
| US20090317399A1 (en) * | 2006-04-10 | 2009-12-24 | Pollack Paul F | Uses and compositions for treatment of CROHN'S disease |
| US9399061B2 (en) * | 2006-04-10 | 2016-07-26 | Abbvie Biotechnology Ltd | Methods for determining efficacy of TNF-α inhibitors for treatment of rheumatoid arthritis |
| EP2666472A3 (en) | 2006-04-10 | 2014-04-02 | Abbott Biotechnology Ltd | Uses and compositions for treatment of psoriatic arthritis |
| US9605064B2 (en) * | 2006-04-10 | 2017-03-28 | Abbvie Biotechnology Ltd | Methods and compositions for treatment of skin disorders |
| WO2007120626A2 (en) * | 2006-04-10 | 2007-10-25 | Abbott Biotechnology Ltd. | Uses and compositions for treatment of ankylosing spondylitis |
| US20080131374A1 (en) * | 2006-04-19 | 2008-06-05 | Medich John R | Uses and compositions for treatment of rheumatoid arthritis |
| US20080311043A1 (en) * | 2006-06-08 | 2008-12-18 | Hoffman Rebecca S | Uses and compositions for treatment of psoriatic arthritis |
| US20100021451A1 (en) * | 2006-06-08 | 2010-01-28 | Wong Robert L | Uses and compositions for treatment of ankylosing spondylitis |
| TWI542374B (zh) | 2006-06-30 | 2016-07-21 | 艾伯維生物技術有限責任公司 | 自動注射裝置 |
| EP2089428B1 (en) * | 2006-10-27 | 2013-11-20 | AbbVie Biotechnology Ltd | Crystalline anti-htnfalpha antibodies |
| EP2165194A4 (en) * | 2007-05-31 | 2010-09-08 | Abbott Lab | BIOMARKERS FOR PREDICTING RESPONSABILITY TO TNF ALPHA INHIBITORS IN AUTOIMMUNE DISEASES |
| WO2008154543A2 (en) | 2007-06-11 | 2008-12-18 | Abbott Biotechnology Ltd. | Methods for treating juvenile idiopathic arthritis |
| EP2173380A4 (en) * | 2007-07-13 | 2011-08-31 | Abbott Biotech Ltd | METHOD AND COMPOSITIONS FOR PULMONARY ADMINISTRATION OF A TNFa HEMMER |
| MX2010001488A (es) * | 2007-08-08 | 2010-03-01 | Abbott Lab | Composiciones y metodos para cristalizar anticuerpos. |
| CN101802005B (zh) * | 2007-08-28 | 2015-09-16 | 艾伯维生物技术有限公司 | 包括关于阿达木单抗的结合蛋白质的组合物和方法 |
| US9404932B2 (en) * | 2007-11-05 | 2016-08-02 | Nordic Bioscience A/S | Pathology biomarker assay |
| CN101969971A (zh) | 2007-11-30 | 2011-02-09 | 雅培制药有限公司 | 蛋白制剂及其制备方法 |
| US8883146B2 (en) | 2007-11-30 | 2014-11-11 | Abbvie Inc. | Protein formulations and methods of making same |
| US20090271164A1 (en) * | 2008-01-03 | 2009-10-29 | Peng Joanna Z | Predicting long-term efficacy of a compound in the treatment of psoriasis |
| RU2537139C2 (ru) | 2008-01-15 | 2014-12-27 | Эбботт Гмбх Унд Ко.Кг | Порошковые белковые композиции и способы их получения |
| AU2009333489A1 (en) | 2008-12-30 | 2010-07-08 | Centocor Ortho Biotech Inc. | Serum markers predicting clinical response to anti-TNF antibodies in patients with ankylosing spondylitis |
| GB0902737D0 (en) * | 2009-02-19 | 2009-04-01 | Univ Gent | GDF15 as a differential marker for spondyloarthropathy |
| US20100260940A1 (en) * | 2009-04-08 | 2010-10-14 | Mccown James Charles | System and method for depositing metallic coatings on substrates using removable masking materials |
| JP5795759B2 (ja) * | 2009-04-16 | 2015-10-14 | アッヴィ・バイオセラピューティクス・インコーポレイテッド | 抗ＴＮＦ−α抗体およびその用途 |
| RU2524487C2 (ru) | 2009-04-29 | 2014-07-27 | Эббви Байотекнолоджи Лтд | Автоматическое инъекционное устройство |
| CN104490767A (zh) * | 2009-05-04 | 2015-04-08 | 艾伯维生物技术有限公司 | 人抗TNF-α抗体的稳定高蛋白质浓度制剂 |
| AU2010306593B2 (en) | 2009-10-15 | 2015-09-10 | Crescendo Bioscience, Inc. | Biomarkers and methods for measuring and monitoring inflammatory disease activity |
| US9082177B2 (en) * | 2009-11-25 | 2015-07-14 | Dental Imaging Technologies Corporation | Method for tracking X-ray markers in serial CT projection images |
| WO2011075524A1 (en) | 2009-12-15 | 2011-06-23 | Abbott Biotechnology Ltd | Improved firing button for automatic injection device |
| CA2796186C (en) | 2010-04-21 | 2019-04-09 | Abbott Biotechnology Ltd. | Wearable automatic injection device for controlled delivery of therapeutic agents |
| PL2575884T3 (pl) | 2010-06-03 | 2018-12-31 | Abbvie Biotechnology Ltd | Zastosowania i kompozycje do leczenia ropni mnogich pach (HS) |
| US8821865B2 (en) * | 2010-11-11 | 2014-09-02 | Abbvie Biotechnology Ltd. | High concentration anti-TNFα antibody liquid formulations |
| ES2710905T3 (es) | 2011-01-24 | 2019-04-29 | E3D Agricultural Coop Association Ltd | Inyector |
| AU2012209223B2 (en) | 2011-01-24 | 2015-11-05 | Abbvie Biotechnology Ltd | Automatic injection devices having overmolded gripping surfaces |
| JP5968914B2 (ja) | 2011-01-24 | 2016-08-10 | アッヴィ バイオテクノロジー リミテッド | シリンジおよび自動注入デバイスからの針シールドの取り外し |
| EP2702077A2 (en) | 2011-04-27 | 2014-03-05 | AbbVie Inc. | Methods for controlling the galactosylation profile of recombinantly-expressed proteins |
| EP2773773B1 (en) * | 2011-11-04 | 2017-01-11 | Adaptive Biotechnologies Corporation | T-cell receptor clonotypes shared among ankylosing spondylitis patients |
| EP3904536B1 (en) | 2011-12-09 | 2025-10-29 | Adaptive Biotechnologies Corporation | Diagnosis of lymphoid malignancies and minimal residual disease detection |
| US9067990B2 (en) | 2013-03-14 | 2015-06-30 | Abbvie, Inc. | Protein purification using displacement chromatography |
| US9181572B2 (en) | 2012-04-20 | 2015-11-10 | Abbvie, Inc. | Methods to modulate lysine variant distribution |
| US9334319B2 (en) | 2012-04-20 | 2016-05-10 | Abbvie Inc. | Low acidic species compositions |
| WO2013176754A1 (en) | 2012-05-24 | 2013-11-28 | Abbvie Inc. | Novel purification of antibodies using hydrophobic interaction chromatography |
| US20140052020A1 (en) * | 2012-08-15 | 2014-02-20 | University Of Florida Research Foundation, Inc. | Magnetic apparatus and methods of use |
| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| BR112015004467A2 (pt) | 2012-09-02 | 2017-03-21 | Abbvie Inc | método para controlar a heterogeneidade de proteínas |
| EP2830651A4 (en) | 2013-03-12 | 2015-09-02 | Abbvie Inc | HUMAN ANTIBODIES THAT BIND TNF-ALPHA AND PREPARATION METHODS |
| US8921526B2 (en) | 2013-03-14 | 2014-12-30 | Abbvie, Inc. | Mutated anti-TNFα antibodies and methods of their use |
| CA2926301A1 (en) | 2013-03-14 | 2014-10-02 | Abbvie Inc. | Low acidic species compositions and methods for producing and using the same |
| US9017687B1 (en) | 2013-10-18 | 2015-04-28 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same using displacement chromatography |
| WO2014159554A1 (en) | 2013-03-14 | 2014-10-02 | Abbvie Inc. | Low acidic species compositions and methods for producing the same using displacement chromatography |
| US9499614B2 (en) | 2013-03-14 | 2016-11-22 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosaccharides |
| WO2015051293A2 (en) | 2013-10-04 | 2015-04-09 | Abbvie, Inc. | Use of metal ions for modulation of protein glycosylation profiles of recombinant proteins |
| US10376582B2 (en) | 2013-10-16 | 2019-08-13 | Outlook Therapeutics, Inc. | Buffer formulations for enhanced antibody stability |
| US8946395B1 (en) | 2013-10-18 | 2015-02-03 | Abbvie Inc. | Purification of proteins using hydrophobic interaction chromatography |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
| US9181337B2 (en) | 2013-10-18 | 2015-11-10 | Abbvie, Inc. | Modulated lysine variant species compositions and methods for producing and using the same |
| US20150139988A1 (en) | 2013-11-15 | 2015-05-21 | Abbvie, Inc. | Glycoengineered binding protein compositions |
| CA2943821A1 (en) | 2014-04-02 | 2015-10-08 | Crescendo Bioscience | Biomarkers and methods for measuring and monitoring juvenile idiopathic arthritis activity |
| KR101598296B1 (ko) | 2014-04-29 | 2016-02-26 | 가톨릭대학교 산학협력단 | Dna 복제수 변이를 이용한 강직성 척추염 발병 고위험도 예측용 조성물 및 이를 이용한 예측 방법 |
| EP3155439A4 (en) | 2014-06-10 | 2018-03-14 | Crescendo Bioscience | Biomarkers and methods for measuring and monitoring axial spondyloarthritis disease activity |
| US10183994B2 (en) * | 2014-06-30 | 2019-01-22 | Merck Patent Gmbh | Anti-TNFα antibodies with pH-dependent antigen binding for improved target clearence |
| US20170226552A1 (en) | 2014-07-03 | 2017-08-10 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using cobalt |
| WO2016007764A1 (en) | 2014-07-09 | 2016-01-14 | Abbvie Inc. | Methods for modulating the glycosylation profile of recombinant proteins using non-commonly used sugars |
| US10696735B2 (en) | 2015-01-21 | 2020-06-30 | Outlook Therapeutics, Inc. | Modulation of charge variants in a monoclonal antibody composition |
| EP3078675A1 (en) | 2015-04-10 | 2016-10-12 | Ares Trading S.A. | Induction dosing regimen for the treatment of tnf alpha mediated disorders |
| JP6830105B2 (ja) | 2015-09-29 | 2021-02-17 | クレッシェンド バイオサイエンス インコーポレイテッド | 乾癬性関節炎の疾患活動性を評価するためのバイオマーカーおよび方法 |
| WO2017058999A2 (en) | 2015-09-29 | 2017-04-06 | Crescendo Bioscience | Biomarkers and methods for assessing response to inflammatory disease therapy withdrawal |
| MX2018009341A (es) | 2016-02-03 | 2019-05-15 | Oncobiologics Inc | Formulaciones tamponadas para una mayor estabilidad de anticuerpos. |
| PL3442657T3 (pl) * | 2016-04-15 | 2023-01-23 | Esm Technologies, Llc | Sposób oceny leków do leczenia ruchomych stawów |
| CN106290885A (zh) * | 2016-07-18 | 2017-01-04 | 本·沙朗 | 一种血清英夫利西elisa检测试剂盒和检测方法 |
| EP4467565A3 (en) | 2016-12-21 | 2025-03-12 | Amgen Inc. | Anti-tnf alpha antibody formulations |
| CN106501523A (zh) * | 2017-01-17 | 2017-03-15 | 安徽同致生物工程股份有限公司 | 基质蛋白酶3测定试剂盒 |
| EP3765634A4 (en) | 2018-03-16 | 2021-12-01 | Scipher Medicine Corporation | METHODS AND SYSTEMS FOR PREDICTING THE RESPONSE TO ANTI-TNF THERAPIES |
| CN108872585A (zh) * | 2018-05-08 | 2018-11-23 | 广州创尔生物技术股份有限公司 | 一种胶原蛋白端肽的检测方法 |
| CN113939583A (zh) * | 2018-07-10 | 2022-01-14 | 台湾地区“中央研究院” | 用于诊断、评估预后及治疗僵直性脊椎炎的生物标记及目标 |
| AU2020308906A1 (en) | 2019-06-27 | 2022-02-03 | Scipher Medicine Corporation | Developing classifiers for stratifying patients |
| RU2724276C1 (ru) * | 2020-03-19 | 2020-06-22 | Федеральное государственное бюджетное научное учреждение "Научно-исследовательский институт ревматологии имени В.А. Насоновой" (ФГБНУ НИИР им. В.А. Насоновой) | Способ экспресс-оценки риска поражения осевого скелета при ранних формах псориатического артрита |
| KR102573606B1 (ko) * | 2021-10-14 | 2023-08-31 | 계명대학교 산학협력단 | 혈청 시료를 이용하여 류마티스성 질환과 강직성 척추염을 구분하여 진단하기 위한 조성물 및 키트 |
| KR102805517B1 (ko) * | 2022-12-22 | 2025-05-12 | 주식회사 셀렉소바이오 | 강직성 척추염 진단용 조성물, 키트 및 이의 정보제공방법 |
| KR20250037336A (ko) | 2023-09-07 | 2025-03-17 | 주식회사 류마커바이오 | 강직척추염 중증도 및 병리학적 골형성 활성을 진단하기 위한 조성물 |
Family Cites Families (116)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5179017A (en) | 1980-02-25 | 1993-01-12 | The Trustees Of Columbia University In The City Of New York | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| US4634665A (en) | 1980-02-25 | 1987-01-06 | The Trustees Of Columbia University In The City Of New York | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| US4399216A (en) | 1980-02-25 | 1983-08-16 | The Trustees Of Columbia University | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| US4510245A (en) | 1982-11-18 | 1985-04-09 | Chiron Corporation | Adenovirus promoter system |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| EP0154316B1 (en) | 1984-03-06 | 1989-09-13 | Takeda Chemical Industries, Ltd. | Chemically modified lymphokine and production thereof |
| JPS6147500A (ja) | 1984-08-15 | 1986-03-07 | Res Dev Corp Of Japan | キメラモノクロ−ナル抗体及びその製造法 |
| EP0173494A3 (en) | 1984-08-27 | 1987-11-25 | The Board Of Trustees Of The Leland Stanford Junior University | Chimeric receptors by dna splicing and expression |
| GB8422238D0 (en) | 1984-09-03 | 1984-10-10 | Neuberger M S | Chimeric proteins |
| JPS61134325A (ja) | 1984-12-04 | 1986-06-21 | Teijin Ltd | ハイブリツド抗体遺伝子の発現方法 |
| US5168062A (en) | 1985-01-30 | 1992-12-01 | University Of Iowa Research Foundation | Transfer vectors and microorganisms containing human cytomegalovirus immediate-early promoter-regulatory DNA sequence |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| US4683195A (en) | 1986-01-30 | 1987-07-28 | Cetus Corporation | Process for amplifying, detecting, and/or-cloning nucleic acid sequences |
| US4968615A (en) | 1985-12-18 | 1990-11-06 | Ciba-Geigy Corporation | Deoxyribonucleic acid segment from a virus |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| DE3631229A1 (de) | 1986-09-13 | 1988-03-24 | Basf Ag | Monoklonale antikoerper gegen humanen tumornekrosefaktor (tnf) und deren verwendung |
| US5702909A (en) | 1987-11-06 | 1997-12-30 | Washington Research Foundation | Methods of detecting collagen type II degradation in vivo |
| US6153732A (en) * | 1987-11-06 | 2000-11-28 | Washington Research Foundation | Kit for detecting analyte indicative of type II collagen resorption in vivo |
| US5300434A (en) | 1987-11-06 | 1994-04-05 | Washington Research Foundation | Hybridoma cell line producing an antibody to type-I collagen amino-terminal telopeptide |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| JP2989002B2 (ja) | 1988-12-22 | 1999-12-13 | キリン―アムジエン・インコーポレーテツド | 化学修飾顆粒球コロニー刺激因子 |
| IL162181A (en) | 1988-12-28 | 2006-04-10 | Pdl Biopharma Inc | A method of producing humanized immunoglubulin, and polynucleotides encoding the same |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US6498237B2 (en) | 1989-08-07 | 2002-12-24 | Peptech Limited | Tumor necrosis factor antibodies |
| US5959087A (en) | 1989-08-07 | 1999-09-28 | Peptide Technology, Ltd. | Tumour necrosis factor binding ligands |
| CA2485553A1 (en) | 1989-09-05 | 1991-03-21 | Immunex Corporation | Tumor necrosis factor - .alpha. and - .beta. receptors |
| US5136248A (en) | 1990-01-29 | 1992-08-04 | Niagara Mohawk Power Corporation | Method and detector for identifying insulator flashover |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| AU665190B2 (en) | 1990-07-10 | 1995-12-21 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| DK0564531T3 (da) | 1990-12-03 | 1998-09-28 | Genentech Inc | Berigelsesfremgangsmåde for variantproteiner med ændrede bindingsegenskaber |
| DK1279731T3 (da) | 1991-03-01 | 2007-09-24 | Dyax Corp | Fremgangsmåde til udvikling af bindende miniproteiner |
| US7192584B2 (en) | 1991-03-18 | 2007-03-20 | Centocor, Inc. | Methods of treating psoriasis with anti-TNF antibodies |
| US20040120952A1 (en) | 2000-08-07 | 2004-06-24 | Centocor, Inc | Anti-TNF antibodies and peptides of human tumor necrosis factor |
| US20070298040A1 (en) | 1991-03-18 | 2007-12-27 | Centocor, Inc. | Methods of treating seronegative arthropathy with anti-TNF antibodies |
| US20060246073A1 (en) | 1991-03-18 | 2006-11-02 | Knight David M | Anti-TNF antibodies and peptides of human tumor necrosis factor |
| US6277969B1 (en) | 1991-03-18 | 2001-08-21 | New York University | Anti-TNF antibodies and peptides of human tumor necrosis factor |
| US5656272A (en) | 1991-03-18 | 1997-08-12 | New York University Medical Center | Methods of treating TNF-α-mediated Crohn's disease using chimeric anti-TNF antibodies |
| DK1471142T3 (da) | 1991-04-10 | 2009-03-09 | Scripps Research Inst | Heterodimere receptor-biblioteker under anvendelse af fagemider |
| DE4122599C2 (de) | 1991-07-08 | 1993-11-11 | Deutsches Krebsforsch | Phagemid zum Screenen von Antikörpern |
| ATE181571T1 (de) | 1991-09-23 | 1999-07-15 | Medical Res Council | Methoden zur herstellung humanisierter antikörper |
| EP0636026B1 (en) | 1992-04-02 | 2001-12-05 | Smithkline Beecham Corporation | Compounds useful for treating inflammatory diseases and inhibiting production of tumor necrosis factor |
| NZ256293A (en) | 1992-09-15 | 1997-06-24 | Immunex Corp | Method of treating tumour necrosis factor - mediated inflammation by use of tnf antagonist |
| EP1262564A3 (en) | 1993-01-07 | 2004-03-31 | Sequenom, Inc. | Dna sequencing by mass spectrometry |
| US5605798A (en) | 1993-01-07 | 1997-02-25 | Sequenom, Inc. | DNA diagnostic based on mass spectrometry |
| WO1994021822A1 (en) | 1993-03-19 | 1994-09-29 | Sequenom, Inc. | Dna sequencing by mass spectrometry via exonuclease degradation |
| US6090382A (en) | 1996-02-09 | 2000-07-18 | Basf Aktiengesellschaft | Human antibodies that bind human TNFα |
| BRPI9707379B8 (pt) | 1996-02-09 | 2015-07-07 | Abbvie Biotechnology Ltd | Composições farmacêuticas compreendendo anticorpo humano recombinante geneticamente engenheirado, e anticorpo humano recombinante geneticamente engenheirado. |
| US6515016B2 (en) * | 1996-12-02 | 2003-02-04 | Angiotech Pharmaceuticals, Inc. | Composition and methods of paclitaxel for treating psoriasis |
| GB9702252D0 (en) | 1997-02-06 | 1997-03-26 | Univ Sheffield Medical The Sch | Collagen assay |
| US6506607B1 (en) | 1997-12-24 | 2003-01-14 | Millennium Pharmaceuticals, Inc. | Methods and compositions for the identification and assessment of prostate cancer therapies and the diagnosis of prostate cancer |
| US6607879B1 (en) | 1998-02-09 | 2003-08-19 | Incyte Corporation | Compositions for the detection of blood cell and immunological response gene expression |
| US6642007B1 (en) * | 1998-11-02 | 2003-11-04 | Pfizer Inc. | Assays for measurement of type II collagen fragments in urine |
| US6423321B2 (en) * | 1999-02-24 | 2002-07-23 | Edward L. Tobinick | Cytokine antagonists for the treatment of sensorineural hearing loss |
| UA81743C2 (uk) | 2000-08-07 | 2008-02-11 | Центокор, Инк. | МОНОКЛОНАЛЬНЕ АНТИТІЛО ЛЮДИНИ, ЩО СПЕЦИФІЧНО ЗВ'ЯЗУЄТЬСЯ З ФАКТОРОМ НЕКРОЗУ ПУХЛИН АЛЬФА (ФНПα), ФАРМАЦЕВТИЧНА КОМПОЗИЦІЯ, ЩО ЙОГО МІСТИТЬ, ТА СПОСІБ ЛІКУВАННЯ РЕВМАТОЇДНОГО АРТРИТУ |
| US20060018907A1 (en) | 2000-08-07 | 2006-01-26 | Centocor, Inc. | Anti-TNF antibodies and peptides of human tumor necrosis factor |
| US20050249735A1 (en) | 2000-08-07 | 2005-11-10 | Centocor, Inc. | Methods of treating ankylosing spondylitis using anti-TNF antibodies and peptides of human tumor necrosis factor |
| KR20030074693A (ko) | 2000-12-28 | 2003-09-19 | 알투스 바이올로직스 인코포레이티드 | 전항체 및 이의 단편의 결정과 이의 제조 및 사용 방법 |
| WO2002070007A1 (en) | 2001-03-02 | 2002-09-12 | Medimmune, Inc. | Methods of preventing or treating inflammatory or autoimmune disorders by administering integrin alphav beta3 antagonists |
| BR0206160A (pt) | 2001-05-25 | 2004-10-26 | Abbott Gmbh & Co Kg | Uso de anticorpos anti-tnf como medicamentos no tratamento de distúrbios sépticos de pacientes anêmicos |
| CA2817619A1 (en) | 2001-06-08 | 2002-12-08 | Abbott Laboratories (Bermuda) Ltd. | Methods of administering anti-tnf.alpha. antibodies |
| US20030161828A1 (en) | 2002-02-19 | 2003-08-28 | Abbott Gmbh & Co. Kg | Use of TNF antagonists as drugs for the treatment of patients with an inflammatory reaction and without suffering from total organ failure |
| US20030206898A1 (en) | 2002-04-26 | 2003-11-06 | Steven Fischkoff | Use of anti-TNFalpha antibodies and another drug |
| US20040009172A1 (en) | 2002-04-26 | 2004-01-15 | Steven Fischkoff | Use of anti-TNFalpha antibodies and another drug |
| CA2493067A1 (en) * | 2002-07-19 | 2004-01-29 | Abbott Biotechnology Ltd. | Treatment of tnf.alpha. related disorders |
| US20090280065A1 (en) | 2006-04-10 | 2009-11-12 | Willian Mary K | Uses and Compositions for Treatment of Psoriasis |
| US20040033228A1 (en) | 2002-08-16 | 2004-02-19 | Hans-Juergen Krause | Formulation of human antibodies for treating TNF-alpha associated disorders |
| MY150740A (en) | 2002-10-24 | 2014-02-28 | Abbvie Biotechnology Ltd | Low dose methods for treating disorders in which tnf? activity is detrimental |
| WO2004042012A2 (en) | 2002-11-01 | 2004-05-21 | Bayer Healthcare Llc | Process for concentration of macromolecules |
| US20040086532A1 (en) | 2002-11-05 | 2004-05-06 | Allergan, Inc., | Botulinum toxin formulations for oral administration |
| EP1558932A2 (en) * | 2002-11-08 | 2005-08-03 | Barnes-Jewish Hospital | Uncoupled collagen synthesis and degradation assays |
| CN1225479C (zh) * | 2002-12-23 | 2005-11-02 | 马菁 | 肿瘤坏死因子抗体，其制备方法以及药物组合物 |
| EP1713502A1 (de) | 2004-02-12 | 2006-10-25 | MERCK PATENT GmbH | Hochkonzentrierte, flüssige formulierungen von anti-egfr-antikörpern |
| TW201705980A (zh) | 2004-04-09 | 2017-02-16 | 艾伯維生物技術有限責任公司 | 用於治療ＴＮＦα相關失調症之多重可變劑量療法 |
| US20060083741A1 (en) | 2004-10-08 | 2006-04-20 | Hoffman Rebecca S | Treatment of respiratory syncytial virus (RSV) infection |
| WO2007011390A2 (en) | 2004-10-09 | 2007-01-25 | Government Of The United States As Represented By The Secretary Of The Army | Large-scale production of human serum butyrylcholinesterase as a bioscavenger |
| US7485468B2 (en) | 2004-10-15 | 2009-02-03 | Galapagos Bv | Molecular targets and compounds, and methods to identify the same, useful in the treatment of joint degenerative and inflammatory diseases |
| US7541028B2 (en) * | 2005-01-04 | 2009-06-02 | Gp Medical, Inc. | Nanoparticles for monoclonal antibody delivery |
| CA2606270A1 (en) | 2005-04-19 | 2006-10-26 | Massachusetts Institute Of Technology | Amphiphilic polymers and methods of use thereof |
| JP5757495B2 (ja) | 2005-05-16 | 2015-07-29 | アッヴィ バイオテクノロジー リミテッド | びらん性多発性関節炎の治療のためのｔｎｆ阻害剤の使用 |
| US20070041905A1 (en) | 2005-08-19 | 2007-02-22 | Hoffman Rebecca S | Method of treating depression using a TNF-alpha antibody |
| JP5198277B2 (ja) | 2005-11-01 | 2013-05-15 | アボツト・バイオテクノロジー・リミテツド | バイオマーカーを用いて強直性脊椎炎を診断するための方法及び組成物 |
| US20070202051A1 (en) | 2006-02-10 | 2007-08-30 | Pari Gmbh | Aerosols for sinunasal drug delivery |
| EP2738179A1 (en) | 2006-04-05 | 2014-06-04 | AbbVie Biotechnology Ltd | Antibody purification |
| US20080118496A1 (en) | 2006-04-10 | 2008-05-22 | Medich John R | Uses and compositions for treatment of juvenile rheumatoid arthritis |
| US9399061B2 (en) | 2006-04-10 | 2016-07-26 | Abbvie Biotechnology Ltd | Methods for determining efficacy of TNF-α inhibitors for treatment of rheumatoid arthritis |
| US20090317399A1 (en) | 2006-04-10 | 2009-12-24 | Pollack Paul F | Uses and compositions for treatment of CROHN'S disease |
| US9605064B2 (en) | 2006-04-10 | 2017-03-28 | Abbvie Biotechnology Ltd | Methods and compositions for treatment of skin disorders |
| EP2666472A3 (en) | 2006-04-10 | 2014-04-02 | Abbott Biotechnology Ltd | Uses and compositions for treatment of psoriatic arthritis |
| WO2007120626A2 (en) | 2006-04-10 | 2007-10-25 | Abbott Biotechnology Ltd. | Uses and compositions for treatment of ankylosing spondylitis |
| US20080131374A1 (en) | 2006-04-19 | 2008-06-05 | Medich John R | Uses and compositions for treatment of rheumatoid arthritis |
| US20100021451A1 (en) | 2006-06-08 | 2010-01-28 | Wong Robert L | Uses and compositions for treatment of ankylosing spondylitis |
| US20080311043A1 (en) | 2006-06-08 | 2008-12-18 | Hoffman Rebecca S | Uses and compositions for treatment of psoriatic arthritis |
| TWI542374B (zh) | 2006-06-30 | 2016-07-21 | 艾伯維生物技術有限責任公司 | 自動注射裝置 |
| MX345141B (es) | 2006-09-13 | 2017-01-18 | Abbvie Inc * | Mejoras de cultivos celulares. |
| EP2089428B1 (en) | 2006-10-27 | 2013-11-20 | AbbVie Biotechnology Ltd | Crystalline anti-htnfalpha antibodies |
| EP2165194A4 (en) | 2007-05-31 | 2010-09-08 | Abbott Lab | BIOMARKERS FOR PREDICTING RESPONSABILITY TO TNF ALPHA INHIBITORS IN AUTOIMMUNE DISEASES |
| EP2152318A4 (en) | 2007-06-01 | 2011-12-07 | Abbott Biotech Ltd | COMPOSITIONS AND USES FOR THE TREATMENT OF PSORIASIS AND CROHN'S DISEASE |
| WO2008154543A2 (en) | 2007-06-11 | 2008-12-18 | Abbott Biotechnology Ltd. | Methods for treating juvenile idiopathic arthritis |
| EP2173380A4 (en) | 2007-07-13 | 2011-08-31 | Abbott Biotech Ltd | METHOD AND COMPOSITIONS FOR PULMONARY ADMINISTRATION OF A TNFa HEMMER |
| MX2010001488A (es) | 2007-08-08 | 2010-03-01 | Abbott Lab | Composiciones y metodos para cristalizar anticuerpos. |
| CN101802005B (zh) | 2007-08-28 | 2015-09-16 | 艾伯维生物技术有限公司 | 包括关于阿达木单抗的结合蛋白质的组合物和方法 |
| US8883146B2 (en) | 2007-11-30 | 2014-11-11 | Abbvie Inc. | Protein formulations and methods of making same |
| CN101969971A (zh) | 2007-11-30 | 2011-02-09 | 雅培制药有限公司 | 蛋白制剂及其制备方法 |
| US20130195888A1 (en) | 2007-11-30 | 2013-08-01 | Abbvie | Ultrafiltration and diafiltration formulation methods for protein processing |
| US20090271164A1 (en) | 2008-01-03 | 2009-10-29 | Peng Joanna Z | Predicting long-term efficacy of a compound in the treatment of psoriasis |
| NZ586576A (en) | 2008-01-15 | 2012-08-31 | Abbott Lab | Improved mammalian expression vectors and uses thereof |
| RU2537139C2 (ru) | 2008-01-15 | 2014-12-27 | Эбботт Гмбх Унд Ко.Кг | Порошковые белковые композиции и способы их получения |
| EP2271671A2 (en) | 2008-03-24 | 2011-01-12 | Abbott Biotechnology Ltd. | Tnf-alpha inhibitors for treating bone loss |
| US9094979B2 (en) | 2008-05-16 | 2015-07-28 | Qualcomm Incorporated | Load balancing in a wireless communication system |
| RU2524487C2 (ru) | 2009-04-29 | 2014-07-27 | Эббви Байотекнолоджи Лтд | Автоматическое инъекционное устройство |
| CN104490767A (zh) | 2009-05-04 | 2015-04-08 | 艾伯维生物技术有限公司 | 人抗TNF-α抗体的稳定高蛋白质浓度制剂 |
| IT1395574B1 (it) | 2009-09-14 | 2012-10-16 | Guala Dispensing Spa | Dispositivo di erogazione |
| US20120014956A1 (en) | 2010-02-02 | 2012-01-19 | Hartmut Kupper | Methods and compositions for predicting responsiveness to treatment with tnf-alpha inhibitor |
| PL2575884T3 (pl) | 2010-06-03 | 2018-12-31 | Abbvie Biotechnology Ltd | Zastosowania i kompozycje do leczenia ropni mnogich pach (HS) |
-
2006
- 2006-10-31 JP JP2008538977A patent/JP5198277B2/ja not_active Expired - Fee Related
- 2006-10-31 TW TW102119988A patent/TW201337266A/zh unknown
- 2006-10-31 RS RS20130493A patent/RS53055B/sr unknown
- 2006-10-31 EP EP06849865.8A patent/EP1948235B1/en active Active
- 2006-10-31 ES ES06849865T patent/ES2431643T3/es active Active
- 2006-10-31 BR BRPI0618085-0A patent/BRPI0618085A2/pt not_active IP Right Cessation
- 2006-10-31 US US11/591,241 patent/US7919264B2/en active Active
- 2006-10-31 AU AU2006337105A patent/AU2006337105B2/en not_active Ceased
- 2006-10-31 HR HRP20131112TT patent/HRP20131112T1/hr unknown
- 2006-10-31 NZ NZ608431A patent/NZ608431A/en not_active IP Right Cessation
- 2006-10-31 PL PL06849865T patent/PL1948235T3/pl unknown
- 2006-10-31 CA CA002626804A patent/CA2626804A1/en not_active Abandoned
- 2006-10-31 DK DK06849865.8T patent/DK1948235T3/da active
- 2006-10-31 NZ NZ567286A patent/NZ567286A/en not_active IP Right Cessation
- 2006-10-31 CN CN200680040803A patent/CN101663048A/zh active Pending
- 2006-10-31 EP EP11155169A patent/EP2357479A1/en not_active Withdrawn
- 2006-10-31 RU RU2008121880/15A patent/RU2438704C2/ru not_active IP Right Cessation
- 2006-10-31 SI SI200631648T patent/SI1948235T1/sl unknown
- 2006-10-31 PT PT68498658T patent/PT1948235E/pt unknown
- 2006-10-31 TW TW095140333A patent/TWI424161B/zh not_active IP Right Cessation
- 2006-10-31 SG SG201100668-1A patent/SG169361A1/en unknown
- 2006-10-31 NZ NZ595340A patent/NZ595340A/xx not_active IP Right Cessation
- 2006-10-31 KR KR1020137031666A patent/KR20140012160A/ko not_active Abandoned
- 2006-10-31 CN CN201310240384XA patent/CN103336129A/zh active Pending
- 2006-10-31 WO PCT/US2006/042564 patent/WO2007089303A2/en not_active Ceased
-
2008
- 2008-04-17 IL IL190964A patent/IL190964A0/en unknown
- 2008-04-30 KR KR1020087010615A patent/KR101468523B1/ko not_active Expired - Fee Related
-
2011
- 2011-01-25 IL IL210876A patent/IL210876A0/en unknown
- 2011-02-25 US US13/034,809 patent/US9086418B2/en not_active Expired - Fee Related
- 2011-06-27 RU RU2011126441/15A patent/RU2011126441A/ru not_active Application Discontinuation
- 2011-11-17 JP JP2011251783A patent/JP2012093361A/ja not_active Ceased
-
2013
- 2013-07-29 JP JP2013156781A patent/JP2014013241A/ja not_active Ceased
-
2014
- 2014-11-28 JP JP2014241725A patent/JP2015096856A/ja active Pending
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TWI671761B (zh) * | 2017-05-01 | 2019-09-11 | 臺中榮民總醫院 | 脊椎關節炎患者疾病活動度電子病歷管理系統 |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| TWI424161B (zh) | 利用生物標記診斷關節黏連脊椎炎之方法及組合物 | |
| US9512216B2 (en) | Use of TNFα inhibitor | |
| AU2012346861A1 (en) | Methods and compositions for determining responsiveness to treatment with a tnf-alpha inhibitor | |
| KR20190097128A (ko) | 루푸스 신염의 중증도 및 진행을 모니터링하기 위한 소변에서 검출된 갈렉틴 3 결합 단백질의 사용 방법 | |
| CA2564435A1 (en) | Methods for monitoring and treating intestinal disorders | |
| AU2013201969A1 (en) | Methods and compositions for diagnosing ankylosing spondylitis using biomarkers | |
| HK1123199B (en) | Methods for determining efficacy of adalimumab in subjects having ankylosing spondylitis using ctx-ii and mmp3 as biomarkers | |
| HK1159757A (en) | Methods and compositions for diagnosing ankylosing spondylitis using biomarkers | |
| AU2012254978C1 (en) | Use of TNF inhibitor for treatment of erosive polyarthritis | |
| HK40014055B (en) | Methods for the use of galectin 3 binding protein detected in the urine for monitoring the severity and progression of lupus nephritis |