AU2010305281C1 - Siglec 15 antibodies in treating bone loss-related disease - Google Patents
Siglec 15 antibodies in treating bone loss-related disease Download PDFInfo
- Publication number
- AU2010305281C1 AU2010305281C1 AU2010305281A AU2010305281A AU2010305281C1 AU 2010305281 C1 AU2010305281 C1 AU 2010305281C1 AU 2010305281 A AU2010305281 A AU 2010305281A AU 2010305281 A AU2010305281 A AU 2010305281A AU 2010305281 C1 AU2010305281 C1 AU 2010305281C1
- Authority
- AU
- Australia
- Prior art keywords
- seq
- chain variable
- variable domain
- antibody
- set forth
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Ceased
Links
- 206010065687 Bone loss Diseases 0.000 title claims abstract description 38
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 title claims abstract description 28
- 101000709472 Homo sapiens Sialic acid-binding Ig-like lectin 15 Proteins 0.000 title claims description 147
- 102100034361 Sialic acid-binding Ig-like lectin 15 Human genes 0.000 title claims description 140
- 201000010099 disease Diseases 0.000 title abstract description 18
- 230000027455 binding Effects 0.000 claims abstract description 330
- 239000012634 fragment Substances 0.000 claims abstract description 301
- 239000000427 antigen Substances 0.000 claims abstract description 291
- 108091007433 antigens Proteins 0.000 claims abstract description 290
- 102000036639 antigens Human genes 0.000 claims abstract description 290
- 210000004027 cell Anatomy 0.000 claims abstract description 176
- 210000002997 osteoclast Anatomy 0.000 claims abstract description 104
- 238000000034 method Methods 0.000 claims abstract description 100
- 206010028980 Neoplasm Diseases 0.000 claims abstract description 39
- 201000011510 cancer Diseases 0.000 claims abstract description 39
- 238000011282 treatment Methods 0.000 claims abstract description 33
- 239000000203 mixture Substances 0.000 claims abstract description 15
- 208000020084 Bone disease Diseases 0.000 claims abstract description 12
- 150000001413 amino acids Chemical class 0.000 claims description 203
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 93
- 150000007523 nucleic acids Chemical class 0.000 claims description 68
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 68
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 62
- 229920001184 polypeptide Polymers 0.000 claims description 61
- 108020004707 nucleic acids Proteins 0.000 claims description 48
- 102000039446 nucleic acids Human genes 0.000 claims description 48
- 230000004069 differentiation Effects 0.000 claims description 44
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 41
- 239000013598 vector Substances 0.000 claims description 34
- 239000013604 expression vector Substances 0.000 claims description 29
- 230000001225 therapeutic effect Effects 0.000 claims description 27
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 claims description 22
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 claims description 22
- 210000001519 tissue Anatomy 0.000 claims description 22
- 241000124008 Mammalia Species 0.000 claims description 20
- 102000014128 RANK Ligand Human genes 0.000 claims description 19
- 108010025832 RANK Ligand Proteins 0.000 claims description 19
- 201000001441 melanoma Diseases 0.000 claims description 19
- 230000002401 inhibitory effect Effects 0.000 claims description 15
- 239000002243 precursor Substances 0.000 claims description 14
- 208000001132 Osteoporosis Diseases 0.000 claims description 12
- 208000008839 Kidney Neoplasms Diseases 0.000 claims description 11
- 206010033128 Ovarian cancer Diseases 0.000 claims description 11
- 206010061535 Ovarian neoplasm Diseases 0.000 claims description 11
- 206010038389 Renal cancer Diseases 0.000 claims description 11
- 201000010982 kidney cancer Diseases 0.000 claims description 11
- 239000008194 pharmaceutical composition Substances 0.000 claims description 11
- 206010006187 Breast cancer Diseases 0.000 claims description 10
- 208000026310 Breast neoplasm Diseases 0.000 claims description 10
- 206010060862 Prostate cancer Diseases 0.000 claims description 10
- 208000000236 Prostatic Neoplasms Diseases 0.000 claims description 10
- 229940127089 cytotoxic agent Drugs 0.000 claims description 10
- 208000006386 Bone Resorption Diseases 0.000 claims description 9
- 206010009944 Colon cancer Diseases 0.000 claims description 9
- 206010058467 Lung neoplasm malignant Diseases 0.000 claims description 9
- 230000024279 bone resorption Effects 0.000 claims description 9
- 208000029742 colonic neoplasm Diseases 0.000 claims description 9
- 208000035475 disorder Diseases 0.000 claims description 9
- 201000005202 lung cancer Diseases 0.000 claims description 9
- 208000020816 lung neoplasm Diseases 0.000 claims description 9
- 230000009870 specific binding Effects 0.000 claims description 9
- 101000934338 Homo sapiens Myeloid cell surface antigen CD33 Proteins 0.000 claims description 8
- 102100025243 Myeloid cell surface antigen CD33 Human genes 0.000 claims description 8
- 239000002246 antineoplastic agent Substances 0.000 claims description 8
- 239000003795 chemical substances by application Substances 0.000 claims description 8
- 238000003745 diagnosis Methods 0.000 claims description 8
- 239000003814 drug Substances 0.000 claims description 8
- 229940079593 drug Drugs 0.000 claims description 8
- 239000003937 drug carrier Substances 0.000 claims description 8
- 238000004519 manufacturing process Methods 0.000 claims description 8
- BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical compound [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 claims description 8
- 102100038080 B-cell receptor CD22 Human genes 0.000 claims description 6
- 108010029157 Sialic Acid Binding Ig-like Lectin 2 Proteins 0.000 claims description 6
- 230000000123 anti-resoprtive effect Effects 0.000 claims description 6
- 230000000903 blocking effect Effects 0.000 claims description 6
- 201000007455 central nervous system cancer Diseases 0.000 claims description 6
- 239000002254 cytotoxic agent Substances 0.000 claims description 6
- 231100000599 cytotoxic agent Toxicity 0.000 claims description 6
- 210000002307 prostate Anatomy 0.000 claims description 6
- 238000004113 cell culture Methods 0.000 claims description 5
- 230000001419 dependent effect Effects 0.000 claims description 5
- 230000001404 mediated effect Effects 0.000 claims description 5
- 208000005368 osteomalacia Diseases 0.000 claims description 5
- 208000014311 Cushing syndrome Diseases 0.000 claims description 4
- 239000012623 DNA damaging agent Substances 0.000 claims description 4
- 101150029707 ERBB2 gene Proteins 0.000 claims description 4
- 206010020850 Hyperthyroidism Diseases 0.000 claims description 4
- 208000010191 Osteitis Deformans Diseases 0.000 claims description 4
- 208000027868 Paget disease Diseases 0.000 claims description 4
- 206010035226 Plasma cell myeloma Diseases 0.000 claims description 4
- 239000002253 acid Substances 0.000 claims description 4
- 230000002927 anti-mitotic effect Effects 0.000 claims description 4
- 231100000433 cytotoxic Toxicity 0.000 claims description 4
- 230000001472 cytotoxic effect Effects 0.000 claims description 4
- 102000052116 epidermal growth factor receptor activity proteins Human genes 0.000 claims description 4
- 108700015053 epidermal growth factor receptor activity proteins Proteins 0.000 claims description 4
- 208000027202 mammary Paget disease Diseases 0.000 claims description 4
- YOHYSYJDKVYCJI-UHFFFAOYSA-N n-[3-[[6-[3-(trifluoromethyl)anilino]pyrimidin-4-yl]amino]phenyl]cyclopropanecarboxamide Chemical compound FC(F)(F)C1=CC=CC(NC=2N=CN=C(NC=3C=C(NC(=O)C4CC4)C=CC=3)C=2)=C1 YOHYSYJDKVYCJI-UHFFFAOYSA-N 0.000 claims description 4
- 229910052697 platinum Inorganic materials 0.000 claims description 4
- 102000004856 Lectins Human genes 0.000 claims description 3
- 108090001090 Lectins Proteins 0.000 claims description 3
- 208000029725 Metabolic bone disease Diseases 0.000 claims description 3
- 208000034578 Multiple myelomas Diseases 0.000 claims description 3
- 206010031243 Osteogenesis imperfecta Diseases 0.000 claims description 3
- 230000004054 inflammatory process Effects 0.000 claims description 3
- 239000002523 lectin Substances 0.000 claims description 3
- 230000003248 secreting effect Effects 0.000 claims description 3
- 210000002966 serum Anatomy 0.000 claims description 3
- 208000000819 Adrenocortical Hyperfunction Diseases 0.000 claims description 2
- 208000002197 Ehlers-Danlos syndrome Diseases 0.000 claims description 2
- 208000026019 Fanconi renotubular syndrome Diseases 0.000 claims description 2
- 208000015872 Gaucher disease Diseases 0.000 claims description 2
- 206010020564 Hyperadrenocorticism Diseases 0.000 claims description 2
- 208000037147 Hypercalcaemia Diseases 0.000 claims description 2
- 201000002980 Hyperparathyroidism Diseases 0.000 claims description 2
- 206010058359 Hypogonadism Diseases 0.000 claims description 2
- 208000001826 Marfan syndrome Diseases 0.000 claims description 2
- 206010027294 Menkes' syndrome Diseases 0.000 claims description 2
- 206010049088 Osteopenia Diseases 0.000 claims description 2
- 208000010067 Pituitary ACTH Hypersecretion Diseases 0.000 claims description 2
- 208000020627 Pituitary-dependent Cushing syndrome Diseases 0.000 claims description 2
- 201000008736 Systemic mastocytosis Diseases 0.000 claims description 2
- 229930003316 Vitamin D Natural products 0.000 claims description 2
- 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 claims description 2
- 201000008101 adult hypophosphatasia Diseases 0.000 claims description 2
- 206010003246 arthritis Diseases 0.000 claims description 2
- 210000004369 blood Anatomy 0.000 claims description 2
- 239000008280 blood Substances 0.000 claims description 2
- 239000012228 culture supernatant Substances 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims description 2
- 230000006378 damage Effects 0.000 claims description 2
- 201000010073 fibrogenesis imperfecta ossium Diseases 0.000 claims description 2
- 230000000148 hypercalcaemia Effects 0.000 claims description 2
- 208000030915 hypercalcemia disease Diseases 0.000 claims description 2
- 208000003532 hypothyroidism Diseases 0.000 claims description 2
- 230000002989 hypothyroidism Effects 0.000 claims description 2
- 210000002540 macrophage Anatomy 0.000 claims description 2
- 208000028169 periodontal disease Diseases 0.000 claims description 2
- 201000009395 primary hyperaldosteronism Diseases 0.000 claims description 2
- 201000010108 pycnodysostosis Diseases 0.000 claims description 2
- 208000007442 rickets Diseases 0.000 claims description 2
- 208000005057 thyrotoxicosis Diseases 0.000 claims description 2
- 235000019166 vitamin D Nutrition 0.000 claims description 2
- 239000011710 vitamin D Substances 0.000 claims description 2
- 150000003710 vitamin D derivatives Chemical class 0.000 claims description 2
- 229940046008 vitamin d Drugs 0.000 claims description 2
- 229940041181 antineoplastic drug Drugs 0.000 claims 4
- 102100022005 B-lymphocyte antigen CD20 Human genes 0.000 claims 2
- 101000897405 Homo sapiens B-lymphocyte antigen CD20 Proteins 0.000 claims 2
- 208000011111 hypophosphatemic rickets Diseases 0.000 claims 1
- 208000011580 syndromic disease Diseases 0.000 claims 1
- 230000014509 gene expression Effects 0.000 abstract description 46
- 210000000988 bone and bone Anatomy 0.000 abstract description 39
- 230000001965 increasing effect Effects 0.000 abstract description 15
- 230000004071 biological effect Effects 0.000 abstract description 5
- 230000003413 degradative effect Effects 0.000 abstract description 2
- 235000001014 amino acid Nutrition 0.000 description 223
- 229940024606 amino acid Drugs 0.000 description 204
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 109
- 238000006467 substitution reaction Methods 0.000 description 42
- 108090000623 proteins and genes Proteins 0.000 description 36
- 230000000694 effects Effects 0.000 description 30
- 102000012745 Immunoglobulin Subunits Human genes 0.000 description 27
- 108010079585 Immunoglobulin Subunits Proteins 0.000 description 27
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 25
- 102000004169 proteins and genes Human genes 0.000 description 25
- 235000018102 proteins Nutrition 0.000 description 24
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 23
- 239000004473 Threonine Substances 0.000 description 23
- 230000002209 hydrophobic effect Effects 0.000 description 21
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 18
- 241000699666 Mus <mouse, genus> Species 0.000 description 18
- 102000007073 Sialic Acid Binding Immunoglobulin-like Lectins Human genes 0.000 description 18
- 108010047827 Sialic Acid Binding Immunoglobulin-like Lectins Proteins 0.000 description 18
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 17
- -1 aromatic amino acid Chemical class 0.000 description 17
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 16
- 230000007935 neutral effect Effects 0.000 description 16
- 239000000523 sample Substances 0.000 description 16
- 108020004414 DNA Proteins 0.000 description 15
- 108060003951 Immunoglobulin Proteins 0.000 description 15
- 239000002299 complementary DNA Substances 0.000 description 15
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 15
- 102000018358 immunoglobulin Human genes 0.000 description 15
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 14
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 14
- 235000003704 aspartic acid Nutrition 0.000 description 14
- 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 14
- 238000001514 detection method Methods 0.000 description 14
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 14
- 210000004072 lung Anatomy 0.000 description 13
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 12
- 230000010072 bone remodeling Effects 0.000 description 12
- 210000003169 central nervous system Anatomy 0.000 description 12
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 11
- 108010029176 Sialic Acid Binding Ig-like Lectin 1 Proteins 0.000 description 11
- 102100032855 Sialoadhesin Human genes 0.000 description 11
- 229960001230 asparagine Drugs 0.000 description 11
- 235000009582 asparagine Nutrition 0.000 description 11
- 230000006870 function Effects 0.000 description 11
- 210000000481 breast Anatomy 0.000 description 10
- 230000015556 catabolic process Effects 0.000 description 10
- 238000006243 chemical reaction Methods 0.000 description 10
- 210000001072 colon Anatomy 0.000 description 10
- 238000005516 engineering process Methods 0.000 description 10
- KDXKERNSBIXSRK-UHFFFAOYSA-N lysine Chemical compound NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 10
- 239000002773 nucleotide Substances 0.000 description 10
- 125000003729 nucleotide group Chemical group 0.000 description 10
- 229910052717 sulfur Inorganic materials 0.000 description 10
- 238000002965 ELISA Methods 0.000 description 9
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 9
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 9
- 108020004459 Small interfering RNA Proteins 0.000 description 9
- 238000006731 degradation reaction Methods 0.000 description 9
- 230000003993 interaction Effects 0.000 description 9
- 108020004999 messenger RNA Proteins 0.000 description 9
- 230000008569 process Effects 0.000 description 9
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 8
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 8
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 8
- 108010076504 Protein Sorting Signals Proteins 0.000 description 8
- 235000004279 alanine Nutrition 0.000 description 8
- 238000003556 assay Methods 0.000 description 8
- 150000001875 compounds Chemical class 0.000 description 8
- 239000013613 expression plasmid Substances 0.000 description 8
- 108020001507 fusion proteins Proteins 0.000 description 8
- 102000037865 fusion proteins Human genes 0.000 description 8
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 8
- 210000004408 hybridoma Anatomy 0.000 description 8
- 238000003119 immunoblot Methods 0.000 description 8
- 208000032839 leukemia Diseases 0.000 description 8
- 239000012528 membrane Substances 0.000 description 8
- 230000002611 ovarian Effects 0.000 description 8
- 230000008685 targeting Effects 0.000 description 8
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 7
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 7
- 102000007651 Macrophage Colony-Stimulating Factor Human genes 0.000 description 7
- 108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 description 7
- 241001529936 Murinae Species 0.000 description 7
- 239000013614 RNA sample Substances 0.000 description 7
- 230000002378 acidificating effect Effects 0.000 description 7
- 238000000338 in vitro Methods 0.000 description 7
- 238000001727 in vivo Methods 0.000 description 7
- 239000006166 lysate Substances 0.000 description 7
- 210000004962 mammalian cell Anatomy 0.000 description 7
- 229910052757 nitrogen Inorganic materials 0.000 description 7
- 238000002360 preparation method Methods 0.000 description 7
- 239000000758 substrate Substances 0.000 description 7
- 108090000625 Cathepsin K Proteins 0.000 description 6
- 102000004171 Cathepsin K Human genes 0.000 description 6
- AOJJSUZBOXZQNB-TZSSRYMLSA-N Doxorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 AOJJSUZBOXZQNB-TZSSRYMLSA-N 0.000 description 6
- 102000004190 Enzymes Human genes 0.000 description 6
- 108090000790 Enzymes Proteins 0.000 description 6
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 6
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 6
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 6
- 229920002873 Polyethylenimine Polymers 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 6
- 235000013922 glutamic acid Nutrition 0.000 description 6
- 239000004220 glutamic acid Substances 0.000 description 6
- 102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 6
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 6
- 230000013595 glycosylation Effects 0.000 description 6
- 238000006206 glycosylation reaction Methods 0.000 description 6
- 230000012010 growth Effects 0.000 description 6
- 102000057657 human SIGLEC15 Human genes 0.000 description 6
- 229930182817 methionine Natural products 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 239000013612 plasmid Substances 0.000 description 6
- 229910052727 yttrium Inorganic materials 0.000 description 6
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 5
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 5
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 5
- 108091034117 Oligonucleotide Proteins 0.000 description 5
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 5
- 108020004511 Recombinant DNA Proteins 0.000 description 5
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 230000008859 change Effects 0.000 description 5
- 229940088597 hormone Drugs 0.000 description 5
- 239000005556 hormone Substances 0.000 description 5
- 210000005260 human cell Anatomy 0.000 description 5
- 229910052739 hydrogen Inorganic materials 0.000 description 5
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 5
- 229960000310 isoleucine Drugs 0.000 description 5
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 238000003146 transient transfection Methods 0.000 description 5
- 229910052720 vanadium Inorganic materials 0.000 description 5
- OGSPWJRAVKPPFI-UHFFFAOYSA-N Alendronic Acid Chemical compound NCCCC(O)(P(O)(O)=O)P(O)(O)=O OGSPWJRAVKPPFI-UHFFFAOYSA-N 0.000 description 4
- 229940122361 Bisphosphonate Drugs 0.000 description 4
- 102000055006 Calcitonin Human genes 0.000 description 4
- 108060001064 Calcitonin Proteins 0.000 description 4
- 102000004127 Cytokines Human genes 0.000 description 4
- 108090000695 Cytokines Proteins 0.000 description 4
- DBVJJBKOTRCVKF-UHFFFAOYSA-N Etidronic acid Chemical compound OP(=O)(O)C(O)(C)P(O)(O)=O DBVJJBKOTRCVKF-UHFFFAOYSA-N 0.000 description 4
- 108091006020 Fc-tagged proteins Proteins 0.000 description 4
- 239000004471 Glycine Substances 0.000 description 4
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 4
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 4
- 102000013463 Immunoglobulin Light Chains Human genes 0.000 description 4
- 108010065825 Immunoglobulin Light Chains Proteins 0.000 description 4
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 4
- 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 4
- 239000004472 Lysine Substances 0.000 description 4
- IIDJRNMFWXDHID-UHFFFAOYSA-N Risedronic acid Chemical compound OP(=O)(O)C(P(O)(O)=O)(O)CC1=CC=CN=C1 IIDJRNMFWXDHID-UHFFFAOYSA-N 0.000 description 4
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 4
- 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 4
- 238000007792 addition Methods 0.000 description 4
- 229940062527 alendronate Drugs 0.000 description 4
- 238000000137 annealing Methods 0.000 description 4
- 150000004663 bisphosphonates Chemical class 0.000 description 4
- 210000002805 bone matrix Anatomy 0.000 description 4
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 4
- 229960004015 calcitonin Drugs 0.000 description 4
- 230000000973 chemotherapeutic effect Effects 0.000 description 4
- 238000012217 deletion Methods 0.000 description 4
- 230000037430 deletion Effects 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 230000018109 developmental process Effects 0.000 description 4
- 210000003238 esophagus Anatomy 0.000 description 4
- 229940011871 estrogen Drugs 0.000 description 4
- 239000000262 estrogen Substances 0.000 description 4
- 238000002474 experimental method Methods 0.000 description 4
- 230000004927 fusion Effects 0.000 description 4
- 239000000499 gel Substances 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- 230000005764 inhibitory process Effects 0.000 description 4
- 210000000963 osteoblast Anatomy 0.000 description 4
- 108091033319 polynucleotide Proteins 0.000 description 4
- 102000040430 polynucleotide Human genes 0.000 description 4
- 239000002157 polynucleotide Substances 0.000 description 4
- 230000002265 prevention Effects 0.000 description 4
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 238000003757 reverse transcription PCR Methods 0.000 description 4
- 229940089617 risedronate Drugs 0.000 description 4
- 125000005629 sialic acid group Chemical group 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 239000000725 suspension Substances 0.000 description 4
- 238000002560 therapeutic procedure Methods 0.000 description 4
- 238000013518 transcription Methods 0.000 description 4
- 230000035897 transcription Effects 0.000 description 4
- 229920000936 Agarose Polymers 0.000 description 3
- 239000004475 Arginine Substances 0.000 description 3
- 206010005949 Bone cancer Diseases 0.000 description 3
- 208000018084 Bone neoplasm Diseases 0.000 description 3
- 108091026890 Coding region Proteins 0.000 description 3
- 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 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 102000004889 Interleukin-6 Human genes 0.000 description 3
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 3
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 3
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 3
- 101100370002 Mus musculus Tnfsf14 gene Proteins 0.000 description 3
- 208000002193 Pain Diseases 0.000 description 3
- 108090000445 Parathyroid hormone Proteins 0.000 description 3
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 3
- 101150071241 SIGLEC15 gene Proteins 0.000 description 3
- 229940123237 Taxane Drugs 0.000 description 3
- 208000035896 Twin-reversed arterial perfusion sequence Diseases 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 238000010171 animal model Methods 0.000 description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 3
- 230000008827 biological function Effects 0.000 description 3
- 239000002617 bone density conservation agent Substances 0.000 description 3
- 239000013592 cell lysate Substances 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 239000008121 dextrose Substances 0.000 description 3
- 239000012636 effector Substances 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 238000010195 expression analysis Methods 0.000 description 3
- 210000000987 immune system Anatomy 0.000 description 3
- 229910052500 inorganic mineral Inorganic materials 0.000 description 3
- 229940100601 interleukin-6 Drugs 0.000 description 3
- 230000007774 longterm Effects 0.000 description 3
- 239000003550 marker Substances 0.000 description 3
- 239000011707 mineral Substances 0.000 description 3
- 108700037473 mouse Siglec-15 Proteins 0.000 description 3
- 238000002703 mutagenesis Methods 0.000 description 3
- 231100000350 mutagenesis Toxicity 0.000 description 3
- 230000035772 mutation Effects 0.000 description 3
- 239000003921 oil Substances 0.000 description 3
- 235000019198 oils Nutrition 0.000 description 3
- 229910052698 phosphorus Inorganic materials 0.000 description 3
- 230000026731 phosphorylation Effects 0.000 description 3
- 238000006366 phosphorylation reaction Methods 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 239000003755 preservative agent Substances 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 102000005962 receptors Human genes 0.000 description 3
- 108020003175 receptors Proteins 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 230000002441 reversible effect Effects 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 230000009885 systemic effect Effects 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 239000004474 valine Substances 0.000 description 3
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 2
- 241000282472 Canis lupus familiaris Species 0.000 description 2
- 108020004635 Complementary DNA Proteins 0.000 description 2
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 108700039887 Essential Genes Proteins 0.000 description 2
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 2
- 108010087819 Fc receptors Proteins 0.000 description 2
- 102000009109 Fc receptors Human genes 0.000 description 2
- 206010017076 Fracture Diseases 0.000 description 2
- 108010010803 Gelatin Proteins 0.000 description 2
- 102000005720 Glutathione transferase Human genes 0.000 description 2
- 108010070675 Glutathione transferase Proteins 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 2
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 2
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 2
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 2
- 108090001005 Interleukin-6 Proteins 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 2
- 125000000393 L-methionino group Chemical group [H]OC(=O)[C@@]([H])(N([H])[*])C([H])([H])C(SC([H])([H])[H])([H])[H] 0.000 description 2
- 102100028123 Macrophage colony-stimulating factor 1 Human genes 0.000 description 2
- 101710127797 Macrophage colony-stimulating factor 1 Proteins 0.000 description 2
- 102000018697 Membrane Proteins Human genes 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 206010028813 Nausea Diseases 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 108010058846 Ovalbumin Proteins 0.000 description 2
- 102000003982 Parathyroid hormone Human genes 0.000 description 2
- 239000004698 Polyethylene Substances 0.000 description 2
- 238000012228 RNA interference-mediated gene silencing Methods 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 108010090804 Streptavidin Proteins 0.000 description 2
- NKANXQFJJICGDU-QPLCGJKRSA-N Tamoxifen Chemical compound C=1C=CC=CC=1C(/CC)=C(C=1C=CC(OCCN(C)C)=CC=1)/C1=CC=CC=C1 NKANXQFJJICGDU-QPLCGJKRSA-N 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 230000000692 anti-sense effect Effects 0.000 description 2
- 239000003080 antimitotic agent Substances 0.000 description 2
- 239000003963 antioxidant agent Substances 0.000 description 2
- 235000006708 antioxidants Nutrition 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 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 2
- 229960002685 biotin Drugs 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 210000002449 bone cell Anatomy 0.000 description 2
- 230000037182 bone density Effects 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 239000011575 calcium Substances 0.000 description 2
- 229910052791 calcium Inorganic materials 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- DQLATGHUWYMOKM-UHFFFAOYSA-L cisplatin Chemical compound N[Pt](N)(Cl)Cl DQLATGHUWYMOKM-UHFFFAOYSA-L 0.000 description 2
- 229960004316 cisplatin Drugs 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 230000004540 complement-dependent cytotoxicity Effects 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 239000010949 copper Substances 0.000 description 2
- 229960001251 denosumab Drugs 0.000 description 2
- 239000003085 diluting agent Substances 0.000 description 2
- 229960004679 doxorubicin Drugs 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 238000000684 flow cytometry Methods 0.000 description 2
- 238000011010 flushing procedure Methods 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 229920000159 gelatin Polymers 0.000 description 2
- 235000019322 gelatine Nutrition 0.000 description 2
- 235000011852 gelatine desserts Nutrition 0.000 description 2
- 230000009368 gene silencing by RNA Effects 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 208000005017 glioblastoma Diseases 0.000 description 2
- 125000003147 glycosyl group Chemical group 0.000 description 2
- 239000003102 growth factor Substances 0.000 description 2
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 230000007794 irritation Effects 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 230000004807 localization Effects 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
- 230000007246 mechanism Effects 0.000 description 2
- 238000002483 medication Methods 0.000 description 2
- 238000002493 microarray Methods 0.000 description 2
- 230000004079 mineral homeostasis Effects 0.000 description 2
- 210000000822 natural killer cell Anatomy 0.000 description 2
- 230000008693 nausea Effects 0.000 description 2
- 229940021182 non-steroidal anti-inflammatory drug Drugs 0.000 description 2
- 229940092253 ovalbumin Drugs 0.000 description 2
- 238000004091 panning Methods 0.000 description 2
- 229960001319 parathyroid hormone Drugs 0.000 description 2
- 239000000199 parathyroid hormone Substances 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
- 210000002381 plasma Anatomy 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 230000001323 posttranslational effect Effects 0.000 description 2
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 2
- 230000005855 radiation Effects 0.000 description 2
- 238000003127 radioimmunoassay Methods 0.000 description 2
- 229960004622 raloxifene Drugs 0.000 description 2
- GZUITABIAKMVPG-UHFFFAOYSA-N raloxifene Chemical compound C1=CC(O)=CC=C1C1=C(C(=O)C=2C=CC(OCCN3CCCCC3)=CC=2)C2=CC=C(O)C=C2S1 GZUITABIAKMVPG-UHFFFAOYSA-N 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 238000007789 sealing Methods 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 229940095743 selective estrogen receptor modulator Drugs 0.000 description 2
- 239000000333 selective estrogen receptor modulator Substances 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 150000003431 steroids Chemical class 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 239000012096 transfection reagent Substances 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- 239000003981 vehicle Substances 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- YMXHPSHLTSZXKH-RVBZMBCESA-N (2,5-dioxopyrrolidin-1-yl) 5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoate Chemical compound C([C@H]1[C@H]2NC(=O)N[C@H]2CS1)CCCC(=O)ON1C(=O)CCC1=O YMXHPSHLTSZXKH-RVBZMBCESA-N 0.000 description 1
- ALBODLTZUXKBGZ-JUUVMNCLSA-N (2s)-2-amino-3-phenylpropanoic acid;(2s)-2,6-diaminohexanoic acid Chemical compound NCCCC[C@H](N)C(O)=O.OC(=O)[C@@H](N)CC1=CC=CC=C1 ALBODLTZUXKBGZ-JUUVMNCLSA-N 0.000 description 1
- LOGFVTREOLYCPF-KXNHARMFSA-N (2s,3r)-2-[[(2r)-1-[(2s)-2,6-diaminohexanoyl]pyrrolidine-2-carbonyl]amino]-3-hydroxybutanoic acid Chemical compound C[C@@H](O)[C@@H](C(O)=O)NC(=O)[C@H]1CCCN1C(=O)[C@@H](N)CCCCN LOGFVTREOLYCPF-KXNHARMFSA-N 0.000 description 1
- GMRQFYUYWCNGIN-ZVUFCXRFSA-N 1,25-dihydroxy vitamin D3 Chemical compound C1([C@@H]2CC[C@@H]([C@]2(CCC1)C)[C@@H](CCCC(C)(C)O)C)=CC=C1C[C@@H](O)C[C@H](O)C1=C GMRQFYUYWCNGIN-ZVUFCXRFSA-N 0.000 description 1
- PNDPGZBMCMUPRI-HVTJNCQCSA-N 10043-66-0 Chemical compound [131I][131I] PNDPGZBMCMUPRI-HVTJNCQCSA-N 0.000 description 1
- FUFLCEKSBBHCMO-UHFFFAOYSA-N 11-dehydrocorticosterone Natural products O=C1CCC2(C)C3C(=O)CC(C)(C(CC4)C(=O)CO)C4C3CCC2=C1 FUFLCEKSBBHCMO-UHFFFAOYSA-N 0.000 description 1
- 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 1
- TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 1
- 208000004998 Abdominal Pain Diseases 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 102000007469 Actins Human genes 0.000 description 1
- 108010085238 Actins Proteins 0.000 description 1
- WQVFQXXBNHHPLX-ZKWXMUAHSA-N Ala-Ala-His Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1cnc[nH]1)C(O)=O WQVFQXXBNHHPLX-ZKWXMUAHSA-N 0.000 description 1
- YYSWCHMLFJLLBJ-ZLUOBGJFSA-N Ala-Ala-Ser Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(O)=O YYSWCHMLFJLLBJ-ZLUOBGJFSA-N 0.000 description 1
- IPWKGIFRRBGCJO-IMJSIDKUSA-N Ala-Ser Chemical compound C[C@H]([NH3+])C(=O)N[C@@H](CO)C([O-])=O IPWKGIFRRBGCJO-IMJSIDKUSA-N 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 108091093088 Amplicon Proteins 0.000 description 1
- PTNFNTOBUDWHNZ-GUBZILKMSA-N Asn-Arg-Met Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(O)=O PTNFNTOBUDWHNZ-GUBZILKMSA-N 0.000 description 1
- MECFLTFREHAZLH-ACZMJKKPSA-N Asn-Glu-Cys Chemical compound C(CC(=O)O)[C@@H](C(=O)N[C@@H](CS)C(=O)O)NC(=O)[C@H](CC(=O)N)N MECFLTFREHAZLH-ACZMJKKPSA-N 0.000 description 1
- KHCNTVRVAYCPQE-CIUDSAMLSA-N Asn-Lys-Asn Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(O)=O KHCNTVRVAYCPQE-CIUDSAMLSA-N 0.000 description 1
- JHFNSBBHKSZXKB-VKHMYHEASA-N Asp-Gly Chemical compound OC(=O)C[C@H](N)C(=O)NCC(O)=O JHFNSBBHKSZXKB-VKHMYHEASA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 208000010392 Bone Fractures Diseases 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 101100454808 Caenorhabditis elegans lgg-2 gene Proteins 0.000 description 1
- 108010001789 Calcitonin Receptors Proteins 0.000 description 1
- 102100038520 Calcitonin receptor Human genes 0.000 description 1
- 102000000584 Calmodulin Human genes 0.000 description 1
- 108010041952 Calmodulin Proteins 0.000 description 1
- 208000024172 Cardiovascular disease Diseases 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- MFYSYFVPBJMHGN-ZPOLXVRWSA-N Cortisone Chemical compound O=C1CC[C@]2(C)[C@H]3C(=O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 MFYSYFVPBJMHGN-ZPOLXVRWSA-N 0.000 description 1
- MFYSYFVPBJMHGN-UHFFFAOYSA-N Cortisone Natural products O=C1CCC2(C)C3C(=O)CC(C)(C(CC4)(O)C(=O)CO)C4C3CCC2=C1 MFYSYFVPBJMHGN-UHFFFAOYSA-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
- 206010051055 Deep vein thrombosis Diseases 0.000 description 1
- 206010012735 Diarrhoea Diseases 0.000 description 1
- LVGKNOAMLMIIKO-UHFFFAOYSA-N Elaidinsaeure-aethylester Natural products CCCCCCCCC=CCCCCCCCC(=O)OCC LVGKNOAMLMIIKO-UHFFFAOYSA-N 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 102100031780 Endonuclease Human genes 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 208000010201 Exanthema Diseases 0.000 description 1
- 108060002716 Exonuclease Proteins 0.000 description 1
- 208000005050 Familial Hypophosphatemic Rickets Diseases 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- GHASVSINZRGABV-UHFFFAOYSA-N Fluorouracil Chemical compound FC1=CNC(=O)NC1=O GHASVSINZRGABV-UHFFFAOYSA-N 0.000 description 1
- YYOBUPFZLKQUAX-FXQIFTODSA-N Glu-Asn-Glu Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O YYOBUPFZLKQUAX-FXQIFTODSA-N 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 108010051696 Growth Hormone Proteins 0.000 description 1
- 102100029360 Hematopoietic cell signal transducer Human genes 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000990188 Homo sapiens Hematopoietic cell signal transducer Proteins 0.000 description 1
- 101000599951 Homo sapiens Insulin-like growth factor I Proteins 0.000 description 1
- 101000957437 Homo sapiens Mitochondrial carnitine/acylcarnitine carrier protein Proteins 0.000 description 1
- 101000709473 Homo sapiens Sialic acid-binding Ig-like lectin 14 Proteins 0.000 description 1
- 101000809875 Homo sapiens TYRO protein tyrosine kinase-binding protein Proteins 0.000 description 1
- 101000808011 Homo sapiens Vascular endothelial growth factor A Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 208000033830 Hot Flashes Diseases 0.000 description 1
- 206010060800 Hot flush Diseases 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 208000013038 Hypocalcemia Diseases 0.000 description 1
- 108010091358 Hypoxanthine Phosphoribosyltransferase Proteins 0.000 description 1
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 1
- 102100029098 Hypoxanthine-guanine phosphoribosyltransferase Human genes 0.000 description 1
- IOVUXUSIGXCREV-DKIMLUQUSA-N Ile-Leu-Phe Chemical compound CC[C@H](C)[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 IOVUXUSIGXCREV-DKIMLUQUSA-N 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 102100037852 Insulin-like growth factor I Human genes 0.000 description 1
- 108090000193 Interleukin-1 beta Proteins 0.000 description 1
- 102000003777 Interleukin-1 beta Human genes 0.000 description 1
- FADYJNXDPBKVCA-UHFFFAOYSA-N L-Phenylalanyl-L-lysin Natural products NCCCCC(C(O)=O)NC(=O)C(N)CC1=CC=CC=C1 FADYJNXDPBKVCA-UHFFFAOYSA-N 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
- 125000000510 L-tryptophano group Chemical group [H]C1=C([H])C([H])=C2N([H])C([H])=C(C([H])([H])[C@@]([H])(C(O[H])=O)N([H])[*])C2=C1[H] 0.000 description 1
- 102100020870 La-related protein 6 Human genes 0.000 description 1
- 108050008265 La-related protein 6 Proteins 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 229910052765 Lutetium Inorganic materials 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 102100038738 Mitochondrial carnitine/acylcarnitine carrier protein Human genes 0.000 description 1
- 101000957678 Mus musculus Cytochrome P450 7B1 Proteins 0.000 description 1
- 101100444898 Mus musculus Egr1 gene Proteins 0.000 description 1
- 101100477893 Mus musculus Siglec1 gene Proteins 0.000 description 1
- 101710135898 Myc proto-oncogene protein Proteins 0.000 description 1
- 102100038895 Myc proto-oncogene protein Human genes 0.000 description 1
- 238000005481 NMR spectroscopy Methods 0.000 description 1
- 206010052437 Nasal discomfort Diseases 0.000 description 1
- RMINQIRDFIBNLE-NNRWGFCXSA-N O-[N-acetyl-alpha-neuraminyl-(2->6)-N-acetyl-alpha-D-galactosaminyl]-L-serine Chemical group O1[C@H](OC[C@H](N)C(O)=O)[C@H](NC(=O)C)[C@@H](O)[C@@H](O)[C@H]1CO[C@@]1(C(O)=O)O[C@@H]([C@H](O)[C@H](O)CO)[C@H](NC(C)=O)[C@@H](O)C1 RMINQIRDFIBNLE-NNRWGFCXSA-N 0.000 description 1
- 206010030247 Oestrogen deficiency Diseases 0.000 description 1
- 102000008108 Osteoprotegerin Human genes 0.000 description 1
- 108010035042 Osteoprotegerin Proteins 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 239000002033 PVDF binder Substances 0.000 description 1
- 102100036893 Parathyroid hormone Human genes 0.000 description 1
- 241000237988 Patellidae Species 0.000 description 1
- 102000015731 Peptide Hormones Human genes 0.000 description 1
- 108010038988 Peptide Hormones Proteins 0.000 description 1
- KIQUCMUULDXTAZ-HJOGWXRNSA-N Phe-Tyr-Tyr Chemical compound N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1ccc(O)cc1)C(O)=O KIQUCMUULDXTAZ-HJOGWXRNSA-N 0.000 description 1
- 108010010677 Phosphodiesterase I Proteins 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 229920000954 Polyglycolide Polymers 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 208000010378 Pulmonary Embolism Diseases 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 238000010240 RT-PCR analysis Methods 0.000 description 1
- 101000957679 Rattus norvegicus 25-hydroxycholesterol 7-alpha-hydroxylase Proteins 0.000 description 1
- 208000036071 Rhinorrhea Diseases 0.000 description 1
- 206010039101 Rhinorrhoea Diseases 0.000 description 1
- 108010039491 Ricin Proteins 0.000 description 1
- QMCDMHWAKMUGJE-IHRRRGAJSA-N Ser-Phe-Val Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](C(C)C)C(O)=O QMCDMHWAKMUGJE-IHRRRGAJSA-N 0.000 description 1
- DKGRNFUXVTYRAS-UBHSHLNASA-N Ser-Ser-Trp Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(O)=O DKGRNFUXVTYRAS-UBHSHLNASA-N 0.000 description 1
- 102100034370 Sialic acid-binding Ig-like lectin 14 Human genes 0.000 description 1
- 108091027967 Small hairpin RNA Proteins 0.000 description 1
- 102100038803 Somatotropin Human genes 0.000 description 1
- 241000519995 Stachys sylvatica Species 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 102100038717 TYRO protein tyrosine kinase-binding protein Human genes 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- 108010049264 Teriparatide Proteins 0.000 description 1
- WDLRUFUQRNWCPK-UHFFFAOYSA-N Tetraxetan Chemical compound OC(=O)CN1CCN(CC(O)=O)CCN(CC(O)=O)CCN(CC(O)=O)CC1 WDLRUFUQRNWCPK-UHFFFAOYSA-N 0.000 description 1
- 102000002933 Thioredoxin Human genes 0.000 description 1
- COYHRQWNJDJCNA-NUJDXYNKSA-N Thr-Thr-Thr Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O COYHRQWNJDJCNA-NUJDXYNKSA-N 0.000 description 1
- 208000007536 Thrombosis Diseases 0.000 description 1
- AUYYCJSJGJYCDS-LBPRGKRZSA-N Thyrolar Chemical class IC1=CC(C[C@H](N)C(O)=O)=CC(I)=C1OC1=CC=C(O)C(I)=C1 AUYYCJSJGJYCDS-LBPRGKRZSA-N 0.000 description 1
- 108091023040 Transcription factor Proteins 0.000 description 1
- 102000040945 Transcription factor Human genes 0.000 description 1
- 101710150448 Transcriptional regulator Myc Proteins 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 208000026928 Turner syndrome Diseases 0.000 description 1
- KHPLUFDSWGDRHD-SLFFLAALSA-N Tyr-Tyr-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CC2=CC=C(C=C2)O)NC(=O)[C@H](CC3=CC=C(C=C3)O)N)C(=O)O KHPLUFDSWGDRHD-SLFFLAALSA-N 0.000 description 1
- 208000025865 Ulcer Diseases 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
- 206010047249 Venous thrombosis Diseases 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 238000011892 Von Kossa's method Methods 0.000 description 1
- 208000031878 X-linked hypophosphatemia Diseases 0.000 description 1
- 208000035724 X-linked hypophosphatemic rickets Diseases 0.000 description 1
- VWQVUPCCIRVNHF-OUBTZVSYSA-N Yttrium-90 Chemical compound [90Y] VWQVUPCCIRVNHF-OUBTZVSYSA-N 0.000 description 1
- AUYLVPGDOVEOML-UHFFFAOYSA-N [6-hydroxy-2-(4-hydroxyphenyl)-1-benzothiophen-3-yl]-[4-(piperidin-1-ylmethoxy)phenyl]methanone Chemical compound C1=CC(O)=CC=C1C1=C(C(=O)C=2C=CC(OCN3CCCCC3)=CC=2)C2=CC=C(O)C=C2S1 AUYLVPGDOVEOML-UHFFFAOYSA-N 0.000 description 1
- KYIKRXIYLAGAKQ-UHFFFAOYSA-N abcn Chemical compound C1CCCCC1(C#N)N=NC1(C#N)CCCCC1 KYIKRXIYLAGAKQ-UHFFFAOYSA-N 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 230000010933 acylation Effects 0.000 description 1
- 238000005917 acylation reaction Methods 0.000 description 1
- 210000004404 adrenal cortex Anatomy 0.000 description 1
- 230000001919 adrenal effect Effects 0.000 description 1
- 229940009456 adriamycin Drugs 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 230000001476 alcoholic effect Effects 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 229910052782 aluminium Inorganic materials 0.000 description 1
- XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 1
- 230000006229 amino acid addition Effects 0.000 description 1
- 229960003896 aminopterin Drugs 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 210000003484 anatomy Anatomy 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 229940069428 antacid Drugs 0.000 description 1
- 239000003159 antacid agent Substances 0.000 description 1
- 229940124650 anti-cancer therapies Drugs 0.000 description 1
- 238000011230 antibody-based therapy Methods 0.000 description 1
- 238000011319 anticancer therapy Methods 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 210000000709 aorta Anatomy 0.000 description 1
- 230000006907 apoptotic process Effects 0.000 description 1
- 239000008365 aqueous carrier Substances 0.000 description 1
- 239000003125 aqueous solvent Substances 0.000 description 1
- 239000003886 aromatase inhibitor Substances 0.000 description 1
- 229940046844 aromatase inhibitors Drugs 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 210000003567 ascitic fluid Anatomy 0.000 description 1
- 235000010323 ascorbic acid Nutrition 0.000 description 1
- 229960005070 ascorbic acid Drugs 0.000 description 1
- 239000011668 ascorbic acid Substances 0.000 description 1
- 108010047857 aspartylglycine Proteins 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- 239000003613 bile acid Substances 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 238000007622 bioinformatic analysis Methods 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N biotin Natural products N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 1
- 229910052797 bismuth Inorganic materials 0.000 description 1
- JCXGWMGPZLAOME-UHFFFAOYSA-N bismuth atom Chemical compound [Bi] JCXGWMGPZLAOME-UHFFFAOYSA-N 0.000 description 1
- 108010009896 bone resorption factor Proteins 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 230000001126 calcilytic effect Effects 0.000 description 1
- GMRQFYUYWCNGIN-NKMMMXOESA-N calcitriol Chemical compound C1(/[C@@H]2CC[C@@H]([C@]2(CCC1)C)[C@@H](CCCC(C)(C)O)C)=C\C=C1\C[C@@H](O)C[C@H](O)C1=C GMRQFYUYWCNGIN-NKMMMXOESA-N 0.000 description 1
- 235000020964 calcitriol Nutrition 0.000 description 1
- 239000011612 calcitriol Substances 0.000 description 1
- 229960005084 calcitriol Drugs 0.000 description 1
- 230000003913 calcium metabolism Effects 0.000 description 1
- 229910001576 calcium mineral Inorganic materials 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- BPKIGYQJPYCAOW-FFJTTWKXSA-I calcium;potassium;disodium;(2s)-2-hydroxypropanoate;dichloride;dihydroxide;hydrate Chemical compound O.[OH-].[OH-].[Na+].[Na+].[Cl-].[Cl-].[K+].[Ca+2].C[C@H](O)C([O-])=O BPKIGYQJPYCAOW-FFJTTWKXSA-I 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000021523 carboxylation Effects 0.000 description 1
- 238000006473 carboxylation reaction Methods 0.000 description 1
- 201000011529 cardiovascular cancer Diseases 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000030833 cell death Effects 0.000 description 1
- 230000007910 cell fusion Effects 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 210000003679 cervix uteri Anatomy 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000010668 complexation reaction Methods 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 238000013270 controlled release Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 229960004544 cortisone Drugs 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 230000006866 deterioration Effects 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 238000006471 dimerization reaction Methods 0.000 description 1
- XEYBRNLFEZDVAW-ARSRFYASSA-N dinoprostone Chemical compound CCCCC[C@H](O)\C=C\[C@H]1[C@H](O)CC(=O)[C@@H]1C\C=C/CCCC(O)=O XEYBRNLFEZDVAW-ARSRFYASSA-N 0.000 description 1
- 229960002986 dinoprostone Drugs 0.000 description 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 230000007783 downstream signaling Effects 0.000 description 1
- 229940000406 drug candidate Drugs 0.000 description 1
- 210000001198 duodenum Anatomy 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 239000002158 endotoxin Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 208000001780 epistaxis Diseases 0.000 description 1
- 210000003617 erythrocyte membrane Anatomy 0.000 description 1
- 238000009164 estrogen replacement therapy Methods 0.000 description 1
- HQPMKSGTIOYHJT-UHFFFAOYSA-N ethane-1,2-diol;propane-1,2-diol Chemical compound OCCO.CC(O)CO HQPMKSGTIOYHJT-UHFFFAOYSA-N 0.000 description 1
- 235000019441 ethanol Nutrition 0.000 description 1
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- LVGKNOAMLMIIKO-QXMHVHEDSA-N ethyl oleate Chemical compound CCCCCCCC\C=C/CCCCCCCC(=O)OCC LVGKNOAMLMIIKO-QXMHVHEDSA-N 0.000 description 1
- 229940093471 ethyl oleate Drugs 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 201000005884 exanthem Diseases 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 102000013165 exonuclease Human genes 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
- 239000012530 fluid Substances 0.000 description 1
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 229960002949 fluorouracil Drugs 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 210000003958 hematopoietic stem cell Anatomy 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 238000002657 hormone replacement therapy Methods 0.000 description 1
- 102000058223 human VEGFA Human genes 0.000 description 1
- 210000004754 hybrid cell Anatomy 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 239000000017 hydrogel Substances 0.000 description 1
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 description 1
- 230000000705 hypocalcaemia Effects 0.000 description 1
- 210000003405 ileum Anatomy 0.000 description 1
- 230000036737 immune function Effects 0.000 description 1
- 230000008105 immune reaction Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000011261 inert gas Substances 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 230000008611 intercellular interaction Effects 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 108010088383 interleukin-6 receptor alpha Proteins 0.000 description 1
- 238000001361 intraarterial administration Methods 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000007913 intrathecal administration Methods 0.000 description 1
- 238000007914 intraventricular administration Methods 0.000 description 1
- XMBWDFGMSWQBCA-YPZZEJLDSA-N iodane Chemical compound [125IH] XMBWDFGMSWQBCA-YPZZEJLDSA-N 0.000 description 1
- 229940044173 iodine-125 Drugs 0.000 description 1
- UWKQSNNFCGGAFS-XIFFEERXSA-N irinotecan Chemical compound C1=C2C(CC)=C3CN(C(C4=C([C@@](C(=O)OC4)(O)CC)C=4)=O)C=4C3=NC2=CC=C1OC(=O)N(CC1)CCC1N1CCCCC1 UWKQSNNFCGGAFS-XIFFEERXSA-N 0.000 description 1
- 229960004768 irinotecan Drugs 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 210000001630 jejunum Anatomy 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 231100000518 lethal Toxicity 0.000 description 1
- 230000001665 lethal effect Effects 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 230000029226 lipidation Effects 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 230000033001 locomotion Effects 0.000 description 1
- OHSVLFRHMCKCQY-UHFFFAOYSA-N lutetium atom Chemical compound [Lu] OHSVLFRHMCKCQY-UHFFFAOYSA-N 0.000 description 1
- 230000002132 lysosomal effect Effects 0.000 description 1
- 230000002101 lytic effect Effects 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 230000014759 maintenance of location Effects 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
- 239000002609 medium Substances 0.000 description 1
- 102000006240 membrane receptors Human genes 0.000 description 1
- 108020004084 membrane receptors Proteins 0.000 description 1
- 230000009245 menopause Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 230000001394 metastastic effect Effects 0.000 description 1
- 208000037819 metastatic cancer Diseases 0.000 description 1
- 208000011575 metastatic malignant neoplasm Diseases 0.000 description 1
- 206010061289 metastatic neoplasm Diseases 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 239000004530 micro-emulsion Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 208000027361 mineral metabolism disease Diseases 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 238000010172 mouse model Methods 0.000 description 1
- 210000005088 multinucleated cell Anatomy 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 239000002105 nanoparticle Substances 0.000 description 1
- 239000007922 nasal spray Substances 0.000 description 1
- 229940097496 nasal spray Drugs 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000020395 negative regulation of osteoclast differentiation Effects 0.000 description 1
- 239000012457 nonaqueous media Substances 0.000 description 1
- 230000000683 nonmetastatic effect Effects 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- XXUPLYBCNPLTIW-UHFFFAOYSA-N octadec-7-ynoic acid Chemical compound CCCCCCCCCCC#CCCCCCC(O)=O XXUPLYBCNPLTIW-UHFFFAOYSA-N 0.000 description 1
- 235000008390 olive oil Nutrition 0.000 description 1
- 239000004006 olive oil Substances 0.000 description 1
- 150000002895 organic esters Chemical class 0.000 description 1
- 230000011164 ossification Effects 0.000 description 1
- 201000008482 osteoarthritis Diseases 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 210000003101 oviduct Anatomy 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000001991 pathophysiological effect Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- WVDDGKGOMKODPV-ZQBYOMGUSA-N phenyl(114C)methanol Chemical compound O[14CH2]C1=CC=CC=C1 WVDDGKGOMKODPV-ZQBYOMGUSA-N 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 229920001983 poloxamer Polymers 0.000 description 1
- 229920001993 poloxamer 188 Polymers 0.000 description 1
- 229920001987 poloxamine Polymers 0.000 description 1
- 229920000747 poly(lactic acid) Polymers 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 239000004633 polyglycolic acid Substances 0.000 description 1
- 239000004626 polylactic acid Substances 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 1
- 208000001685 postmenopausal osteoporosis Diseases 0.000 description 1
- 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 1
- 229960004618 prednisone Drugs 0.000 description 1
- 210000005238 principal cell Anatomy 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- XEYBRNLFEZDVAW-UHFFFAOYSA-N prostaglandin E2 Natural products CCCCCC(O)C=CC1C(O)CC(=O)C1CC=CCCCC(O)=O XEYBRNLFEZDVAW-UHFFFAOYSA-N 0.000 description 1
- 239000011253 protective coating Substances 0.000 description 1
- 230000012846 protein folding Effects 0.000 description 1
- 230000018883 protein targeting Effects 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 239000002096 quantum dot Substances 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 206010037844 rash Diseases 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- WUAPFZMCVAUBPE-IGMARMGPSA-N rhenium-186 Chemical compound [186Re] WUAPFZMCVAUBPE-IGMARMGPSA-N 0.000 description 1
- 239000012266 salt solution Substances 0.000 description 1
- SIXSYDAISGFNSX-NJFSPNSNSA-N scandium-47 Chemical compound [47Sc] SIXSYDAISGFNSX-NJFSPNSNSA-N 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 238000007423 screening assay Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 239000004017 serum-free culture medium Substances 0.000 description 1
- 102000036068 sialic acid binding proteins Human genes 0.000 description 1
- 108091000315 sialic acid binding proteins Proteins 0.000 description 1
- 230000009450 sialylation Effects 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- 231100000046 skin rash Toxicity 0.000 description 1
- 239000004055 small Interfering RNA Substances 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- HRZFUMHJMZEROT-UHFFFAOYSA-L sodium disulfite Chemical compound [Na+].[Na+].[O-]S(=O)S([O-])(=O)=O HRZFUMHJMZEROT-UHFFFAOYSA-L 0.000 description 1
- 229940001584 sodium metabisulfite Drugs 0.000 description 1
- 235000010262 sodium metabisulphite Nutrition 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 230000010473 stable expression Effects 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 238000005728 strengthening Methods 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 238000013268 sustained release Methods 0.000 description 1
- 239000012730 sustained-release form Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 229960001603 tamoxifen Drugs 0.000 description 1
- OGBMKVWORPGQRR-UMXFMPSGSA-N teriparatide Chemical compound C([C@H](NC(=O)[C@H](CCSC)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@@H](N)CO)C(C)C)[C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1N=CNC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1N=CNC=1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CNC=N1 OGBMKVWORPGQRR-UMXFMPSGSA-N 0.000 description 1
- 229960005460 teriparatide Drugs 0.000 description 1
- 210000001550 testis Anatomy 0.000 description 1
- 229940126622 therapeutic monoclonal antibody Drugs 0.000 description 1
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 1
- 229940033663 thimerosal Drugs 0.000 description 1
- 108060008226 thioredoxin Proteins 0.000 description 1
- 229940094937 thioredoxin Drugs 0.000 description 1
- 229940113082 thymine Drugs 0.000 description 1
- 210000001541 thymus gland Anatomy 0.000 description 1
- 210000001685 thyroid gland Anatomy 0.000 description 1
- 239000005495 thyroid hormone Substances 0.000 description 1
- 229940036555 thyroid hormone Drugs 0.000 description 1
- 239000003104 tissue culture media Substances 0.000 description 1
- 239000008181 tonicity modifier Substances 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 210000003437 trachea Anatomy 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 230000017105 transposition Effects 0.000 description 1
- 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 1
- 230000004614 tumor growth Effects 0.000 description 1
- 231100000397 ulcer Toxicity 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 230000003827 upregulation Effects 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 238000010200 validation analysis Methods 0.000 description 1
- 235000015112 vegetable and seed oil Nutrition 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 239000001993 wax Substances 0.000 description 1
Classifications
-
- 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
- C07K16/2803—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/70—Carbohydrates; Sugars; Derivatives thereof
- A61K31/7088—Compounds having three or more nucleosides or nucleotides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/70—Carbohydrates; Sugars; Derivatives thereof
- A61K31/7088—Compounds having three or more nucleosides or nucleotides
- A61K31/713—Double-stranded nucleic acids or oligonucleotides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/18—Growth factors; Growth regulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
- A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/30—Macromolecular organic or inorganic compounds, e.g. inorganic polyphosphates
- A61K47/42—Proteins; Polypeptides; Degradation products thereof; Derivatives thereof, e.g. albumin, gelatin or zein
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
- A61K47/6835—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment the modifying agent being an antibody or an immunoglobulin bearing at least one antigen-binding site
- A61K47/6849—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment the modifying agent being an antibody or an immunoglobulin bearing at least one antigen-binding site the antibody targeting a receptor, a cell surface antigen or a cell surface determinant
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K48/00—Medicinal preparations containing genetic material which is inserted into cells of the living body to treat genetic diseases; Gene therapy
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K49/00—Preparations for testing in vivo
- A61K49/06—Nuclear magnetic resonance [NMR] contrast preparations; Magnetic resonance imaging [MRI] contrast preparations
- A61K49/08—Nuclear magnetic resonance [NMR] contrast preparations; Magnetic resonance imaging [MRI] contrast preparations characterised by the carrier
- A61K49/10—Organic compounds
- A61K49/14—Peptides, e.g. proteins
- A61K49/16—Antibodies; Immunoglobulins; Fragments thereof
-
- 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
-
- 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
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
-
- 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
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
- A61P19/10—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease for osteoporosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/475—Growth factors; Growth regulators
-
- 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
-
- 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
- C07K16/22—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against growth factors ; against growth regulators
-
- 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
-
- 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
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
-
- 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
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/574—Immunoassay; Biospecific binding assay; Materials therefor for cancer
- G01N33/57407—Specifically defined cancers
-
- 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
- G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/33—Crossreactivity, e.g. for species or epitope, or lack of said crossreactivity
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/54—F(ab')2
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
- C07K2317/62—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising only variable region components
- C07K2317/622—Single chain antibody (scFv)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- 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
- G01N2800/108—Osteoporosis
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Pharmacology & Pharmacy (AREA)
- Epidemiology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Cell Biology (AREA)
- Hematology (AREA)
- Biomedical Technology (AREA)
- Urology & Nephrology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Physical Education & Sports Medicine (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Food Science & Technology (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Rheumatology (AREA)
- General Chemical & Material Sciences (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Mycology (AREA)
- Hospice & Palliative Care (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AU2014224071A AU2014224071A1 (en) | 2009-10-06 | 2014-09-11 | Siglec 15 antibodies in treating bone loss-related disease |
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US24896009P | 2009-10-06 | 2009-10-06 | |
| US61/248,960 | 2009-10-06 | ||
| US12/580,943 | 2009-10-16 | ||
| US12/580,943 US8168181B2 (en) | 2006-02-13 | 2009-10-16 | Methods of impairing osteoclast differentiation using antibodies that bind siglec-15 |
| PCT/CA2010/001586 WO2011041894A1 (en) | 2009-10-06 | 2010-10-06 | Siglec 15 antibodies in treating bone loss-related disease |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2014224071A Division AU2014224071A1 (en) | 2009-10-06 | 2014-09-11 | Siglec 15 antibodies in treating bone loss-related disease |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| AU2010305281A1 AU2010305281A1 (en) | 2012-05-03 |
| AU2010305281B2 AU2010305281B2 (en) | 2014-06-12 |
| AU2010305281C1 true AU2010305281C1 (en) | 2014-12-04 |
Family
ID=43856338
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2010305281A Ceased AU2010305281C1 (en) | 2009-10-06 | 2010-10-06 | Siglec 15 antibodies in treating bone loss-related disease |
| AU2014224071A Abandoned AU2014224071A1 (en) | 2009-10-06 | 2014-09-11 | Siglec 15 antibodies in treating bone loss-related disease |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2014224071A Abandoned AU2014224071A1 (en) | 2009-10-06 | 2014-09-11 | Siglec 15 antibodies in treating bone loss-related disease |
Country Status (13)
| Country | Link |
|---|---|
| US (6) | US8168181B2 (enExample) |
| EP (1) | EP2486060A4 (enExample) |
| JP (2) | JP5855569B2 (enExample) |
| KR (1) | KR20120086297A (enExample) |
| CN (2) | CN102803293B (enExample) |
| AU (2) | AU2010305281C1 (enExample) |
| BR (1) | BR112012007860A2 (enExample) |
| CA (2) | CA2870980A1 (enExample) |
| IL (1) | IL218985A0 (enExample) |
| MX (1) | MX2012004084A (enExample) |
| NZ (1) | NZ599193A (enExample) |
| RU (1) | RU2596392C2 (enExample) |
| WO (1) | WO2011041894A1 (enExample) |
Families Citing this family (46)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8168181B2 (en) * | 2006-02-13 | 2012-05-01 | Alethia Biotherapeutics, Inc. | Methods of impairing osteoclast differentiation using antibodies that bind siglec-15 |
| DK1994155T4 (da) † | 2006-02-13 | 2022-07-25 | Daiichi Sankyo Co Ltd | Polynukleotid- og polypeptidsekvenser involveret i fremgangsmåden med knogleremodellering |
| CN103483169A (zh) * | 2007-09-28 | 2014-01-01 | 第一三共株式会社 | 用于制备双环γ-氨基酸衍生物的中间体 |
| SG10201605897RA (en) * | 2007-10-11 | 2016-09-29 | Daiichi Sankyo Co Ltd | ANTIBODY TARGETING OSTEOCLAST-RELATED PROTEIN Siglec-15 |
| JP5557292B2 (ja) | 2009-03-26 | 2014-07-23 | 第一三共株式会社 | 二環性γ−アミノ酸誘導体の製造方法 |
| MX2011007342A (es) | 2009-04-09 | 2011-07-21 | Daiichi Sankyo Co Ltd | Anticuerpo anti-lectina similar a inmunoglobulina de union a acido sialico-15. |
| BR112013008255A2 (pt) | 2010-10-05 | 2018-09-25 | Daiichi Sankyo Co Ltd | anticorpo isolado ou um fragmento funcional do mesmo, uso de um anticorpo isolado ou de um fragmento funcional do mesmo, composição farmacêutica, polinucleotídeo, vetor, célula transformada, e, método para produzir anticorpo |
| CA2848074A1 (en) | 2011-09-09 | 2013-03-14 | Medimmune Limited | Anti-siglec-15 antibodies and uses thereof |
| US9003797B2 (en) * | 2011-11-02 | 2015-04-14 | E L Du Pont De Nemours And Company | Use of compositions comprising 1,1,1,2,3-pentafluoropropane and optionally Z-1,1,1,4,4,4-hexafluoro-2-butene in power cycles |
| KR20140138215A (ko) | 2012-03-30 | 2014-12-03 | 다이이찌 산쿄 가부시키가이샤 | 신규 항 Siglec-15 항체 |
| NZ631509A (en) * | 2012-03-30 | 2016-09-30 | Daiichi Sankyo Co Ltd | Cdr-modified anti-siglec-15 antibody |
| US9493562B2 (en) * | 2012-07-19 | 2016-11-15 | Alethia Biotherapeutics Inc. | Anti-Siglec-15 antibodies |
| ES2729797T3 (es) * | 2013-12-20 | 2019-11-06 | Dev Ct Biotechnology | Anticuerpos específicos de la alfa-enolasa y métodos de uso en terapias contra el cáncer |
| US9382331B2 (en) * | 2013-12-27 | 2016-07-05 | Development Center For Biotechnology | Alpha-enolase specific antibodies and methods of uses in cancer therapy |
| US20170129956A1 (en) * | 2014-06-18 | 2017-05-11 | Daiichi Sankyo Company, Limited | Anti-siglec-15 antibodies for use in treatment of osteogenesis imperfecta |
| FR3024731B1 (fr) * | 2014-08-08 | 2019-06-14 | International - Drug - Development - Biotech | Anticorps anti-ck8 pour utilisation dans le traitement des cancers |
| US9616114B1 (en) | 2014-09-18 | 2017-04-11 | David Gordon Bermudes | Modified bacteria having improved pharmacokinetics and tumor colonization enhancing antitumor activity |
| CN107427563B (zh) * | 2014-12-31 | 2021-03-02 | 财团法人生物技术开发中心 | 人源化α-烯醇酶特异性抗体及用于癌症治疗的方法 |
| US9527922B2 (en) | 2014-12-31 | 2016-12-27 | Development Center For Biotechnology | Humanized alpha-enolase specific antibodies and methods of uses in cancer therapy |
| US10676723B2 (en) | 2015-05-11 | 2020-06-09 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| KR102810368B1 (ko) * | 2015-11-10 | 2025-05-19 | 예일 유니버시티 | 자가면역 질환 및 암을 치료하기 위한 조성물 및 방법 |
| CN105367658B (zh) * | 2015-12-02 | 2020-06-16 | 朱进 | 人源抗唾液酸结合免疫球蛋白样凝集素-9的抗体IgG及其应用 |
| EP3515478B1 (en) * | 2016-09-21 | 2024-02-28 | Nextcure, Inc. | Antibodies for siglec-15 and methods of use thereof |
| US11129906B1 (en) | 2016-12-07 | 2021-09-28 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| US11180535B1 (en) | 2016-12-07 | 2021-11-23 | David Gordon Bermudes | Saccharide binding, tumor penetration, and cytotoxic antitumor chimeric peptides from therapeutic bacteria |
| CN109912716B (zh) * | 2017-12-13 | 2022-08-23 | 凯惠科技发展(上海)有限公司 | 一种egfr抗体及其制备方法和应用 |
| JP6544669B1 (ja) | 2018-03-16 | 2019-07-17 | ディヴェロップメント センター フォー バイオテクノロジー | アルファエノラーゼに特異的な抗体及びその使用 |
| GB201901710D0 (en) * | 2019-02-07 | 2019-03-27 | Nordic Bioscience As | Collagen type 23 assay |
| CN110386982A (zh) * | 2019-04-09 | 2019-10-29 | 广东三九脑科医院 | 鼠抗人Siglec-15蛋白单克隆抗体制备及其用途 |
| WO2021142260A1 (en) * | 2020-01-10 | 2021-07-15 | Dyne Therapeutics, Inc. | Muscle targeting complexes and uses thereof for modulation of acvr1 |
| CN111378043B (zh) * | 2020-02-19 | 2021-02-09 | 南京医科大学 | 一种具有中和作用的人鼠嵌合抗Siglec-15全分子IgG及其制备方法和应用 |
| EP4126938A4 (en) * | 2020-03-27 | 2024-04-10 | Biosion, Inc. | ANTIBODIES BINDING TO SIGLEC15 AND THEIR USES |
| CN112625131B (zh) * | 2020-08-10 | 2021-08-17 | 北京鼎成肽源生物技术有限公司 | 抗人c-Met人鼠嵌合单克隆抗体及其应用 |
| WO2022123394A1 (en) * | 2020-12-08 | 2022-06-16 | Guizhou Sinorda Biotechnology Co. Ltd. | Modified t cells for adoptive immunotherapy |
| CN112625132B (zh) * | 2021-01-15 | 2022-08-02 | 沈阳荣欣生物制药科技有限公司 | 纳米抗体及其编码基因、表达载体、宿主细胞和应用 |
| IL305409A (en) * | 2021-02-23 | 2023-10-01 | Shanghai Jemincare Pharmaceuticals Co Ltd | Preparation of SIGLEC-15 binding protein and its use |
| CN114957468A (zh) * | 2021-02-25 | 2022-08-30 | 石药集团巨石生物制药有限公司 | 一种抗Siglec15抗体及其用途 |
| KR20230158058A (ko) * | 2021-03-19 | 2023-11-17 | 엘피스 바이오파마슈티컬즈 | 시알산-결합 ig-유사 렉틴 15에 특이적인 항체 및 이의 용도 |
| CN112979761B (zh) * | 2021-03-19 | 2021-12-10 | 江苏元本生物科技有限公司 | 一种靶向Siglec-15的噬菌体多肽 |
| CN112961217B (zh) * | 2021-03-19 | 2022-11-08 | 江苏元本生物科技有限公司 | 一种靶向Siglec-15的噬菌体多肽 |
| CN117203241A (zh) * | 2021-04-22 | 2023-12-08 | 上海医药集团股份有限公司 | 抗Siglec15抗体及其用途 |
| CN114591434B (zh) * | 2021-04-30 | 2023-02-28 | 杭州邦顺制药有限公司 | 抗Siglec15抗体及其制备方法和用途 |
| CN115947855B (zh) * | 2022-05-20 | 2023-10-27 | 杭州邦顺制药有限公司 | 抗cd24抗体的制备及其用途 |
| GB202209786D0 (en) * | 2022-07-04 | 2022-08-17 | Ucl Business Ltd | B7H3 Binders |
| CN120303296A (zh) * | 2022-10-02 | 2025-07-11 | 瑞美德生物医药科技有限公司 | C-c趋化因子受体8型(ccr8)拮抗剂抗体 |
| CN117903311B (zh) * | 2024-03-20 | 2024-10-25 | 湖南卓润生物科技有限公司 | sST2特异性结合蛋白及其制备方法和应用 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007093042A1 (en) * | 2006-02-13 | 2007-08-23 | Alethia Biotherapeutics Inc. | Polynucleotides and polypeptide sequences involved in the process of bone remodeling |
| WO2009048072A1 (ja) * | 2007-10-11 | 2009-04-16 | Daiichi Sankyo Company, Limited | 破骨細胞関連蛋白質Siglec-15を標的とした抗体 |
Family Cites Families (218)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6018030A (en) * | 1986-11-04 | 2000-01-25 | Protein Polymer Technologies, Inc. | Peptides comprising repetitive units of amino acids and DNA sequences encoding the same |
| US5589458A (en) | 1992-11-13 | 1996-12-31 | Thomas Jefferson University | Compounds that inhibit T cell proliferation and methods for using the same |
| US5817303A (en) * | 1995-05-05 | 1998-10-06 | Protein Polymer Technologies, Inc. | Bonding together tissue with adhesive containing polyfunctional crosslinking agent and protein polymer |
| US5712127A (en) | 1996-04-29 | 1998-01-27 | Genescape Inc. | Subtractive amplification |
| US6617434B1 (en) | 1996-05-31 | 2003-09-09 | North Shore Long Island Jewish Research Institute | Identificiaton of differentially methylated and mutated nucleic acids |
| US5871917A (en) | 1996-05-31 | 1999-02-16 | North Shore University Hospital Research Corp. | Identification of differentially methylated and mutated nucleic acids |
| US7411051B2 (en) * | 1997-03-07 | 2008-08-12 | Human Genome Sciences, Inc. | Antibodies to HDPPA04 polypeptide |
| US6057098A (en) | 1997-04-04 | 2000-05-02 | Biosite Diagnostics, Inc. | Polyvalent display libraries |
| ES2263204T5 (es) * | 1997-04-15 | 2013-10-14 | Daiichi Sankyo Company, Limited | Nueva proteína y proceso para producir la misma |
| FR2767337B1 (fr) | 1997-08-14 | 2002-07-05 | Pasteur Institut | Sequences nucleiques de polypeptides exportes de mycobacteri es, vecteurs les comprenant et applications au diagnostic et a la prevention de la tuberculose |
| NZ527414A (en) | 1998-03-04 | 2005-07-29 | Genencor Int | Modified forms of pullulanase |
| US6472367B1 (en) | 1998-05-05 | 2002-10-29 | Adherex Technologies, Inc. | Compounds and methods for modulating OB-cadherin mediated cell adhesion |
| US7060433B1 (en) * | 1999-11-12 | 2006-06-13 | Rigel Pharmaceuticals, Inc. | Methods and compositions for screening using diphtheria toxin constructs |
| US7090976B2 (en) * | 1999-11-10 | 2006-08-15 | Rigel Pharmaceuticals, Inc. | Methods and compositions comprising Renilla GFP |
| US7534579B2 (en) * | 1998-06-30 | 2009-05-19 | Millennium Pharmaceuticals, Inc. | 14273 receptor, a novel G-protein coupled receptor |
| US7662409B2 (en) * | 1998-09-25 | 2010-02-16 | Gel-Del Technologies, Inc. | Protein matrix materials, devices and methods of making and using thereof |
| US7488590B2 (en) * | 1998-10-23 | 2009-02-10 | Amgen Inc. | Modified peptides as therapeutic agents |
| US20030104526A1 (en) | 1999-03-24 | 2003-06-05 | Qiang Liu | Position dependent recognition of GNN nucleotide triplets by zinc fingers |
| US6943235B1 (en) * | 1999-04-12 | 2005-09-13 | Agensys, Inc. | Transmembrane protein expressed in prostate cancer |
| US6942981B1 (en) | 1999-05-14 | 2005-09-13 | Arbor Vita Corporation | Method of determining interactions with PDZ-domain polypeptides |
| US20090175821A1 (en) * | 1999-05-17 | 2009-07-09 | Bridon Dominique P | Modified therapeutic peptides with extended half-lives in vivo |
| EP1200109A4 (en) | 1999-07-19 | 2005-06-15 | Epimmune Inc | USE OF PEPTIDE NUCLEIC ACID COMPOUNDS TO TRIGGER CELLULAR IMMUNE RESPONSES TO HEPATITIS C |
| ES2360155T3 (es) * | 2000-01-26 | 2011-06-01 | Agensys, Inc. | 84p2a9: una proteína específica de próstata y testículos altamente expresada en el cáncer de próstata. |
| US7585839B2 (en) | 2000-02-23 | 2009-09-08 | Zealand Pharma A/S | Medical uses of intercellular communication facilitating compounds |
| US7378248B2 (en) | 2000-03-06 | 2008-05-27 | Rigel Pharmaceuticals, Inc. | In vivo production of cyclic peptides for inhibiting protein-protein interaction |
| EP1300418A1 (en) * | 2001-10-04 | 2003-04-09 | Erasmus Universiteit Rotterdam | Gene regulation by oligopeptides |
| US7358330B2 (en) | 2001-03-29 | 2008-04-15 | Biotempt B.V. | Immunoregulatory compositions |
| TWI318983B (en) | 2000-05-02 | 2010-01-01 | Uab Research Foundation | An antibody selective for a tumor necrosis factor-related apoptosis-inducing ligand receptor and uses thereof |
| US6635448B2 (en) * | 2000-08-21 | 2003-10-21 | Clonexdevelopment, Inc. | Methods and compositions for increasing protein yield from a cell culture |
| US7358353B2 (en) | 2000-08-22 | 2008-04-15 | Agensys, Inc. | Nucleic acid and corresponding protein named 158P1D7 useful in the treatment and detection of bladder and other cancers |
| CA2421200A1 (en) | 2000-09-08 | 2002-03-14 | Board Of Regents, The University Of Texas System | Adenoviral targeting and manipulation of immune system response using targeting peptides |
| US7608704B2 (en) | 2000-11-08 | 2009-10-27 | Incyte Corporation | Secreted proteins |
| CA2428140A1 (en) | 2000-11-08 | 2002-05-16 | Incyte Genomics, Inc. | Secreted proteins |
| JP4173733B2 (ja) * | 2000-12-12 | 2008-10-29 | アンジオラボ・インコーポレイテッド | 抗−血管新生およびマトリックスメタロプロテイナーゼ阻害活性を有するメリッサ葉抽出物を含む組成物 |
| US7459539B2 (en) | 2000-12-15 | 2008-12-02 | Agensys, Inc. | Antibody that binds zinc transporter protein 108P5H8 |
| US20030133939A1 (en) | 2001-01-17 | 2003-07-17 | Genecraft, Inc. | Binding domain-immunoglobulin fusion proteins |
| US7754208B2 (en) | 2001-01-17 | 2010-07-13 | Trubion Pharmaceuticals, Inc. | Binding domain-immunoglobulin fusion proteins |
| EP1369479A4 (en) | 2001-02-15 | 2004-12-08 | Mochida Pharm Co Ltd | "NEW CELL ADHESION MOLECULES SPECIFIC FOR ACTIVATED LEUKOCYTES" |
| EP2105141B1 (en) | 2001-03-28 | 2012-08-08 | Helix Biomedix, Inc. | Short bioactive peptides and methods for their use |
| US7736654B2 (en) | 2001-04-10 | 2010-06-15 | Agensys, Inc. | Nucleic acids and corresponding proteins useful in the detection and treatment of various cancers |
| US6967021B2 (en) | 2001-04-27 | 2005-11-22 | Trustees Of Tufts College | Use of Galectin-3 to promote the re-epithelialization of wounds |
| CA2446185C (en) | 2001-05-07 | 2013-06-18 | National Research Council Of Canada | Enhanced production of recombinant proteins by transient transfection of suspension-growing mammalian cells |
| WO2002102432A1 (en) * | 2001-06-15 | 2002-12-27 | Johns Hopkins Singapore Pte Ltd | Biofunctional fibers |
| DK2270052T3 (en) | 2001-06-26 | 2018-07-02 | Amgen Inc | Antibodies to OPGL |
| US7033991B2 (en) | 2001-07-16 | 2006-04-25 | Board Of Supervisors Of Louisiana State University And Agriculture And Mechanical College | Inhibiting furin with polybasic peptides |
| CA2652991A1 (en) | 2001-07-16 | 2003-11-13 | Caprotec Bioanalytics Gmbh | Capture compounds, collections thereof and methods for analyzing the proteome and complex compositions |
| US20090075377A1 (en) * | 2001-08-03 | 2009-03-19 | Arbor Vita Corporation | Molecular interactions in cells |
| US7402664B2 (en) | 2002-09-03 | 2008-07-22 | Genencor International, Inc. | Nucleic acids and expression vectors comprising carotenoid binding peptides |
| JP4120778B2 (ja) | 2001-09-26 | 2008-07-16 | 国立大学法人 奈良先端科学技術大学院大学 | 骨代謝異常疾患マーカー及びその利用 |
| US20050107588A1 (en) * | 2001-11-13 | 2005-05-19 | Duggan Brendan M. | Receptors and membrane-associated proteins |
| JP2003210166A (ja) | 2001-11-16 | 2003-07-29 | Sanyo Chem Ind Ltd | 変温動物由来細胞の細胞接着基材 |
| US20080194489A1 (en) * | 2001-12-21 | 2008-08-14 | Khan Nisar A | Treatment of iatrogenic disease |
| US7786084B2 (en) * | 2001-12-21 | 2010-08-31 | Biotempt B.V. | Treatment of burns |
| US7560433B2 (en) * | 2001-12-21 | 2009-07-14 | Biotempt B.V. | Treatment of multiple sclerosis (MS) |
| US20080242837A1 (en) | 2001-12-21 | 2008-10-02 | Khan Nisar A | Peptide compositions |
| US20080318871A1 (en) | 2001-12-21 | 2008-12-25 | Khan Nisar A | Treatment of neurological disorders |
| US7501391B2 (en) * | 2001-12-21 | 2009-03-10 | Biotempt B.V. | Treatment of transplant survival |
| US20080242618A1 (en) | 2001-12-21 | 2008-10-02 | Khan Nisar A | Stratification |
| AU2003201733B2 (en) | 2002-01-09 | 2008-11-06 | Xigen Sa | Cell-permeable peptide inhibitors of the JNK signal transduction pathway |
| US7514407B2 (en) * | 2002-03-04 | 2009-04-07 | Nymox Corporation | Spheron component peptides and pharmaceutical compositions |
| US8298606B2 (en) * | 2002-03-08 | 2012-10-30 | The Regents Of The University Of California | Methods and compositions for stabilizing the myocardium |
| KR20030076448A (ko) | 2002-03-21 | 2003-09-26 | 주식회사 코메드 | 항-rank 단클론 항체 및 이를 함유한 약학 조성물 |
| US7193069B2 (en) | 2002-03-22 | 2007-03-20 | Research Association For Biotechnology | Full-length cDNA |
| JP4761710B2 (ja) | 2002-04-05 | 2011-08-31 | アムジェン インコーポレイテッド | 選択的opgl経路インヒビターとしてのヒト抗opgl中和抗体 |
| US20040102608A1 (en) * | 2002-05-13 | 2004-05-27 | Cornell Research Foundation, Inc. | Multiblock copolymers having improved mechanical properties |
| AU2003239531A1 (en) * | 2002-05-17 | 2003-12-02 | Montana State University | Protein cages for the delivery of medical imaging and therapy |
| CN100532549C (zh) * | 2002-06-06 | 2009-08-26 | 肿瘤疗法科学股份有限公司 | 与人结肠癌相关的基因和多肽 |
| US7357929B2 (en) * | 2002-06-28 | 2008-04-15 | D. Collen Research Foundation Vzw | Placental growth factor as a target for the treatment of osteoporosis |
| CA2487528A1 (en) | 2002-07-24 | 2004-02-12 | Innogenetics N.V. | Prevention, treatment and diagnosis of diseases associated with beta-amyloid formation and/or aggregation |
| US20060135433A1 (en) * | 2002-10-08 | 2006-06-22 | Murray Christopher J | Phenolic binding peptides |
| US7572894B2 (en) | 2002-11-01 | 2009-08-11 | Trustees Of Tufts College | Templated native silk smectic gels |
| MXPA05005920A (es) | 2002-12-03 | 2006-03-17 | American Nat Red Cross | Ligandos de proteina prion y metodos de uso. |
| JP2004189848A (ja) | 2002-12-10 | 2004-07-08 | Giken:Kk | 炭化処理方法および炭化処理システム |
| US20060051879A9 (en) | 2003-01-16 | 2006-03-09 | Hubert Koster | Capture compounds, collections thereof and methods for analyzing the proteome and complex compositions |
| JP3906924B2 (ja) | 2003-02-28 | 2007-04-18 | 独立行政法人農業生物資源研究所 | 絹タンパクから細胞生育ペプチドの抽出と利用 |
| WO2004085633A1 (en) * | 2003-03-24 | 2004-10-07 | The University Of Hong Kong | A novel human virus causing severe acute respiratory syndrome (sars) and uses thereof |
| US7547512B2 (en) * | 2003-03-24 | 2009-06-16 | The University Of Hong Kong | High-throughput diagnostic assay for the human virus causing severe acute respiratory syndrome (SARS) |
| US7517529B2 (en) * | 2003-04-08 | 2009-04-14 | Biotempt B.V. | Treatment of type I diabetes |
| JP4698596B2 (ja) | 2003-04-10 | 2011-06-08 | タフツ ユニバーシティー | 濃縮された水性シルクフィブロイン溶液およびそれらの使用 |
| EP1627062A1 (en) * | 2003-05-14 | 2006-02-22 | Domantis Limited | A process for recovering polypeptides that unfold reversibly from a polypeptide repertoire |
| JP3915983B2 (ja) | 2003-05-27 | 2007-05-16 | ゼライス株式会社 | プロテアーゼ、このプロテアーゼをコードするdna、プロテアーゼの製造方法 |
| US7671011B2 (en) * | 2003-06-19 | 2010-03-02 | Yeda Research & Development Co. Ltd. | Antimicrobial and anticancer lipopeptides |
| US20050106667A1 (en) * | 2003-08-01 | 2005-05-19 | Genentech, Inc | Binding polypeptides with restricted diversity sequences |
| FR2860237B1 (fr) | 2003-09-30 | 2006-03-10 | Centre Nat Rech Scient | Polypeptide d'interaction comprenant un motif heptapeptidique et un domaine de penetration cellulaire |
| US20050118625A1 (en) * | 2003-10-02 | 2005-06-02 | Mounts William M. | Nucleic acid arrays for detecting gene expression associated with human osteoarthritis and human proteases |
| US20090226374A1 (en) | 2003-10-27 | 2009-09-10 | Health Aide, Inc. | Anaphylatoxins for detecting clinical conditions |
| US20050153333A1 (en) * | 2003-12-02 | 2005-07-14 | Sooknanan Roy R. | Selective terminal tagging of nucleic acids |
| AT412785B (de) * | 2003-12-04 | 2005-07-25 | Kungl Andreas J Dr | Gag-bindungsproteine |
| EP1544215A1 (en) | 2003-12-17 | 2005-06-22 | Institut National De La Sante Et De La Recherche Medicale (Inserm) | Human anti-idiotypic antibody fragments that mimic HER-2/neu |
| US20090227505A1 (en) | 2004-01-07 | 2009-09-10 | Biotempt B.V. | Methods and uses for protein breakdown products |
| WO2005066337A2 (en) * | 2004-01-09 | 2005-07-21 | Yissum Research Development Company Of The Hebrew University Of Jerusalem | Compounds, pharmaceutical compositions and therapeutic methods of preventing and treating diseases and disorders associated with amyloid fibril formation |
| US8338138B2 (en) * | 2004-01-28 | 2012-12-25 | The John Hopkins University | Methods for making and using molecular switches involving circular permutation |
| TWI359026B (en) | 2004-02-12 | 2012-03-01 | Sankyo Co | Pharmaceutical composition for the osteoclast rela |
| EP1716181B1 (en) | 2004-02-19 | 2009-12-16 | Genentech, Inc. | Cdr-repaired antibodies |
| EA200601575A1 (ru) | 2004-03-01 | 2007-06-29 | Пептера Фармасьютикалс Лтд. | Казеиновые пептиды и их терапевтическое применение |
| WO2005098043A2 (en) * | 2004-03-30 | 2005-10-20 | The President And Fellows Of Harvard College | Ligand-dependent protein splicing |
| AU2005233550B2 (en) * | 2004-04-08 | 2010-11-18 | Sangamo Therapeutics, Inc. | Treatment of neuropathic pain with zinc finger proteins |
| US7189697B2 (en) | 2004-04-13 | 2007-03-13 | Trustees Of Tufts College | Compositions and uses of a galectin for treatment of dry eye syndrome |
| WO2005109158A2 (en) * | 2004-05-05 | 2005-11-17 | Massachusetts Institute Of Technology | Methods and systems for generating peptides |
| JP2008505928A (ja) | 2004-07-08 | 2008-02-28 | アムジェン インコーポレーテッド | 治療用ペプチド |
| CA2573293A1 (en) | 2004-07-10 | 2006-02-16 | Alexion Pharmaceuticals, Inc. | Methods for discovering antibodies specific to cancer cells and antibodies discovered thereby |
| AT413946B (de) * | 2004-07-13 | 2006-07-15 | Mattner Frank Dr | Impfstoff gegen die alzheimer-krankheit |
| EP1784211A4 (en) | 2004-07-29 | 2010-06-30 | Novartis Vaccines & Diagnostic | IMMUNOGENIC COMPOSITIONS FOR GRAMPOSITIVE BACTERIA SUCH AS STREPTOCOCCUS AGALACTIAE |
| AU2005267734A1 (en) * | 2004-08-06 | 2006-02-09 | Sopherion Therapeutics, Inc. | Anti-angiogenic peptides and methods of use thereof |
| JP2006068378A (ja) | 2004-09-03 | 2006-03-16 | Terumo Corp | 血管内留置物 |
| US7265092B2 (en) * | 2004-09-30 | 2007-09-04 | Kai Pharmaceuticals, Inc. | Pharmaceutical formulation |
| AU2005293568B2 (en) * | 2004-10-13 | 2010-10-28 | Beth Israel Deaconess Medical Center Inc. | Improved adenoviral vectors and uses thereof |
| EP1812030A4 (en) * | 2004-10-14 | 2009-01-14 | Sopherion Therapeutics Inc | ANTI-ANGIOGENIC PEPTIDES AND METHODS OF USE THEREOF |
| EP3061461A1 (en) * | 2004-10-29 | 2016-08-31 | ratiopharm GmbH | Remodeling and glycopegylation of fibroblast growth factor (fgf) |
| CA2629751A1 (en) * | 2004-11-12 | 2006-05-18 | The University Of British Columbia | Antimicrobial peptides |
| WO2007046818A2 (en) | 2004-11-16 | 2007-04-26 | Board Of Regents, The University Of Texas System | Compositions and methods related to synchronous selection of homing peptides for multiple tissues by in vivo phage display |
| WO2006062776A2 (en) | 2004-11-29 | 2006-06-15 | The Regents Of The University Of California | Hydroxyapatite-binding peptides for bone growth and inhibition |
| US7947436B2 (en) | 2004-12-13 | 2011-05-24 | Alethia Biotherapeutics Inc. | Polynucleotides and polypeptide sequences involved in the process of bone remodeling |
| WO2006078746A2 (en) * | 2005-01-19 | 2006-07-27 | Mathew Mark Zuckerman | Method, compositions and classification for tumor diagnostics and treatment |
| AU2006210724A1 (en) * | 2005-02-03 | 2006-08-10 | Antitope Limited | Human antibodies and proteins |
| EP1853620B1 (en) * | 2005-02-09 | 2012-01-11 | Helix Biomedix, Inc. | Antimicrobial hexapeptides |
| EP1861498A4 (en) | 2005-03-17 | 2009-06-24 | Ca Nat Research Council | EXPRESSION VECTORS FOR TRANSIENT GENETIC EXPRESSION AND MAMMALIAN CELLS EXPRESSING THE SAME |
| US9162005B2 (en) | 2005-04-25 | 2015-10-20 | Arch Biosurgery, Inc. | Compositions for prevention of adhesions and other barrier applications |
| EP1874800A4 (en) * | 2005-04-26 | 2009-11-18 | Karyon Ctt Ltd | DIAGNOSTIC AND THERAPEUTIC AGENTS |
| US7964200B2 (en) | 2005-05-18 | 2011-06-21 | Children's Hospital & Research Center At Oakland | Methods and compositions for immunizing against Chlamydia infection |
| US8227573B2 (en) | 2005-05-20 | 2012-07-24 | University Of Kentucky Research Foundation | Utility of phylloplanins as antibiotics, selective fungicides and for enhancing microbial resistance in plants |
| US7528232B2 (en) * | 2005-05-20 | 2009-05-05 | The University Of Kentucky Research Foundation | Utility of phylloplanins as antibiotics, selective fungicides and for enhancing microbial resistance in crop plants |
| AU2006266609C1 (en) * | 2005-07-05 | 2011-10-27 | Biotempt B.V. | Treatment of tumors |
| JP4604184B2 (ja) | 2005-07-12 | 2010-12-22 | 独立行政法人産業技術総合研究所 | 新規糖鎖認識蛋白質及びその遺伝子 |
| WO2007019062A2 (en) | 2005-08-11 | 2007-02-15 | The Scripps Research Institute | Zinc finger binding domains for cnn |
| US8445641B2 (en) | 2005-08-22 | 2013-05-21 | The United States Of America As Represented By The Secretary Of The Air Force | Nanocomposites of repeat sequence proteins and phyllosilicate clays and their preparation |
| WO2007027954A2 (en) | 2005-08-30 | 2007-03-08 | Children's Hospital & Research Center At Oakland | Methods for identifying an epitope of a polypeptide, chlamydial antigenic polypeptides identified thereby, and methods of use thereof |
| US20090275503A1 (en) | 2005-09-22 | 2009-11-05 | Yeda Research And Developent Co., Ltd. At The Weizman Institute Of Science | Diastereomeric peptides for modulating t cell immunity |
| AU2006294663B2 (en) | 2005-09-26 | 2012-03-22 | Medarex, Inc. | Human monoclonal antibodies to CD70 |
| US7846445B2 (en) | 2005-09-27 | 2010-12-07 | Amunix Operating, Inc. | Methods for production of unstructured recombinant polymers and uses thereof |
| US20090099031A1 (en) * | 2005-09-27 | 2009-04-16 | Stemmer Willem P | Genetic package and uses thereof |
| US8137670B2 (en) * | 2005-09-29 | 2012-03-20 | Medimmune, Llc | Method of identifying membrane IgE specific antibodies and use thereof for targeting IgE producing precursor cells |
| JP5047978B2 (ja) | 2005-10-13 | 2012-10-10 | バイオコン・リミテッド | インスリン複合体の調製のための方法 |
| US7575876B2 (en) * | 2005-10-27 | 2009-08-18 | The University Of Washington | Biomarkers for neurodegenerative disorders |
| US7901942B2 (en) * | 2005-11-08 | 2011-03-08 | Tohoku University | Method of quantifying membrane protein by mass spectrometry using peptide selection criteria |
| UA96139C2 (uk) | 2005-11-08 | 2011-10-10 | Дженентек, Інк. | Антитіло до нейропіліну-1 (nrp1) |
| US8252338B2 (en) * | 2005-11-10 | 2012-08-28 | The Regents Of The University Of California | Synthetic LDL as targeted drug delivery vehicle |
| JP2009520463A (ja) | 2005-11-28 | 2009-05-28 | ザ スクリプス リサーチ インスティテュート | Tnnのための亜鉛フィンガー結合ドメイン |
| GB0524313D0 (en) | 2005-11-29 | 2006-01-04 | Imp College Innovations Ltd | Particles |
| KR100838715B1 (ko) | 2005-12-16 | 2008-06-16 | 국립암센터 | 트란스글루타미나제를 억제하는 펩타이드 |
| US8168181B2 (en) | 2006-02-13 | 2012-05-01 | Alethia Biotherapeutics, Inc. | Methods of impairing osteoclast differentiation using antibodies that bind siglec-15 |
| EP1986611B1 (en) | 2006-02-23 | 2013-05-01 | Danisco US Inc. | Repeat sequence protein polymer nanoparticles optionally containing active agents and their preparation |
| WO2007102346A1 (ja) * | 2006-02-28 | 2007-09-13 | Japan Science And Technology Agency | グルカン量を低減させることなくリグニン量およびセルロース量を低減させた植物体およびその生産方法、並びにこれらの利用 |
| US7501557B1 (en) * | 2006-02-28 | 2009-03-10 | University Of Kentucky Research Foundation | Method utilizing the tobacco phylloplanin promoter for expression of nucleic acids as gene products directed to aerial surfaces of plants |
| CA2645277A1 (en) | 2006-03-09 | 2007-09-13 | Wadih Arap | Compositions and methods based on peptide binding profiling |
| WO2007108205A1 (ja) * | 2006-03-17 | 2007-09-27 | Sanyo Chemical Industries, Ltd. | 細胞培養用担体 |
| WO2007111952A2 (en) | 2006-03-22 | 2007-10-04 | The Scripps Research Institute | Method of preparing glycopeptides |
| JP2009532027A (ja) | 2006-03-28 | 2009-09-10 | バイオジェン・アイデック・エムエイ・インコーポレイテッド | 抗igf−1r抗体およびその使用 |
| JO3324B1 (ar) | 2006-04-21 | 2019-03-13 | Amgen Inc | مركبات علاجية مجففة بالتبريد تتعلق بالعصارة الهضمية |
| CA2652247C (en) | 2006-05-08 | 2015-11-17 | Adaerata, Limited Partnership | Chimeric pcsk9 proteins, cells comprising same, and assays using same |
| FR2900826B1 (fr) | 2006-05-12 | 2008-08-15 | Soc Extraction Principes Actif | Utilisation de peptides en tant que principes actifs amincissants. |
| WO2007146319A2 (en) | 2006-06-13 | 2007-12-21 | Symphony Medical, Inc. | Methods and apparatus for using polymer-based beads and hydrogels for cardiac applications |
| KR20090031938A (ko) | 2006-07-05 | 2009-03-30 | 더 스크립스 리서치 인스티튜트 | 방향성 진화로 촉매 작용을 최적화시킨 키메라 징크 핑거 리컴비나제 |
| MX2008016352A (es) | 2006-07-08 | 2009-04-17 | Univ Kentucky Res Found | Analisis diagnostico para cancer de pulmon. |
| AU2007284651B2 (en) | 2006-08-09 | 2014-03-20 | Institute For Systems Biology | Organ-specific proteins and methods of their use |
| CL2007002502A1 (es) * | 2006-08-31 | 2008-05-30 | Hoffmann La Roche | Variantes del factor de crecimiento similar a insulina-1 humano (igf-1) pegilados en lisina; metodo de produccion; proteina de fusion que la comprende; y su uso para tratar la enfermedad de alzheimer. |
| JP2008094822A (ja) | 2006-09-15 | 2008-04-24 | Univ Of Tokyo | セルロース結合性ペプチドおよびその製造方法 |
| WO2008055225A2 (en) * | 2006-10-31 | 2008-05-08 | Musc Foundation For Research Development | Systems and methods for in vivo measurement of interstitial biological activity, processes and/or compositions |
| CA2668640A1 (en) | 2006-11-01 | 2008-05-29 | George Mason Intellectual Properties, Inc. | Biomarkers for neurological conditions |
| ITTO20060852A1 (it) * | 2006-11-30 | 2008-06-01 | Univ Degli Studi Torino | Peptidi metastasi-specifici e loro applicazioni diagnostiche e terapeutiche |
| AU2008206077A1 (en) * | 2007-01-19 | 2008-07-24 | Kai Pharmaceuticals, Inc. | Modifications of peptide compositions to increase stability and delivery efficiency |
| US9175422B2 (en) * | 2007-01-22 | 2015-11-03 | The United States Of America As Represented By The Secretary Of The Army | Polymer-micelle complex as an aid to electrospinning |
| AU2008211854C1 (en) | 2007-01-29 | 2014-01-23 | Procell Therapeutics Inc. | Novel macromolecule transduction domains and methods for identification and uses thereof |
| EP2111413A2 (en) | 2007-02-16 | 2009-10-28 | Genetech, Inc. | Htra1-pdz and htra3-pdz modulators |
| DK2146733T3 (da) | 2007-03-14 | 2021-01-11 | Arch Biosurgery Inc | Treatment of leaky or damaged tight junctions and enhancing extracellular matrix |
| WO2008112904A2 (en) | 2007-03-15 | 2008-09-18 | Invitrogen Corporation | Adhering surfaces |
| ES2449753T3 (es) | 2007-03-19 | 2014-03-21 | National Research Council Of Canada | Proteínas de fusión que comprenden dos dominios de unión tgf-beta |
| WO2008116468A2 (en) | 2007-03-26 | 2008-10-02 | Dako Denmark A/S | Mhc peptide complexes and uses thereof in infectious diseases |
| JP2008263955A (ja) | 2007-03-29 | 2008-11-06 | Sanyo Chem Ind Ltd | 無血清培地 |
| US20080306001A1 (en) | 2007-04-04 | 2008-12-11 | Anzelika Liik | Transcriptional modulation of extracellular matrix (ecm) of dermal fibroblasts |
| WO2008137122A2 (en) * | 2007-05-04 | 2008-11-13 | Shiloh Laoratories, Inc. | Inducing premature senescence to stabilize stem cell feeder layer cells |
| US8097581B2 (en) * | 2007-05-10 | 2012-01-17 | Grant Industries Inc. | Anti-wrinkle cosmetic composition |
| WO2008151146A2 (en) * | 2007-06-01 | 2008-12-11 | Digitab, Inc. | Peptide arrays and methods of use |
| EP2009023A1 (en) | 2007-06-04 | 2008-12-31 | Rentschler Beteiligungs GmbH | Novel peptides and their use for the treatment of edema |
| JP5328780B2 (ja) * | 2007-06-13 | 2013-10-30 | エフ エム シー コーポレーション | アルギネート被覆多糖ゲル含有発泡体複合物、その製法および用途 |
| US20090017460A1 (en) * | 2007-06-15 | 2009-01-15 | Wyeth | Differential expression profiling analysis of cell culture phenotypes and uses thereof |
| WO2009005793A2 (en) | 2007-06-29 | 2009-01-08 | Avi Biopharma, Inc. | Tissue specific peptide conjugates and methods |
| US20100016215A1 (en) * | 2007-06-29 | 2010-01-21 | Avi Biopharma, Inc. | Compound and method for treating myotonic dystrophy |
| AU2008273096B2 (en) | 2007-07-12 | 2013-05-02 | Academisch Ziekenhuis Leiden | Molecules for targeting compounds to various selected organs or tissues |
| CL2008002085A1 (es) * | 2007-07-16 | 2008-11-21 | Genentech Inc | Anticuerpo humanizado anti-cd79b/igbeta/b29; polinucleotido codificacnte, vector, celula huesped; metodo de fabricacion; inmunoconjugado; composicion farmaceutica; uso para tratar cancer; metodo in vitro para determinar presencia de cd79b, oinhibir crecimiento de celulas quqe expresa cd79b; ensayo in vitro para detectar celulas b |
| US7960336B2 (en) * | 2007-08-03 | 2011-06-14 | Pharmain Corporation | Composition for long-acting peptide analogs |
| JP5099138B2 (ja) | 2007-08-06 | 2012-12-12 | 国立大学法人 筑波大学 | 花の形態が改変された植物体の生産方法 |
| WO2009023125A1 (en) | 2007-08-14 | 2009-02-19 | The Board Of Trustees Of The Leland Stanford Junior University | Neuronostatin and its uses |
| BRPI0815416A2 (pt) * | 2007-08-15 | 2014-10-21 | Amunix Inc | Composições e métodos para modificar propriedades de polipeptídeos biologicamente ativos |
| CN101918007B (zh) | 2007-08-28 | 2014-06-04 | Fmc有限公司 | 延迟的自胶凝藻酸盐体系及其应用 |
| KR100887266B1 (ko) | 2007-09-04 | 2009-03-06 | 주식회사 프로셀제약 | 세포투과성 p18 재조합 단백질, 이를 코딩하는폴리뉴클레오티드 및 이를 유효성분으로 함유하는 항암조성물 |
| EP2185707B1 (en) | 2007-09-04 | 2013-07-03 | Procell Therapeutics Inc. | Cell permeable nm23 recombinant proteins, polynucleotides encoding the same, and anti-metastatic composition comprising the same |
| JP5000439B2 (ja) | 2007-09-19 | 2012-08-15 | 三洋化成工業株式会社 | 細胞培養用担体 |
| MX2010003110A (es) | 2007-09-20 | 2010-05-19 | David Gladstone Inst | Composiciones de polipeptido de elemento nuclear intercalado largo y metodos de uso de las mismas. |
| US10611818B2 (en) | 2007-09-27 | 2020-04-07 | Agilent Technologies, Inc. | MHC multimers in tuberculosis diagnostics, vaccine and therapeutics |
| GB0720156D0 (en) | 2007-10-15 | 2007-11-28 | Univ Nottingham Trent | Breast cancer associated antigen |
| EP2205623B1 (en) * | 2007-10-29 | 2016-03-16 | Helix Biomedix Inc. | Protective skin care tetrapeptides |
| US7923253B2 (en) * | 2007-11-05 | 2011-04-12 | Battelle Memorial Institute | Method for identifying type I diabetes mellitus in humans |
| DK2208073T3 (da) | 2007-11-05 | 2020-03-30 | Nordic Bioscience As | Biokemiske markører til cvd-risikovurdering |
| WO2009061130A2 (en) | 2007-11-06 | 2009-05-14 | Procell Therapeutics Inc. | Cell permeable runx3 recombinant proteins, polynucleotides encoding the same, and anticancer compositions including the same |
| US20110262508A1 (en) | 2007-11-07 | 2011-10-27 | Paul Michael Watt | Antimicrobial compositions, formulations and uses thereof |
| US20100240057A1 (en) | 2007-11-08 | 2010-09-23 | St. Jude Children's Research Hospital | Methods and compositions for the diagnosis and treatment of chronic myeloid leukemia and acute lymphoblastic leukemia |
| AU2008321016B2 (en) | 2007-11-12 | 2013-03-28 | Theraclone Sciences, Inc. | Compositions and methods for the therapy and diagnosis of influenza |
| FR2925500B1 (fr) | 2007-12-21 | 2011-05-06 | Vincience | Peptide derive d'une proteine de la famille des aquaporines et composition cosmetique et/ou pharmaceutique le contenant |
| FR2925501B1 (fr) | 2007-12-21 | 2012-12-14 | Vincience | Peptide activateur de la synthese des aquaporines et composition cosmetique et/ou pharmaceutique le contenant |
| WO2009090651A2 (en) | 2008-01-15 | 2009-07-23 | Technion Research And Development Foundation Ltd. | Major histocompatibility complex hla-b2705 ligands useful for therapy and diagnosis |
| CA2713089C (en) | 2008-01-23 | 2017-11-21 | Dana Farber Cancer Institute | Compositions and methods for the treatment of viral infections |
| EP2250278B1 (en) | 2008-02-21 | 2023-04-05 | Burnham Institute for Medical Research | Methods and compositions related to peptides and proteins with c-terminal elements |
| WO2009117524A2 (en) | 2008-03-18 | 2009-09-24 | The Regents Of The University Of California | Sparse matrix system and method for identification of specific ligands or targets |
| WO2009146179A1 (en) | 2008-04-15 | 2009-12-03 | University Of Iowa Research Foundation | Zinc finger nuclease for the cftr gene and methods of use thereof |
| EP2113255A1 (en) | 2008-05-02 | 2009-11-04 | f-star Biotechnologische Forschungs- und Entwicklungsges.m.b.H. | Cytotoxic immunoglobulin |
| US20090281038A1 (en) | 2008-05-09 | 2009-11-12 | University Of Kentucky Research Foundation | Phylloplanins Inhibition of Microbial Growth on Organic Materials |
| KR20110016867A (ko) | 2008-05-16 | 2011-02-18 | 주식회사 프로셀제약 | 세포투과성 p27 재조합 단백질, 이를 코딩하는 폴리뉴클레오티드 및 이를 유효성분으로 함유하는 항암 조성물 |
| EA201100146A1 (ru) | 2008-07-04 | 2011-12-30 | Басф Плант Сайенс Гмбх | Растения, имеющие улучшенные характеристики урожайности, и способ их получения |
| KR101783272B1 (ko) | 2008-09-17 | 2017-09-29 | 젠코어 인코포레이티드 | IgE-매개된 장애를 치료하기 위한 신규 조성물 및 방법 |
| JP5299956B2 (ja) | 2008-09-29 | 2013-09-25 | 国立大学法人東北大学 | 質量分析装置を用いた代謝酵素群の一斉タンパク質定量に用いるペプチド |
| US20110318380A1 (en) | 2008-10-01 | 2011-12-29 | Dako Denmark A/S | MHC Multimers in Cancer Vaccines and Immune Monitoring |
| CA2753702C (en) | 2009-03-05 | 2017-01-03 | Medarex, Inc. | Fully human antibodies specific to cadm1 |
| MX2011007342A (es) * | 2009-04-09 | 2011-07-21 | Daiichi Sankyo Co Ltd | Anticuerpo anti-lectina similar a inmunoglobulina de union a acido sialico-15. |
| ES2566602T3 (es) | 2010-04-09 | 2016-04-14 | Aveo Pharmaceuticals, Inc. | Anticuerpos anti-ErbB3 |
| BR112013008255A2 (pt) * | 2010-10-05 | 2018-09-25 | Daiichi Sankyo Co Ltd | anticorpo isolado ou um fragmento funcional do mesmo, uso de um anticorpo isolado ou de um fragmento funcional do mesmo, composição farmacêutica, polinucleotídeo, vetor, célula transformada, e, método para produzir anticorpo |
| NZ631509A (en) | 2012-03-30 | 2016-09-30 | Daiichi Sankyo Co Ltd | Cdr-modified anti-siglec-15 antibody |
| US9493562B2 (en) | 2012-07-19 | 2016-11-15 | Alethia Biotherapeutics Inc. | Anti-Siglec-15 antibodies |
-
2009
- 2009-10-16 US US12/580,943 patent/US8168181B2/en not_active Ceased
-
2010
- 2010-10-06 EP EP10821519.5A patent/EP2486060A4/en not_active Withdrawn
- 2010-10-06 NZ NZ599193A patent/NZ599193A/en not_active IP Right Cessation
- 2010-10-06 RU RU2012118643/10A patent/RU2596392C2/ru not_active IP Right Cessation
- 2010-10-06 AU AU2010305281A patent/AU2010305281C1/en not_active Ceased
- 2010-10-06 CN CN201080053103.4A patent/CN102803293B/zh not_active Expired - Fee Related
- 2010-10-06 CA CA2870980A patent/CA2870980A1/en not_active Abandoned
- 2010-10-06 WO PCT/CA2010/001586 patent/WO2011041894A1/en not_active Ceased
- 2010-10-06 MX MX2012004084A patent/MX2012004084A/es active IP Right Grant
- 2010-10-06 CA CA2775793A patent/CA2775793C/en active Active
- 2010-10-06 CN CN201610363038.4A patent/CN106046160A/zh active Pending
- 2010-10-06 JP JP2012532427A patent/JP5855569B2/ja active Active
- 2010-10-06 BR BR112012007860A patent/BR112012007860A2/pt not_active IP Right Cessation
- 2010-10-06 KR KR1020127010573A patent/KR20120086297A/ko not_active Ceased
- 2010-10-06 US US13/499,792 patent/US8741289B2/en active Active
-
2012
- 2012-04-02 IL IL218985A patent/IL218985A0/en unknown
-
2014
- 2014-01-07 US US14/148,800 patent/US8900579B2/en active Active
- 2014-09-04 US US14/477,042 patent/US9388242B2/en active Active
- 2014-09-11 AU AU2014224071A patent/AU2014224071A1/en not_active Abandoned
-
2015
- 2015-12-09 JP JP2015240031A patent/JP2016040324A/ja active Pending
-
2016
- 2016-04-25 US US15/137,250 patent/US9617337B2/en active Active
-
2017
- 2017-09-06 US US15/697,069 patent/USRE47672E1/en active Active - Reinstated
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007093042A1 (en) * | 2006-02-13 | 2007-08-23 | Alethia Biotherapeutics Inc. | Polynucleotides and polypeptide sequences involved in the process of bone remodeling |
| WO2009048072A1 (ja) * | 2007-10-11 | 2009-04-16 | Daiichi Sankyo Company, Limited | 破骨細胞関連蛋白質Siglec-15を標的とした抗体 |
Non-Patent Citations (4)
| Title |
|---|
| Bespalov IA et al. Preparation of single-chained antibodies to human ferritin in Escherichia coli. Mol Biol (Mosk). 1993 Mar-Apr;27(2):451-60. * |
| Carrier A et al. Recombinant antibody-alkaline phosphatase conjugates for diagnosis of human IgGs: application to anti-HBsAg detection. J Immunol Methods. 1995 Apr 26;181(2):177-86. * |
| Pereira B et al. Cardiolipin binding a light chain from lupus-prone mice. Biochemistry. 1998 Feb 3;37(5):1430-7 * |
| Roovers RC et al. High-affinity recombinant phage antibodies to the pan-carcinoma marker epithelial glycoprotein-2 for tumour targeting. Br J Cancer. 1998 Dec;78(11):1407-16. * |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| AU2010305281C1 (en) | Siglec 15 antibodies in treating bone loss-related disease | |
| EP1999153B1 (en) | Agonist antibodies against tshr | |
| CA2876517C (en) | Anti-siglec-15 antibodies | |
| EP3130674B1 (en) | Antibodies that specifically block the biological activity of a tumor antigen | |
| JP2022043040A (ja) | 抗gpc-1抗体 | |
| KR102562418B1 (ko) | 항-테나신 c 항체 및 이의 용도 | |
| JP2019510739A (ja) | Gfral受容体療法 | |
| CN102089327A (zh) | 抗PirB抗体 | |
| WO2018087143A2 (en) | Anti-pd-1 antibodies | |
| US8722041B2 (en) | Anti-human equilibrative nucleoside transporter 1 (hENT1) antibodies and methods of use thereof | |
| JPWO2007049624A1 (ja) | 癌の予防・治療剤 | |
| EP1971619A2 (en) | Nogo-b receptor | |
| US12344665B2 (en) | Treatment of fibrodysplasia ossificans progressiva by administration of an anti-activin a antibody | |
| AU2016211890A1 (en) | Methods and Compositions for Regulating Iron Homeostasis by Modulation of BMP-6 | |
| WO2024118636A1 (en) | Targeting gpr158 (mglyr) with nanobodies for therapeutic benefits |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| DA2 | Applications for amendment section 104 |
Free format text: THE NATURE OF THE AMENDMENT IS AS SHOWN IN THE STATEMENT(S) FILED 01 AUG 2014 . |
|
| DA3 | Amendments made section 104 |
Free format text: THE NATURE OF THE AMENDMENT IS AS SHOWN IN THE STATEMENT(S) FILED 01 AUG 2014 |
|
| FGA | Letters patent sealed or granted (standard patent) | ||
| MK14 | Patent ceased section 143(a) (annual fees not paid) or expired |