ES2341608T3 - Homologos del receptor de nogo. - Google Patents
Homologos del receptor de nogo. Download PDFInfo
- Publication number
- ES2341608T3 ES2341608T3 ES01979595T ES01979595T ES2341608T3 ES 2341608 T3 ES2341608 T3 ES 2341608T3 ES 01979595 T ES01979595 T ES 01979595T ES 01979595 T ES01979595 T ES 01979595T ES 2341608 T3 ES2341608 T3 ES 2341608T3
- Authority
- ES
- Spain
- Prior art keywords
- ngr
- polypeptide
- protein
- seq
- amino acids
- 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.)
- Expired - Lifetime
Links
- 108010077641 Nogo Proteins Proteins 0.000 title abstract description 27
- 102100029831 Reticulon-4 Human genes 0.000 title 1
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 306
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 273
- 238000000034 method Methods 0.000 claims abstract description 176
- 230000014509 gene expression Effects 0.000 claims abstract description 114
- 239000000203 mixture Substances 0.000 claims abstract description 47
- 230000003376 axonal effect Effects 0.000 claims abstract description 31
- 230000012010 growth Effects 0.000 claims abstract description 21
- 230000005764 inhibitory process Effects 0.000 claims abstract description 20
- 208000016192 Demyelinating disease Diseases 0.000 claims abstract description 14
- 208000014674 injury Diseases 0.000 claims abstract description 14
- 208000006011 Stroke Diseases 0.000 claims abstract description 6
- 208000020431 spinal cord injury Diseases 0.000 claims abstract description 5
- 229920001184 polypeptide Polymers 0.000 claims description 253
- 210000004027 cell Anatomy 0.000 claims description 228
- 150000007523 nucleic acids Chemical class 0.000 claims description 121
- 102000039446 nucleic acids Human genes 0.000 claims description 109
- 108020004707 nucleic acids Proteins 0.000 claims description 109
- 150000001413 amino acids Chemical class 0.000 claims description 104
- 230000027455 binding Effects 0.000 claims description 97
- 239000013598 vector Substances 0.000 claims description 83
- 102000040430 polynucleotide Human genes 0.000 claims description 66
- 108091033319 polynucleotide Proteins 0.000 claims description 66
- 239000002157 polynucleotide Substances 0.000 claims description 66
- 239000012634 fragment Substances 0.000 claims description 60
- 241000282414 Homo sapiens Species 0.000 claims description 59
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 47
- 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 claims description 46
- 210000003169 central nervous system Anatomy 0.000 claims description 37
- 210000002569 neuron Anatomy 0.000 claims description 28
- 238000006467 substitution reaction Methods 0.000 claims description 27
- 208000035475 disorder Diseases 0.000 claims description 24
- 201000010099 disease Diseases 0.000 claims description 23
- 102000005781 Nogo Receptor Human genes 0.000 claims description 21
- 108020003872 Nogo receptor Proteins 0.000 claims description 21
- 241000124008 Mammalia Species 0.000 claims description 20
- 238000002360 preparation method Methods 0.000 claims description 20
- 239000000427 antigen Substances 0.000 claims description 17
- 108091007433 antigens Proteins 0.000 claims description 17
- 102000036639 antigens Human genes 0.000 claims description 17
- 230000007423 decrease Effects 0.000 claims description 16
- 239000002253 acid Substances 0.000 claims description 15
- 239000008194 pharmaceutical composition Substances 0.000 claims description 12
- 108010070675 Glutathione transferase Proteins 0.000 claims description 11
- 238000000338 in vitro Methods 0.000 claims description 10
- 208000027418 Wounds and injury Diseases 0.000 claims description 8
- 230000006378 damage Effects 0.000 claims description 8
- 206010012305 Demyelination Diseases 0.000 claims description 7
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 7
- 230000007850 degeneration Effects 0.000 claims description 6
- 208000015114 central nervous system disease Diseases 0.000 claims description 5
- 230000003247 decreasing effect Effects 0.000 claims description 5
- 238000001990 intravenous administration Methods 0.000 claims description 5
- 238000007920 subcutaneous administration Methods 0.000 claims description 5
- 208000029028 brain injury Diseases 0.000 claims description 4
- 230000003902 lesion Effects 0.000 claims description 4
- 208000011403 Alexander disease Diseases 0.000 claims description 3
- 208000010055 Globoid Cell Leukodystrophy Diseases 0.000 claims description 3
- 208000028226 Krabbe disease Diseases 0.000 claims description 3
- 208000034800 Leukoencephalopathies Diseases 0.000 claims description 3
- 206010056332 Panencephalitis Diseases 0.000 claims description 3
- 201000002491 encephalomyelitis Diseases 0.000 claims description 3
- 201000006417 multiple sclerosis Diseases 0.000 claims description 3
- 238000007911 parenteral administration Methods 0.000 claims description 3
- 208000022526 Canavan disease Diseases 0.000 claims description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 2
- 102100029100 Hematopoietic prostaglandin D synthase Human genes 0.000 claims 2
- 230000009036 growth inhibition Effects 0.000 claims 1
- 208000036546 leukodystrophy Diseases 0.000 claims 1
- 230000003458 metachromatic effect Effects 0.000 claims 1
- 101710093481 Reticulon-4 receptor Proteins 0.000 abstract description 567
- 102100029826 Reticulon-4 receptor Human genes 0.000 abstract description 562
- 108090000623 proteins and genes Proteins 0.000 abstract description 214
- 102000004169 proteins and genes Human genes 0.000 abstract description 156
- 230000000694 effects Effects 0.000 abstract description 95
- 102000010410 Nogo Proteins Human genes 0.000 abstract description 26
- 238000011282 treatment Methods 0.000 abstract description 22
- 230000001404 mediated effect Effects 0.000 abstract description 9
- 241000699670 Mus sp. Species 0.000 abstract description 6
- 230000008733 trauma Effects 0.000 abstract description 6
- 230000002490 cerebral effect Effects 0.000 abstract 1
- 150000001875 compounds Chemical class 0.000 description 178
- 235000018102 proteins Nutrition 0.000 description 132
- 238000004458 analytical method Methods 0.000 description 87
- 235000001014 amino acid Nutrition 0.000 description 85
- 108020004414 DNA Proteins 0.000 description 84
- 229940024606 amino acid Drugs 0.000 description 80
- 241001465754 Metazoa Species 0.000 description 72
- 125000003729 nucleotide group Chemical group 0.000 description 59
- 239000002773 nucleotide Substances 0.000 description 56
- 239000003446 ligand Substances 0.000 description 55
- 239000003795 chemical substances by application Substances 0.000 description 51
- 239000003814 drug Substances 0.000 description 51
- 230000000692 anti-sense effect Effects 0.000 description 46
- 238000012360 testing method Methods 0.000 description 44
- 229940079593 drug Drugs 0.000 description 39
- 239000013604 expression vector Substances 0.000 description 39
- 108091028043 Nucleic acid sequence Proteins 0.000 description 36
- 125000003275 alpha amino acid group Chemical group 0.000 description 35
- 102000037865 fusion proteins Human genes 0.000 description 33
- 108020001507 fusion proteins Proteins 0.000 description 33
- 108020004999 messenger RNA Proteins 0.000 description 32
- 210000001519 tissue Anatomy 0.000 description 32
- 239000000126 substance Substances 0.000 description 30
- 102000005962 receptors Human genes 0.000 description 26
- 108020003175 receptors Proteins 0.000 description 26
- 230000001225 therapeutic effect Effects 0.000 description 26
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 25
- 230000006870 function Effects 0.000 description 24
- 230000003993 interaction Effects 0.000 description 24
- 230000007246 mechanism Effects 0.000 description 22
- 101150089520 ngr gene Proteins 0.000 description 22
- 230000001105 regulatory effect Effects 0.000 description 22
- 230000000295 complement effect Effects 0.000 description 21
- 239000000047 product Substances 0.000 description 21
- 239000000523 sample Substances 0.000 description 21
- 238000009396 hybridization Methods 0.000 description 20
- 239000000243 solution Substances 0.000 description 19
- 108091034117 Oligonucleotide Proteins 0.000 description 18
- 230000002159 abnormal effect Effects 0.000 description 18
- 230000004927 fusion Effects 0.000 description 18
- 230000009261 transgenic effect Effects 0.000 description 18
- 101710095853 Reticulon-4 receptor-like 1 Proteins 0.000 description 17
- 108700019146 Transgenes Proteins 0.000 description 17
- 239000003112 inhibitor Substances 0.000 description 17
- 239000012528 membrane Substances 0.000 description 17
- 229920000642 polymer Polymers 0.000 description 17
- 238000003752 polymerase chain reaction Methods 0.000 description 17
- 102000006386 Myelin Proteins Human genes 0.000 description 16
- 108010083674 Myelin Proteins Proteins 0.000 description 16
- 102100031540 Reticulon-4 receptor-like 1 Human genes 0.000 description 16
- 125000000539 amino acid group Chemical group 0.000 description 16
- 210000003050 axon Anatomy 0.000 description 16
- 210000005012 myelin Anatomy 0.000 description 16
- 229920001223 polyethylene glycol Polymers 0.000 description 16
- 238000012216 screening Methods 0.000 description 16
- 239000002202 Polyethylene glycol Substances 0.000 description 15
- 239000002299 complementary DNA Substances 0.000 description 15
- 102000004190 Enzymes Human genes 0.000 description 14
- 108090000790 Enzymes Proteins 0.000 description 14
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 14
- 241000699666 Mus <mouse, genus> Species 0.000 description 14
- 102000000473 Nogo Receptor 2 Human genes 0.000 description 14
- 108010041253 Nogo Receptor 2 Proteins 0.000 description 14
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 14
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 14
- 229940088598 enzyme Drugs 0.000 description 14
- 108091026890 Coding region Proteins 0.000 description 13
- 206010028980 Neoplasm Diseases 0.000 description 13
- 230000015572 biosynthetic process Effects 0.000 description 13
- -1 F (ab) 2 Substances 0.000 description 12
- 101000727477 Homo sapiens Reticulon-4 receptor Proteins 0.000 description 12
- 230000004913 activation Effects 0.000 description 12
- 230000004071 biological effect Effects 0.000 description 12
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 12
- 239000000306 component Substances 0.000 description 12
- 102000048720 human RTN4R Human genes 0.000 description 12
- 239000003550 marker Substances 0.000 description 12
- 230000004048 modification Effects 0.000 description 12
- 238000012986 modification Methods 0.000 description 12
- 230000010076 replication Effects 0.000 description 12
- 108010076504 Protein Sorting Signals Proteins 0.000 description 11
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 11
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 11
- 238000003556 assay Methods 0.000 description 11
- 238000002744 homologous recombination Methods 0.000 description 11
- 230000006801 homologous recombination Effects 0.000 description 11
- 230000035772 mutation Effects 0.000 description 11
- 230000004044 response Effects 0.000 description 11
- 108020004511 Recombinant DNA Proteins 0.000 description 10
- 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 10
- 230000001413 cellular effect Effects 0.000 description 10
- 239000013043 chemical agent Substances 0.000 description 10
- 238000001514 detection method Methods 0.000 description 10
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 10
- 239000000463 material Substances 0.000 description 10
- 241000894007 species Species 0.000 description 10
- 238000013518 transcription Methods 0.000 description 10
- 230000035897 transcription Effects 0.000 description 10
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 9
- 241000894006 Bacteria Species 0.000 description 9
- 108090000994 Catalytic RNA Proteins 0.000 description 9
- 102000053642 Catalytic RNA Human genes 0.000 description 9
- 102000005720 Glutathione transferase Human genes 0.000 description 9
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 9
- 201000011510 cancer Diseases 0.000 description 9
- 238000007796 conventional method Methods 0.000 description 9
- 238000013461 design Methods 0.000 description 9
- 230000002255 enzymatic effect Effects 0.000 description 9
- 210000004408 hybridoma Anatomy 0.000 description 9
- 230000002401 inhibitory effect Effects 0.000 description 9
- 238000004519 manufacturing process Methods 0.000 description 9
- 239000002609 medium Substances 0.000 description 9
- 238000003199 nucleic acid amplification method Methods 0.000 description 9
- 239000013612 plasmid Substances 0.000 description 9
- 238000000746 purification Methods 0.000 description 9
- 108091092562 ribozyme Proteins 0.000 description 9
- 238000003786 synthesis reaction Methods 0.000 description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 102000053602 DNA Human genes 0.000 description 8
- 241000238631 Hexapoda Species 0.000 description 8
- 241001529936 Murinae Species 0.000 description 8
- 230000001594 aberrant effect Effects 0.000 description 8
- 239000002671 adjuvant Substances 0.000 description 8
- 230000003321 amplification Effects 0.000 description 8
- 238000013459 approach Methods 0.000 description 8
- 238000012217 deletion Methods 0.000 description 8
- 230000037430 deletion Effects 0.000 description 8
- 238000005516 engineering process Methods 0.000 description 8
- 230000002163 immunogen Effects 0.000 description 8
- 230000003834 intracellular effect Effects 0.000 description 8
- 238000002955 isolation Methods 0.000 description 8
- 230000002974 pharmacogenomic effect Effects 0.000 description 8
- 239000007787 solid Substances 0.000 description 8
- 229940124597 therapeutic agent Drugs 0.000 description 8
- 230000003612 virological effect Effects 0.000 description 8
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 7
- 108700008625 Reporter Genes Proteins 0.000 description 7
- 108010022394 Threonine synthase Proteins 0.000 description 7
- 239000000556 agonist Substances 0.000 description 7
- 210000000170 cell membrane Anatomy 0.000 description 7
- 239000012707 chemical precursor Substances 0.000 description 7
- 238000004587 chromatography analysis Methods 0.000 description 7
- 235000018417 cysteine Nutrition 0.000 description 7
- 238000001415 gene therapy Methods 0.000 description 7
- 210000000020 growth cone Anatomy 0.000 description 7
- 238000001727 in vivo Methods 0.000 description 7
- 238000003780 insertion Methods 0.000 description 7
- 230000037431 insertion Effects 0.000 description 7
- 230000008929 regeneration Effects 0.000 description 7
- 238000011069 regeneration method Methods 0.000 description 7
- 230000014616 translation Effects 0.000 description 7
- 239000002699 waste material Substances 0.000 description 7
- 241000588724 Escherichia coli Species 0.000 description 6
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 6
- 241000700605 Viruses Species 0.000 description 6
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 6
- 101710185494 Zinc finger protein Proteins 0.000 description 6
- 102100023597 Zinc finger protein 816 Human genes 0.000 description 6
- 238000010521 absorption reaction Methods 0.000 description 6
- 230000009471 action Effects 0.000 description 6
- 239000005557 antagonist Substances 0.000 description 6
- 230000000890 antigenic effect Effects 0.000 description 6
- 239000000074 antisense oligonucleotide Substances 0.000 description 6
- 238000012230 antisense oligonucleotides Methods 0.000 description 6
- 238000011161 development Methods 0.000 description 6
- 230000018109 developmental process Effects 0.000 description 6
- 102000004419 dihydrofolate reductase Human genes 0.000 description 6
- 239000003085 diluting agent Substances 0.000 description 6
- 230000002068 genetic effect Effects 0.000 description 6
- 239000003966 growth inhibitor Substances 0.000 description 6
- 230000001965 increasing effect Effects 0.000 description 6
- 238000010369 molecular cloning Methods 0.000 description 6
- 239000002904 solvent Substances 0.000 description 6
- 238000010396 two-hybrid screening Methods 0.000 description 6
- 241000701447 unidentified baculovirus Species 0.000 description 6
- 229910052725 zinc Inorganic materials 0.000 description 6
- 239000011701 zinc Substances 0.000 description 6
- 108091035707 Consensus sequence Proteins 0.000 description 5
- 108010001237 Cytochrome P-450 CYP2D6 Proteins 0.000 description 5
- 241000282412 Homo Species 0.000 description 5
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 5
- 108010091086 Recombinases Proteins 0.000 description 5
- 102000018120 Recombinases Human genes 0.000 description 5
- 108091023040 Transcription factor Proteins 0.000 description 5
- 102000040945 Transcription factor Human genes 0.000 description 5
- 230000004075 alteration Effects 0.000 description 5
- 238000010171 animal model Methods 0.000 description 5
- 230000008485 antagonism Effects 0.000 description 5
- 229960002685 biotin Drugs 0.000 description 5
- 235000020958 biotin Nutrition 0.000 description 5
- 239000011616 biotin Substances 0.000 description 5
- 239000000969 carrier Substances 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 5
- 239000006185 dispersion Substances 0.000 description 5
- 229960003180 glutathione Drugs 0.000 description 5
- 235000011187 glycerol Nutrition 0.000 description 5
- 238000004128 high performance liquid chromatography Methods 0.000 description 5
- 230000002209 hydrophobic effect Effects 0.000 description 5
- 210000003000 inclusion body Anatomy 0.000 description 5
- 230000001939 inductive effect Effects 0.000 description 5
- 239000004615 ingredient Substances 0.000 description 5
- 239000007788 liquid Substances 0.000 description 5
- 210000004962 mammalian cell Anatomy 0.000 description 5
- 230000004060 metabolic process Effects 0.000 description 5
- 238000002703 mutagenesis Methods 0.000 description 5
- 231100000350 mutagenesis Toxicity 0.000 description 5
- 210000000287 oocyte Anatomy 0.000 description 5
- 230000008488 polyadenylation Effects 0.000 description 5
- 210000001236 prokaryotic cell Anatomy 0.000 description 5
- 230000000069 prophylactic effect Effects 0.000 description 5
- 238000003259 recombinant expression Methods 0.000 description 5
- 108091008146 restriction endonucleases Proteins 0.000 description 5
- 238000012552 review Methods 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 239000000758 substrate Substances 0.000 description 5
- 238000001890 transfection Methods 0.000 description 5
- 230000009466 transformation Effects 0.000 description 5
- 238000013519 translation Methods 0.000 description 5
- 238000011144 upstream manufacturing Methods 0.000 description 5
- 210000005253 yeast cell Anatomy 0.000 description 5
- 108020000948 Antisense Oligonucleotides Proteins 0.000 description 4
- 108020005544 Antisense RNA Proteins 0.000 description 4
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 4
- 108091033380 Coding strand Proteins 0.000 description 4
- 102100021704 Cytochrome P450 2D6 Human genes 0.000 description 4
- 241000196324 Embryophyta Species 0.000 description 4
- 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 4
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 4
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 4
- 108060001084 Luciferase Proteins 0.000 description 4
- 239000005089 Luciferase Substances 0.000 description 4
- 108010090804 Streptavidin Proteins 0.000 description 4
- 238000005917 acylation reaction Methods 0.000 description 4
- 230000008484 agonism Effects 0.000 description 4
- 210000004102 animal cell Anatomy 0.000 description 4
- 210000000628 antibody-producing cell Anatomy 0.000 description 4
- YZXBAPSDXZZRGB-DOFZRALJSA-N arachidonic acid Chemical compound CCCCC\C=C/C\C=C/C\C=C/C\C=C/CCCC(O)=O YZXBAPSDXZZRGB-DOFZRALJSA-N 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 230000024245 cell differentiation Effects 0.000 description 4
- 239000003638 chemical reducing agent Substances 0.000 description 4
- 239000003184 complementary RNA Substances 0.000 description 4
- 230000009918 complex formation Effects 0.000 description 4
- 238000010276 construction Methods 0.000 description 4
- 239000012636 effector Substances 0.000 description 4
- 238000004520 electroporation Methods 0.000 description 4
- 210000001671 embryonic stem cell Anatomy 0.000 description 4
- 239000003623 enhancer Substances 0.000 description 4
- 238000001914 filtration Methods 0.000 description 4
- 230000005714 functional activity Effects 0.000 description 4
- 210000003128 head Anatomy 0.000 description 4
- 230000001900 immune effect Effects 0.000 description 4
- 230000028993 immune response Effects 0.000 description 4
- 230000003053 immunization Effects 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- 239000002502 liposome Substances 0.000 description 4
- HQKMJHAJHXVSDF-UHFFFAOYSA-L magnesium stearate Chemical compound [Mg+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O HQKMJHAJHXVSDF-UHFFFAOYSA-L 0.000 description 4
- 210000001161 mammalian embryo Anatomy 0.000 description 4
- 239000011159 matrix material Substances 0.000 description 4
- 229960000485 methotrexate Drugs 0.000 description 4
- 244000005700 microbiome Species 0.000 description 4
- 229930014626 natural product Natural products 0.000 description 4
- 210000002241 neurite Anatomy 0.000 description 4
- 239000002858 neurotransmitter agent Substances 0.000 description 4
- 210000004248 oligodendroglia Anatomy 0.000 description 4
- 230000006320 pegylation Effects 0.000 description 4
- 102000054765 polymorphisms of proteins Human genes 0.000 description 4
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 4
- 230000002285 radioactive effect Effects 0.000 description 4
- 230000011664 signaling Effects 0.000 description 4
- 150000003384 small molecules Chemical class 0.000 description 4
- 230000004083 survival effect Effects 0.000 description 4
- 239000003826 tablet Substances 0.000 description 4
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 3
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 3
- WVDDGKGOMKODPV-UHFFFAOYSA-N Benzyl alcohol Chemical compound OCC1=CC=CC=C1 WVDDGKGOMKODPV-UHFFFAOYSA-N 0.000 description 3
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 3
- 230000004568 DNA-binding Effects 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 108010024636 Glutathione Proteins 0.000 description 3
- 108060003951 Immunoglobulin Proteins 0.000 description 3
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 3
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 3
- 101000727479 Mus musculus Reticulon-4 receptor Proteins 0.000 description 3
- 208000028389 Nerve injury Diseases 0.000 description 3
- 108090000189 Neuropeptides Proteins 0.000 description 3
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 3
- 241000283973 Oryctolagus cuniculus Species 0.000 description 3
- 108010029485 Protein Isoforms Proteins 0.000 description 3
- 102000001708 Protein Isoforms Human genes 0.000 description 3
- 241000700159 Rattus Species 0.000 description 3
- 238000012300 Sequence Analysis Methods 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 238000002105 Southern blotting Methods 0.000 description 3
- 102100040296 TATA-box-binding protein Human genes 0.000 description 3
- 101710145783 TATA-box-binding protein Proteins 0.000 description 3
- 239000012190 activator Substances 0.000 description 3
- 238000007792 addition Methods 0.000 description 3
- 150000001299 aldehydes Chemical class 0.000 description 3
- 239000003242 anti bacterial agent Substances 0.000 description 3
- 239000011324 bead Substances 0.000 description 3
- 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 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 230000037396 body weight Effects 0.000 description 3
- 210000004556 brain Anatomy 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 238000000576 coating method Methods 0.000 description 3
- 230000002860 competitive effect Effects 0.000 description 3
- 230000008878 coupling Effects 0.000 description 3
- 238000010168 coupling process Methods 0.000 description 3
- 238000005859 coupling reaction Methods 0.000 description 3
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 3
- 230000003412 degenerative effect Effects 0.000 description 3
- 210000001787 dendrite Anatomy 0.000 description 3
- 239000003599 detergent Substances 0.000 description 3
- 238000003745 diagnosis Methods 0.000 description 3
- 230000029087 digestion Effects 0.000 description 3
- 239000002552 dosage form Substances 0.000 description 3
- 239000003937 drug carrier Substances 0.000 description 3
- 238000007876 drug discovery Methods 0.000 description 3
- 238000007877 drug screening Methods 0.000 description 3
- 150000002148 esters Chemical class 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 102000018358 immunoglobulin Human genes 0.000 description 3
- 230000000670 limiting effect Effects 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 230000033001 locomotion Effects 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 239000002207 metabolite Substances 0.000 description 3
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 3
- 238000000520 microinjection Methods 0.000 description 3
- 230000008764 nerve damage Effects 0.000 description 3
- 239000002751 oligonucleotide probe Substances 0.000 description 3
- 210000000056 organ Anatomy 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 230000001575 pathological effect Effects 0.000 description 3
- 239000000816 peptidomimetic Substances 0.000 description 3
- 239000000546 pharmaceutical excipient Substances 0.000 description 3
- 239000012071 phase Substances 0.000 description 3
- 230000000704 physical effect Effects 0.000 description 3
- 229920005862 polyol Polymers 0.000 description 3
- 150000003077 polyols Chemical class 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 238000011321 prophylaxis Methods 0.000 description 3
- 238000011002 quantification Methods 0.000 description 3
- 238000010188 recombinant method Methods 0.000 description 3
- 230000006798 recombination Effects 0.000 description 3
- 238000005215 recombination Methods 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 230000019491 signal transduction Effects 0.000 description 3
- 239000007921 spray Substances 0.000 description 3
- 235000000346 sugar Nutrition 0.000 description 3
- 239000000829 suppository Substances 0.000 description 3
- 231100000419 toxicity Toxicity 0.000 description 3
- 230000001988 toxicity Effects 0.000 description 3
- 238000010361 transduction Methods 0.000 description 3
- 230000026683 transduction Effects 0.000 description 3
- 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 3
- 239000003981 vehicle Substances 0.000 description 3
- 239000013603 viral vector Substances 0.000 description 3
- 229920003169 water-soluble polymer Polymers 0.000 description 3
- RFLVMTUMFYRZCB-UHFFFAOYSA-N 1-methylguanine Chemical compound O=C1N(C)C(N)=NC2=C1N=CN2 RFLVMTUMFYRZCB-UHFFFAOYSA-N 0.000 description 2
- YSAJFXWTVFGPAX-UHFFFAOYSA-N 2-[(2,4-dioxo-1h-pyrimidin-5-yl)oxy]acetic acid Chemical compound OC(=O)COC1=CNC(=O)NC1=O YSAJFXWTVFGPAX-UHFFFAOYSA-N 0.000 description 2
- FZWGECJQACGGTI-UHFFFAOYSA-N 2-amino-7-methyl-1,7-dihydro-6H-purin-6-one Chemical compound NC1=NC(O)=C2N(C)C=NC2=N1 FZWGECJQACGGTI-UHFFFAOYSA-N 0.000 description 2
- OIVLITBTBDPEFK-UHFFFAOYSA-N 5,6-dihydrouracil Chemical compound O=C1CCNC(=O)N1 OIVLITBTBDPEFK-UHFFFAOYSA-N 0.000 description 2
- ZLAQATDNGLKIEV-UHFFFAOYSA-N 5-methyl-2-sulfanylidene-1h-pyrimidin-4-one Chemical compound CC1=CNC(=S)NC1=O ZLAQATDNGLKIEV-UHFFFAOYSA-N 0.000 description 2
- 102100031126 6-phosphogluconolactonase Human genes 0.000 description 2
- 108010029731 6-phosphogluconolactonase Proteins 0.000 description 2
- LRFVTYWOQMYALW-UHFFFAOYSA-N 9H-xanthine Chemical compound O=C1NC(=O)NC2=C1NC=N2 LRFVTYWOQMYALW-UHFFFAOYSA-N 0.000 description 2
- 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 2
- 239000004475 Arginine Substances 0.000 description 2
- 102100038110 Arylamine N-acetyltransferase 2 Human genes 0.000 description 2
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- IVOMOUWHDPKRLL-KQYNXXCUSA-N Cyclic adenosine monophosphate Chemical compound C([C@H]1O2)OP(O)(=O)O[C@H]1[C@@H](O)[C@@H]2N1C(N=CN=C2N)=C2N=C1 IVOMOUWHDPKRLL-KQYNXXCUSA-N 0.000 description 2
- 108010026925 Cytochrome P-450 CYP2C19 Proteins 0.000 description 2
- 241000701022 Cytomegalovirus Species 0.000 description 2
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 2
- 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 2
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 2
- 101150074155 DHFR gene Proteins 0.000 description 2
- 230000008304 DNA mechanism Effects 0.000 description 2
- 102000052510 DNA-Binding Proteins Human genes 0.000 description 2
- 241000702421 Dependoparvovirus Species 0.000 description 2
- 229920002307 Dextran Polymers 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- 108091000126 Dihydroorotase Proteins 0.000 description 2
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 2
- 241000701959 Escherichia virus Lambda Species 0.000 description 2
- 108091029865 Exogenous DNA Proteins 0.000 description 2
- 108091006020 Fc-tagged proteins Proteins 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- 108010010803 Gelatin Proteins 0.000 description 2
- 108010018962 Glucosephosphate Dehydrogenase Proteins 0.000 description 2
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
- XKMLYUALXHKNFT-UUOKFMHZSA-N Guanosine-5'-triphosphate Chemical compound C1=2NC(N)=NC(=O)C=2N=CN1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O XKMLYUALXHKNFT-UUOKFMHZSA-N 0.000 description 2
- 101000884399 Homo sapiens Arylamine N-acetyltransferase 2 Proteins 0.000 description 2
- 101001130250 Homo sapiens Reticulon-4 receptor-like 1 Proteins 0.000 description 2
- 101001130247 Homo sapiens Reticulon-4 receptor-like 2 Proteins 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 2
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 2
- 108091092195 Intron Proteins 0.000 description 2
- 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 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 229930195725 Mannitol Natural products 0.000 description 2
- 208000030136 Marchiafava-Bignami Disease Diseases 0.000 description 2
- 201000011442 Metachromatic leukodystrophy Diseases 0.000 description 2
- 102000017099 Myelin-Associated Glycoprotein Human genes 0.000 description 2
- 108010013731 Myelin-Associated Glycoprotein Proteins 0.000 description 2
- HYVABZIGRDEKCD-UHFFFAOYSA-N N(6)-dimethylallyladenine Chemical compound CC(C)=CCNC1=NC=NC2=C1N=CN2 HYVABZIGRDEKCD-UHFFFAOYSA-N 0.000 description 2
- PXHVJJICTQNCMI-UHFFFAOYSA-N Nickel Chemical compound [Ni] PXHVJJICTQNCMI-UHFFFAOYSA-N 0.000 description 2
- 108091092724 Noncoding DNA Proteins 0.000 description 2
- 101710163270 Nuclease Proteins 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 238000012408 PCR amplification Methods 0.000 description 2
- 108010067902 Peptide Library Proteins 0.000 description 2
- 108091093037 Peptide nucleic acid Proteins 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 241000276498 Pollachius virens Species 0.000 description 2
- 102000001253 Protein Kinase Human genes 0.000 description 2
- 229920002472 Starch Polymers 0.000 description 2
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- 208000036142 Viral infection Diseases 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 230000002411 adverse Effects 0.000 description 2
- 239000000443 aerosol Substances 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 238000001261 affinity purification Methods 0.000 description 2
- 238000005804 alkylation reaction Methods 0.000 description 2
- 229960000723 ampicillin Drugs 0.000 description 2
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 2
- 230000000844 anti-bacterial effect Effects 0.000 description 2
- 230000003302 anti-idiotype Effects 0.000 description 2
- 230000005875 antibody response Effects 0.000 description 2
- 229940121375 antifungal agent Drugs 0.000 description 2
- 239000002246 antineoplastic agent Substances 0.000 description 2
- 229940041181 antineoplastic drug Drugs 0.000 description 2
- 230000006907 apoptotic process Effects 0.000 description 2
- 229940114079 arachidonic acid Drugs 0.000 description 2
- 235000021342 arachidonic acid Nutrition 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 235000010323 ascorbic acid Nutrition 0.000 description 2
- 229960005070 ascorbic acid Drugs 0.000 description 2
- 239000011668 ascorbic acid Substances 0.000 description 2
- 230000028600 axonogenesis Effects 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- 230000004888 barrier function Effects 0.000 description 2
- 108091008324 binding proteins Proteins 0.000 description 2
- 210000000601 blood cell Anatomy 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 239000001506 calcium phosphate Substances 0.000 description 2
- 229910000389 calcium phosphate Inorganic materials 0.000 description 2
- 235000011010 calcium phosphates Nutrition 0.000 description 2
- 238000004422 calculation algorithm Methods 0.000 description 2
- 239000002775 capsule Substances 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
- 210000005056 cell body Anatomy 0.000 description 2
- 230000030833 cell death Effects 0.000 description 2
- 230000004663 cell proliferation Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- OSASVXMJTNOKOY-UHFFFAOYSA-N chlorobutanol Chemical compound CC(C)(O)C(Cl)(Cl)Cl OSASVXMJTNOKOY-UHFFFAOYSA-N 0.000 description 2
- 230000002759 chromosomal effect Effects 0.000 description 2
- 238000000975 co-precipitation Methods 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 229940110456 cocoa butter Drugs 0.000 description 2
- 235000019868 cocoa butter Nutrition 0.000 description 2
- OROGSEYTTFOCAN-DNJOTXNNSA-N codeine Chemical compound C([C@H]1[C@H](N(CC[C@@]112)C)C3)=C[C@H](O)[C@@H]1OC1=C2C3=CC=C1OC OROGSEYTTFOCAN-DNJOTXNNSA-N 0.000 description 2
- 230000009850 completed effect Effects 0.000 description 2
- 230000021615 conjugation Effects 0.000 description 2
- ORTQZVOHEJQUHG-UHFFFAOYSA-L copper(II) chloride Chemical compound Cl[Cu]Cl ORTQZVOHEJQUHG-UHFFFAOYSA-L 0.000 description 2
- CVSVTCORWBXHQV-UHFFFAOYSA-N creatine Chemical compound NC(=[NH2+])N(C)CC([O-])=O CVSVTCORWBXHQV-UHFFFAOYSA-N 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 229960002086 dextran Drugs 0.000 description 2
- 239000008121 dextrose Substances 0.000 description 2
- 150000001982 diacylglycerols Chemical class 0.000 description 2
- 238000002405 diagnostic procedure Methods 0.000 description 2
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 2
- 208000037765 diseases and disorders Diseases 0.000 description 2
- 239000002612 dispersion medium Substances 0.000 description 2
- 238000006073 displacement reaction Methods 0.000 description 2
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 2
- 230000008030 elimination Effects 0.000 description 2
- 238000003379 elimination reaction Methods 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 238000011049 filling Methods 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 2
- 239000008273 gelatin Substances 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
- 238000012252 genetic analysis Methods 0.000 description 2
- 210000004602 germ cell Anatomy 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 230000013595 glycosylation Effects 0.000 description 2
- 238000006206 glycosylation reaction Methods 0.000 description 2
- 239000003102 growth factor Substances 0.000 description 2
- 239000005556 hormone Substances 0.000 description 2
- 229940088597 hormone Drugs 0.000 description 2
- 102000053414 human RTN4RL2 Human genes 0.000 description 2
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 description 2
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 2
- 238000002649 immunization Methods 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 238000001114 immunoprecipitation Methods 0.000 description 2
- 238000011065 in-situ storage Methods 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- 229910052500 inorganic mineral Inorganic materials 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- 239000008101 lactose Substances 0.000 description 2
- 235000019359 magnesium stearate Nutrition 0.000 description 2
- 239000000594 mannitol Substances 0.000 description 2
- 235000010355 mannitol Nutrition 0.000 description 2
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 2
- 239000011707 mineral Substances 0.000 description 2
- BQJCRHHNABKAKU-KBQPJGBKSA-N morphine Chemical compound O([C@H]1[C@H](C=C[C@H]23)O)C4=C5[C@@]12CCN(C)[C@@H]3CC5=CC=C4O BQJCRHHNABKAKU-KBQPJGBKSA-N 0.000 description 2
- 210000000653 nervous system Anatomy 0.000 description 2
- 230000003472 neutralizing effect Effects 0.000 description 2
- 239000000346 nonvolatile oil Substances 0.000 description 2
- 239000002674 ointment Substances 0.000 description 2
- 150000002894 organic compounds Chemical class 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- 238000010647 peptide synthesis reaction Methods 0.000 description 2
- 239000000825 pharmaceutical preparation Substances 0.000 description 2
- 230000003285 pharmacodynamic effect Effects 0.000 description 2
- 239000002953 phosphate buffered saline Substances 0.000 description 2
- 150000003905 phosphatidylinositols Chemical class 0.000 description 2
- 230000035790 physiological processes and functions Effects 0.000 description 2
- 230000006461 physiological response Effects 0.000 description 2
- 230000036470 plasma concentration Effects 0.000 description 2
- 229920001451 polypropylene glycol Polymers 0.000 description 2
- 230000003389 potentiating effect Effects 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000002062 proliferating effect Effects 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- 230000006916 protein interaction Effects 0.000 description 2
- 108060006633 protein kinase Proteins 0.000 description 2
- 239000000941 radioactive substance Substances 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 239000013049 sediment Substances 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 231100000004 severe toxicity Toxicity 0.000 description 2
- 239000007790 solid phase Substances 0.000 description 2
- 238000005063 solubilization Methods 0.000 description 2
- 230000007928 solubilization Effects 0.000 description 2
- 210000001082 somatic cell Anatomy 0.000 description 2
- 239000000600 sorbitol Substances 0.000 description 2
- 235000010356 sorbitol Nutrition 0.000 description 2
- 235000019698 starch Nutrition 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 150000008163 sugars Chemical class 0.000 description 2
- 239000013589 supplement Substances 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 208000024891 symptom Diseases 0.000 description 2
- 238000007910 systemic administration Methods 0.000 description 2
- RYYWUUFWQRZTIU-UHFFFAOYSA-K thiophosphate Chemical compound [O-]P([O-])([O-])=S RYYWUUFWQRZTIU-UHFFFAOYSA-K 0.000 description 2
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 2
- 231100000041 toxicology testing Toxicity 0.000 description 2
- 230000005030 transcription termination Effects 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 238000011426 transformation method Methods 0.000 description 2
- 230000001131 transforming effect Effects 0.000 description 2
- 230000032258 transport Effects 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 241001430294 unidentified retrovirus Species 0.000 description 2
- 238000012795 verification Methods 0.000 description 2
- 230000009385 viral infection Effects 0.000 description 2
- 230000029663 wound healing Effects 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 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
- DIGQNXIGRZPYDK-WKSCXVIASA-N (2R)-6-amino-2-[[2-[[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-[[(2R,3S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S,3S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2R)-2-[[2-[[2-[[2-[(2-amino-1-hydroxyethylidene)amino]-3-carboxy-1-hydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1,5-dihydroxy-5-iminopentylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]hexanoic acid Chemical compound C[C@@H]([C@@H](C(=N[C@@H](CS)C(=N[C@@H](C)C(=N[C@@H](CO)C(=NCC(=N[C@@H](CCC(=N)O)C(=NC(CS)C(=N[C@H]([C@H](C)O)C(=N[C@H](CS)C(=N[C@H](CO)C(=NCC(=N[C@H](CS)C(=NCC(=N[C@H](CCCCN)C(=O)O)O)O)O)O)O)O)O)O)O)O)O)O)O)N=C([C@H](CS)N=C([C@H](CO)N=C([C@H](CO)N=C([C@H](C)N=C(CN=C([C@H](CO)N=C([C@H](CS)N=C(CN=C(C(CS)N=C(C(CC(=O)O)N=C(CN)O)O)O)O)O)O)O)O)O)O)O)O DIGQNXIGRZPYDK-WKSCXVIASA-N 0.000 description 1
- ASWBNKHCZGQVJV-UHFFFAOYSA-N (3-hexadecanoyloxy-2-hydroxypropyl) 2-(trimethylazaniumyl)ethyl phosphate Chemical compound CCCCCCCCCCCCCCCC(=O)OCC(O)COP([O-])(=O)OCC[N+](C)(C)C ASWBNKHCZGQVJV-UHFFFAOYSA-N 0.000 description 1
- WJNGQIYEQLPJMN-IOSLPCCCSA-N 1-methylinosine Chemical compound C1=NC=2C(=O)N(C)C=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O WJNGQIYEQLPJMN-IOSLPCCCSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
- UFBJCMHMOXMLKC-UHFFFAOYSA-N 2,4-dinitrophenol Chemical compound OC1=CC=C([N+]([O-])=O)C=C1[N+]([O-])=O UFBJCMHMOXMLKC-UHFFFAOYSA-N 0.000 description 1
- HLYBTPMYFWWNJN-UHFFFAOYSA-N 2-(2,4-dioxo-1h-pyrimidin-5-yl)-2-hydroxyacetic acid Chemical compound OC(=O)C(O)C1=CNC(=O)NC1=O HLYBTPMYFWWNJN-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-UHFFFAOYSA-N 2-(hydroxymethyl)-6-[4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxane-3,4,5-triol Chemical compound OCC1OC(OC2C(O)C(O)C(O)OC2CO)C(O)C(O)C1O GUBGYTABKSRVRQ-UHFFFAOYSA-N 0.000 description 1
- SGAKLDIYNFXTCK-UHFFFAOYSA-N 2-[(2,4-dioxo-1h-pyrimidin-5-yl)methylamino]acetic acid Chemical compound OC(=O)CNCC1=CNC(=O)NC1=O SGAKLDIYNFXTCK-UHFFFAOYSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- XMSMHKMPBNTBOD-UHFFFAOYSA-N 2-dimethylamino-6-hydroxypurine Chemical compound N1C(N(C)C)=NC(=O)C2=C1N=CN2 XMSMHKMPBNTBOD-UHFFFAOYSA-N 0.000 description 1
- SMADWRYCYBUIKH-UHFFFAOYSA-N 2-methyl-7h-purin-6-amine Chemical compound CC1=NC(N)=C2NC=NC2=N1 SMADWRYCYBUIKH-UHFFFAOYSA-N 0.000 description 1
- FUBFWTUFPGFHOJ-UHFFFAOYSA-N 2-nitrofuran Chemical class [O-][N+](=O)C1=CC=CO1 FUBFWTUFPGFHOJ-UHFFFAOYSA-N 0.000 description 1
- HATKUFQZJPLPGN-UHFFFAOYSA-N 2-phosphanylethane-1,1,1-tricarboxylic acid Chemical compound OC(=O)C(CP)(C(O)=O)C(O)=O HATKUFQZJPLPGN-UHFFFAOYSA-N 0.000 description 1
- UMCMPZBLKLEWAF-BCTGSCMUSA-N 3-[(3-cholamidopropyl)dimethylammonio]propane-1-sulfonate Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCC[N+](C)(C)CCCS([O-])(=O)=O)C)[C@@]2(C)[C@@H](O)C1 UMCMPZBLKLEWAF-BCTGSCMUSA-N 0.000 description 1
- GUQQBLRVXOUDTN-XOHPMCGNSA-N 3-[dimethyl-[3-[[(4r)-4-[(3r,5s,7r,8r,9s,10s,12s,13r,14s,17r)-3,7,12-trihydroxy-10,13-dimethyl-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1h-cyclopenta[a]phenanthren-17-yl]pentanoyl]amino]propyl]azaniumyl]-2-hydroxypropane-1-sulfonate Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCC[N+](C)(C)CC(O)CS([O-])(=O)=O)C)[C@@]2(C)[C@@H](O)C1 GUQQBLRVXOUDTN-XOHPMCGNSA-N 0.000 description 1
- KOLPWZCZXAMXKS-UHFFFAOYSA-N 3-methylcytosine Chemical compound CN1C(N)=CC=NC1=O KOLPWZCZXAMXKS-UHFFFAOYSA-N 0.000 description 1
- GJAKJCICANKRFD-UHFFFAOYSA-N 4-acetyl-4-amino-1,3-dihydropyrimidin-2-one Chemical compound CC(=O)C1(N)NC(=O)NC=C1 GJAKJCICANKRFD-UHFFFAOYSA-N 0.000 description 1
- OVONXEQGWXGFJD-UHFFFAOYSA-N 4-sulfanylidene-1h-pyrimidin-2-one Chemical compound SC=1C=CNC(=O)N=1 OVONXEQGWXGFJD-UHFFFAOYSA-N 0.000 description 1
- MQJSSLBGAQJNER-UHFFFAOYSA-N 5-(methylaminomethyl)-1h-pyrimidine-2,4-dione Chemical compound CNCC1=CNC(=O)NC1=O MQJSSLBGAQJNER-UHFFFAOYSA-N 0.000 description 1
- WPYRHVXCOQLYLY-UHFFFAOYSA-N 5-[(methoxyamino)methyl]-2-sulfanylidene-1h-pyrimidin-4-one Chemical compound CONCC1=CNC(=S)NC1=O WPYRHVXCOQLYLY-UHFFFAOYSA-N 0.000 description 1
- LQLQRFGHAALLLE-UHFFFAOYSA-N 5-bromouracil Chemical compound BrC1=CNC(=O)NC1=O LQLQRFGHAALLLE-UHFFFAOYSA-N 0.000 description 1
- VKLFQTYNHLDMDP-PNHWDRBUSA-N 5-carboxymethylaminomethyl-2-thiouridine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C(=S)NC(=O)C(CNCC(O)=O)=C1 VKLFQTYNHLDMDP-PNHWDRBUSA-N 0.000 description 1
- ZFTBZKVVGZNMJR-UHFFFAOYSA-N 5-chlorouracil Chemical compound ClC1=CNC(=O)NC1=O ZFTBZKVVGZNMJR-UHFFFAOYSA-N 0.000 description 1
- KSNXJLQDQOIRIP-UHFFFAOYSA-N 5-iodouracil Chemical compound IC1=CNC(=O)NC1=O KSNXJLQDQOIRIP-UHFFFAOYSA-N 0.000 description 1
- KELXHQACBIUYSE-UHFFFAOYSA-N 5-methoxy-1h-pyrimidine-2,4-dione Chemical compound COC1=CNC(=O)NC1=O KELXHQACBIUYSE-UHFFFAOYSA-N 0.000 description 1
- LRSASMSXMSNRBT-UHFFFAOYSA-N 5-methylcytosine Chemical compound CC1=CNC(=O)N=C1N LRSASMSXMSNRBT-UHFFFAOYSA-N 0.000 description 1
- DCPSTSVLRXOYGS-UHFFFAOYSA-N 6-amino-1h-pyrimidine-2-thione Chemical compound NC1=CC=NC(S)=N1 DCPSTSVLRXOYGS-UHFFFAOYSA-N 0.000 description 1
- CJIJXIFQYOPWTF-UHFFFAOYSA-N 7-hydroxycoumarin Natural products O1C(=O)C=CC2=CC(O)=CC=C21 CJIJXIFQYOPWTF-UHFFFAOYSA-N 0.000 description 1
- MSSXOMSJDRHRMC-UHFFFAOYSA-N 9H-purine-2,6-diamine Chemical compound NC1=NC(N)=C2NC=NC2=N1 MSSXOMSJDRHRMC-UHFFFAOYSA-N 0.000 description 1
- 102000012440 Acetylcholinesterase Human genes 0.000 description 1
- 108010022752 Acetylcholinesterase Proteins 0.000 description 1
- 102000007469 Actins Human genes 0.000 description 1
- 108010085238 Actins Proteins 0.000 description 1
- 206010067484 Adverse reaction Diseases 0.000 description 1
- 108010000239 Aequorin Proteins 0.000 description 1
- 235000001674 Agaricus brunnescens Nutrition 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 108700028369 Alleles Proteins 0.000 description 1
- 102100023635 Alpha-fetoprotein Human genes 0.000 description 1
- 102000030907 Aspartate Carbamoyltransferase Human genes 0.000 description 1
- 241000416162 Astragalus gummifer Species 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- LSNNMFCWUKXFEE-UHFFFAOYSA-M Bisulfite Chemical compound OS([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-M 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 101150010738 CYP2D6 gene Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 240000001432 Calendula officinalis Species 0.000 description 1
- 235000005881 Calendula officinalis Nutrition 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 101710113083 Carbamoyl-phosphate synthase Proteins 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 102000019034 Chemokines Human genes 0.000 description 1
- 108010012236 Chemokines Proteins 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 1
- 241000282552 Chlorocebus aethiops Species 0.000 description 1
- 208000000532 Chronic Brain Injury Diseases 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 108020004394 Complementary RNA Proteins 0.000 description 1
- 229920002261 Corn starch Polymers 0.000 description 1
- 241000186216 Corynebacterium Species 0.000 description 1
- 108010051219 Cre recombinase Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 102100029363 Cytochrome P450 2C19 Human genes 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
- 230000004544 DNA amplification Effects 0.000 description 1
- 101710177611 DNA polymerase II large subunit Proteins 0.000 description 1
- 101710184669 DNA polymerase II small subunit Proteins 0.000 description 1
- 230000006820 DNA synthesis Effects 0.000 description 1
- 108700020911 DNA-Binding Proteins Proteins 0.000 description 1
- 101710096438 DNA-binding protein Proteins 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
- 208000002249 Diabetes Complications Diseases 0.000 description 1
- 206010012655 Diabetic complications Diseases 0.000 description 1
- 102100034581 Dihydroorotase Human genes 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- 241000255601 Drosophila melanogaster Species 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 108010059378 Endopeptidases Proteins 0.000 description 1
- 102000005593 Endopeptidases Human genes 0.000 description 1
- 241000792859 Enema Species 0.000 description 1
- 108010013369 Enteropeptidase Proteins 0.000 description 1
- 102100029727 Enteropeptidase Human genes 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 241000588722 Escherichia Species 0.000 description 1
- 241000702191 Escherichia virus P1 Species 0.000 description 1
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 206010015548 Euthanasia Diseases 0.000 description 1
- 102000018389 Exopeptidases Human genes 0.000 description 1
- 108010091443 Exopeptidases Proteins 0.000 description 1
- 108010046276 FLP recombinase Proteins 0.000 description 1
- 108010074860 Factor Xa Proteins 0.000 description 1
- 102100028072 Fibroblast growth factor 4 Human genes 0.000 description 1
- 229920001917 Ficoll Polymers 0.000 description 1
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 1
- GHASVSINZRGABV-UHFFFAOYSA-N Fluorouracil Chemical compound FC1=CNC(=O)NC1=O GHASVSINZRGABV-UHFFFAOYSA-N 0.000 description 1
- 102000003688 G-Protein-Coupled Receptors Human genes 0.000 description 1
- 108090000045 G-Protein-Coupled Receptors Proteins 0.000 description 1
- 230000035519 G0 Phase Effects 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- 241000288105 Grus Species 0.000 description 1
- 206010018910 Haemolysis Diseases 0.000 description 1
- 102000001554 Hemoglobins Human genes 0.000 description 1
- 108010054147 Hemoglobins Proteins 0.000 description 1
- 241001272567 Hominoidea Species 0.000 description 1
- 101000690301 Homo sapiens Aldo-keto reductase family 1 member C4 Proteins 0.000 description 1
- 101001116548 Homo sapiens Protein CBFA2T1 Proteins 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 241000701109 Human adenovirus 2 Species 0.000 description 1
- 241000725303 Human immunodeficiency virus Species 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
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 1
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 1
- 206010061216 Infarction Diseases 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 229930010555 Inosine Natural products 0.000 description 1
- UGQMRVRMYYASKQ-KQYNXXCUSA-N Inosine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C2=NC=NC(O)=C2N=C1 UGQMRVRMYYASKQ-KQYNXXCUSA-N 0.000 description 1
- 102100034349 Integrase Human genes 0.000 description 1
- 101710203526 Integrase Proteins 0.000 description 1
- 108090000862 Ion Channels Proteins 0.000 description 1
- 102000004310 Ion Channels Human genes 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- 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 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 108010006444 Leucine-Rich Repeat Proteins Proteins 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
- 102000043136 MAP kinase family Human genes 0.000 description 1
- 108091054455 MAP kinase family Proteins 0.000 description 1
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 235000006679 Mentha X verticillata Nutrition 0.000 description 1
- 235000002899 Mentha suaveolens Nutrition 0.000 description 1
- 235000001636 Mentha x rotundifolia Nutrition 0.000 description 1
- IMTUWVJPCQPJEE-IUCAKERBSA-N Met-Lys Chemical compound CSCC[C@H](N)C(=O)N[C@H](C(O)=O)CCCCN IMTUWVJPCQPJEE-IUCAKERBSA-N 0.000 description 1
- 102000003792 Metallothionein Human genes 0.000 description 1
- 108090000157 Metallothionein Proteins 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 241000713333 Mouse mammary tumor virus Species 0.000 description 1
- 101100001708 Mus musculus Angptl4 gene Proteins 0.000 description 1
- 101000931108 Mus musculus DNA (cytosine-5)-methyltransferase 1 Proteins 0.000 description 1
- 101001130249 Mus musculus Reticulon-4 receptor-like 1 Proteins 0.000 description 1
- 101000798092 Mus musculus tRNA (cytosine(38)-C(5))-methyltransferase Proteins 0.000 description 1
- 108010021466 Mutant Proteins Proteins 0.000 description 1
- 102000008300 Mutant Proteins Human genes 0.000 description 1
- 241001467552 Mycobacterium bovis BCG Species 0.000 description 1
- 102000003505 Myosin Human genes 0.000 description 1
- 108060008487 Myosin Proteins 0.000 description 1
- 101000860173 Myxococcus xanthus C-factor Proteins 0.000 description 1
- 125000000534 N(2)-L-lysino group Chemical group [H]OC(=O)[C@@]([H])(N([H])[*])C([H])([H])C([H])([H])C(C([H])([H])N([H])[H])([H])[H] 0.000 description 1
- SGSSKEDGVONRGC-UHFFFAOYSA-N N(2)-methylguanine Chemical compound O=C1NC(NC)=NC2=C1N=CN2 SGSSKEDGVONRGC-UHFFFAOYSA-N 0.000 description 1
- NQTADLQHYWFPDB-UHFFFAOYSA-N N-Hydroxysuccinimide Chemical compound ON1C(=O)CCC1=O NQTADLQHYWFPDB-UHFFFAOYSA-N 0.000 description 1
- WHNWPMSKXPGLAX-UHFFFAOYSA-N N-Vinyl-2-pyrrolidone Chemical compound C=CN1CCCC1=O WHNWPMSKXPGLAX-UHFFFAOYSA-N 0.000 description 1
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
- 238000011887 Necropsy Methods 0.000 description 1
- 241000244206 Nematoda Species 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 208000012902 Nervous system disease Diseases 0.000 description 1
- 108010088373 Neurofilament Proteins Proteins 0.000 description 1
- 102000008763 Neurofilament Proteins Human genes 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 208000008589 Obesity Diseases 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108700020796 Oncogene Proteins 0.000 description 1
- 208000012868 Overgrowth Diseases 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 244000046052 Phaseolus vulgaris Species 0.000 description 1
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 1
- 108010064785 Phospholipases Proteins 0.000 description 1
- 102000015439 Phospholipases Human genes 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 241000235648 Pichia Species 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 1
- 229920002732 Polyanhydride Polymers 0.000 description 1
- 239000004698 Polyethylene Substances 0.000 description 1
- 229920000954 Polyglycolide Polymers 0.000 description 1
- 229920001710 Polyorthoester Polymers 0.000 description 1
- 229920002685 Polyoxyl 35CastorOil Polymers 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 241000125945 Protoparvovirus Species 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 201000004681 Psoriasis Diseases 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 108020005091 Replication Origin Proteins 0.000 description 1
- 206010038997 Retroviral infections Diseases 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 241000714474 Rous sarcoma virus Species 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 241000251131 Sphyrna Species 0.000 description 1
- 241000191940 Staphylococcus Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 108091008874 T cell receptors Proteins 0.000 description 1
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
- 108700026226 TATA Box Proteins 0.000 description 1
- 241000223892 Tetrahymena Species 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 102000006601 Thymidine Kinase Human genes 0.000 description 1
- 108020004440 Thymidine kinase Proteins 0.000 description 1
- 229920001615 Tragacanth Polymers 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 229920004929 Triton X-114 Polymers 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 108091023045 Untranslated Region Proteins 0.000 description 1
- 229910052770 Uranium Inorganic materials 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 239000005862 Whey Substances 0.000 description 1
- 102000007544 Whey Proteins Human genes 0.000 description 1
- 108010046377 Whey Proteins Proteins 0.000 description 1
- 241000269368 Xenopus laevis Species 0.000 description 1
- MMWCIQZXVOZEGG-HOZKJCLWSA-N [(1S,2R,3S,4S,5R,6S)-2,3,5-trihydroxy-4,6-diphosphonooxycyclohexyl] dihydrogen phosphate Chemical compound O[C@H]1[C@@H](O)[C@H](OP(O)(O)=O)[C@@H](OP(O)(O)=O)[C@H](O)[C@H]1OP(O)(O)=O MMWCIQZXVOZEGG-HOZKJCLWSA-N 0.000 description 1
- RJZZTNAWUTTWMJ-WYIOVZGUSA-N [(2r,3s,5s)-5-amino-2-[2-(4-methoxyphenyl)-2,2-diphenylethyl]-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-3-yl]oxyphosphonamidous acid Chemical compound C1=CC(OC)=CC=C1C(C=1C=CC=CC=1)(C=1C=CC=CC=1)C[C@@H]1[C@@H](OP(N)O)C[C@](N)(N2C(NC(=O)C(C)=C2)=O)O1 RJZZTNAWUTTWMJ-WYIOVZGUSA-N 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 150000001242 acetic acid derivatives Chemical class 0.000 description 1
- 229940022698 acetylcholinesterase Drugs 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 125000000641 acridinyl group Chemical group C1(=CC=CC2=NC3=CC=CC=C3C=C12)* 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 230000010933 acylation Effects 0.000 description 1
- 230000002730 additional effect Effects 0.000 description 1
- 229960000643 adenine Drugs 0.000 description 1
- 102000030621 adenylate cyclase Human genes 0.000 description 1
- 108060000200 adenylate cyclase Proteins 0.000 description 1
- 230000006838 adverse reaction Effects 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- 238000000787 affinity precipitation Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 125000003172 aldehyde group Chemical group 0.000 description 1
- 235000010443 alginic acid Nutrition 0.000 description 1
- 229920000615 alginic acid Polymers 0.000 description 1
- 230000029936 alkylation Effects 0.000 description 1
- 230000003281 allosteric effect Effects 0.000 description 1
- 239000012637 allosteric effector Substances 0.000 description 1
- 108010026331 alpha-Fetoproteins Proteins 0.000 description 1
- VREFGVBLTWBCJP-UHFFFAOYSA-N alprazolam Chemical compound C12=CC(Cl)=CC=C2N2C(C)=NN=C2CN=C1C1=CC=CC=C1 VREFGVBLTWBCJP-UHFFFAOYSA-N 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 230000000202 analgesic effect Effects 0.000 description 1
- 229940035676 analgesics Drugs 0.000 description 1
- 238000004873 anchoring Methods 0.000 description 1
- 230000033115 angiogenesis Effects 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 230000003042 antagnostic effect Effects 0.000 description 1
- 239000000730 antalgic agent Substances 0.000 description 1
- 230000001093 anti-cancer Effects 0.000 description 1
- 230000000843 anti-fungal effect Effects 0.000 description 1
- 229940121363 anti-inflammatory agent Drugs 0.000 description 1
- 239000002260 anti-inflammatory agent Substances 0.000 description 1
- 230000003110 anti-inflammatory effect Effects 0.000 description 1
- 230000000078 anti-malarial effect Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000003429 antifungal agent Substances 0.000 description 1
- 239000003430 antimalarial agent Substances 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 235000006708 antioxidants Nutrition 0.000 description 1
- 238000003782 apoptosis assay Methods 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 125000004429 atom Chemical group 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 229960000190 bacillus calmette–guérin vaccine Drugs 0.000 description 1
- 230000003385 bacteriostatic effect Effects 0.000 description 1
- 230000006399 behavior Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- DZBUGLKDJFMEHC-UHFFFAOYSA-N benzoquinolinylidene Natural products C1=CC=CC2=CC3=CC=CC=C3N=C21 DZBUGLKDJFMEHC-UHFFFAOYSA-N 0.000 description 1
- 235000019445 benzyl alcohol Nutrition 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 239000003833 bile salt Substances 0.000 description 1
- 229940093761 bile salts Drugs 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 229920002988 biodegradable polymer Polymers 0.000 description 1
- 239000004621 biodegradable polymer Substances 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000008512 biological response Effects 0.000 description 1
- 239000012472 biological sample Substances 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 229940088623 biologically active substance Drugs 0.000 description 1
- 239000000090 biomarker Substances 0.000 description 1
- 230000006287 biotinylation Effects 0.000 description 1
- 238000007413 biotinylation Methods 0.000 description 1
- 210000002459 blastocyst Anatomy 0.000 description 1
- 210000001109 blastomere Anatomy 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 230000008499 blood brain barrier function Effects 0.000 description 1
- 239000012503 blood component Substances 0.000 description 1
- 238000004820 blood count Methods 0.000 description 1
- 210000001218 blood-brain barrier Anatomy 0.000 description 1
- 210000005013 brain tissue Anatomy 0.000 description 1
- 235000010633 broth Nutrition 0.000 description 1
- DQXBYHZEEUGOBF-UHFFFAOYSA-N but-3-enoic acid;ethene Chemical compound C=C.OC(=O)CC=C DQXBYHZEEUGOBF-UHFFFAOYSA-N 0.000 description 1
- 101150057411 cII gene Proteins 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 229910001424 calcium ion Inorganic materials 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 230000023549 cell-cell signaling Effects 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 230000005754 cellular signaling Effects 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 201000007455 central nervous system cancer Diseases 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 230000003196 chaotropic effect Effects 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 230000009920 chelation Effects 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- 229960004926 chlorobutanol Drugs 0.000 description 1
- 235000012000 cholesterol Nutrition 0.000 description 1
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Natural products C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 150000001860 citric acid derivatives Chemical class 0.000 description 1
- 230000002566 clonic effect Effects 0.000 description 1
- 238000012411 cloning technique Methods 0.000 description 1
- 229960004126 codeine Drugs 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 229940075614 colloidal silicon dioxide Drugs 0.000 description 1
- 230000009137 competitive binding Effects 0.000 description 1
- 230000006957 competitive inhibition Effects 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 238000005094 computer simulation Methods 0.000 description 1
- 238000013270 controlled release Methods 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- 239000008120 corn starch Substances 0.000 description 1
- 229940099112 cornstarch Drugs 0.000 description 1
- 239000006184 cosolvent Substances 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 229960003624 creatine Drugs 0.000 description 1
- 239000006046 creatine Substances 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- 229960003280 cupric chloride Drugs 0.000 description 1
- OOTFVKOQINZBBF-UHFFFAOYSA-N cystamine Chemical compound CCSSCCN OOTFVKOQINZBBF-UHFFFAOYSA-N 0.000 description 1
- 229940099500 cystamine Drugs 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N cystine group Chemical group C([C@@H](C(=O)O)N)SSC[C@@H](C(=O)O)N LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 210000000172 cytosol Anatomy 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 125000001295 dansyl group Chemical group [H]C1=C([H])C(N(C([H])([H])[H])C([H])([H])[H])=C2C([H])=C([H])C([H])=C(C2=C1[H])S(*)(=O)=O 0.000 description 1
- 230000009849 deactivation Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000001934 delay Effects 0.000 description 1
- 230000002074 deregulated effect Effects 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- UGMCXQCYOVCMTB-UHFFFAOYSA-K dihydroxy(stearato)aluminium Chemical compound CCCCCCCCCCCCCCCCCC(=O)O[Al](O)O UGMCXQCYOVCMTB-UHFFFAOYSA-K 0.000 description 1
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 230000007783 downstream signaling Effects 0.000 description 1
- 230000002500 effect on skin Effects 0.000 description 1
- 230000005684 electric field Effects 0.000 description 1
- 230000013020 embryo development Effects 0.000 description 1
- 210000002308 embryonic cell Anatomy 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 239000006274 endogenous ligand Substances 0.000 description 1
- 229940066758 endopeptidases Drugs 0.000 description 1
- 239000007920 enema Substances 0.000 description 1
- 229940079360 enema for constipation Drugs 0.000 description 1
- 239000003344 environmental pollutant Substances 0.000 description 1
- 238000001952 enzyme assay Methods 0.000 description 1
- 238000001976 enzyme digestion Methods 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- RTZKZFJDLAIYFH-UHFFFAOYSA-N ether Substances CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 1
- 239000005038 ethylene vinyl acetate Substances 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 230000003631 expected effect Effects 0.000 description 1
- 238000001400 expression cloning Methods 0.000 description 1
- 239000000284 extract Substances 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
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 230000003176 fibrotic effect Effects 0.000 description 1
- 239000000796 flavoring agent Substances 0.000 description 1
- 238000005206 flow analysis Methods 0.000 description 1
- 238000002875 fluorescence polarization Methods 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 229960002949 fluorouracil Drugs 0.000 description 1
- 235000013355 food flavoring agent Nutrition 0.000 description 1
- 230000037406 food intake Effects 0.000 description 1
- 235000003599 food sweetener Nutrition 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 239000003205 fragrance Substances 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 238000010230 functional analysis Methods 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- IECPWNUMDGFDKC-MZJAQBGESA-M fusidate Chemical class O[C@@H]([C@@H]12)C[C@H]3\C(=C(/CCC=C(C)C)C([O-])=O)[C@@H](OC(C)=O)C[C@]3(C)[C@@]2(C)CC[C@@H]2[C@]1(C)CC[C@@H](O)[C@H]2C IECPWNUMDGFDKC-MZJAQBGESA-M 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 239000007903 gelatin capsule Substances 0.000 description 1
- 238000001476 gene delivery Methods 0.000 description 1
- 230000004077 genetic alteration Effects 0.000 description 1
- 231100000118 genetic alteration Toxicity 0.000 description 1
- 235000003869 genetically modified organism Nutrition 0.000 description 1
- 238000003205 genotyping method Methods 0.000 description 1
- 208000005017 glioblastoma Diseases 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 125000005456 glyceride group Chemical group 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 150000002357 guanidines Chemical class 0.000 description 1
- 229940083094 guanine derivative acting on arteriolar smooth muscle Drugs 0.000 description 1
- 230000008588 hemolysis Effects 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 238000000265 homogenisation Methods 0.000 description 1
- 229920001519 homopolymer Polymers 0.000 description 1
- 102000054751 human RUNX1T1 Human genes 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- OROGSEYTTFOCAN-UHFFFAOYSA-N hydrocodone Natural products C1C(N(CCC234)C)C2C=CC(O)C3OC2=C4C1=CC=C2OC OROGSEYTTFOCAN-UHFFFAOYSA-N 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 150000002431 hydrogen Chemical class 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 238000003384 imaging method Methods 0.000 description 1
- 230000008086 immune related sensitivity Effects 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 239000003547 immunosorbent Substances 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 239000003701 inert diluent Substances 0.000 description 1
- 230000007574 infarction Effects 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 229960003786 inosine Drugs 0.000 description 1
- 239000000138 intercalating agent Substances 0.000 description 1
- 239000000543 intermediate Substances 0.000 description 1
- 230000004068 intracellular signaling Effects 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 238000001038 ionspray mass spectrometry Methods 0.000 description 1
- 150000002540 isothiocyanates Chemical class 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 101150066555 lacZ gene Proteins 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- IZWSFJTYBVKZNK-UHFFFAOYSA-N lauryl sulfobetaine Chemical compound CCCCCCCCCCCC[N+](C)(C)CCCS([O-])(=O)=O IZWSFJTYBVKZNK-UHFFFAOYSA-N 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 210000004901 leucine-rich repeat Anatomy 0.000 description 1
- 230000029226 lipidation Effects 0.000 description 1
- 238000001638 lipofection Methods 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 239000000314 lubricant Substances 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 108010026228 mRNA guanylyltransferase Proteins 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 229940057948 magnesium stearate Drugs 0.000 description 1
- 238000002595 magnetic resonance imaging Methods 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 210000005075 mammary gland Anatomy 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 210000003574 melanophore Anatomy 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 229940095102 methyl benzoate Drugs 0.000 description 1
- 150000004702 methyl esters Chemical class 0.000 description 1
- YACKEPLHDIMKIO-UHFFFAOYSA-N methylphosphonic acid Chemical compound CP(O)(O)=O YACKEPLHDIMKIO-UHFFFAOYSA-N 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 238000002493 microarray Methods 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 239000002480 mineral oil Substances 0.000 description 1
- 235000010446 mineral oil Nutrition 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229960005181 morphine Drugs 0.000 description 1
- 210000000472 morula Anatomy 0.000 description 1
- 239000002324 mouth wash Substances 0.000 description 1
- 229940051866 mouthwash Drugs 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- XJVXMWNLQRTRGH-UHFFFAOYSA-N n-(3-methylbut-3-enyl)-2-methylsulfanyl-7h-purin-6-amine Chemical compound CSC1=NC(NCCC(C)=C)=C2NC=NC2=N1 XJVXMWNLQRTRGH-UHFFFAOYSA-N 0.000 description 1
- UMWKZHPREXJQGR-XOSAIJSUSA-N n-methyl-n-[(2s,3r,4r,5r)-2,3,4,5,6-pentahydroxyhexyl]decanamide Chemical compound CCCCCCCCCC(=O)N(C)C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO UMWKZHPREXJQGR-XOSAIJSUSA-N 0.000 description 1
- SBWGZAXBCCNRTM-CTHBEMJXSA-N n-methyl-n-[(2s,3r,4r,5r)-2,3,4,5,6-pentahydroxyhexyl]octanamide Chemical compound CCCCCCCC(=O)N(C)C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO SBWGZAXBCCNRTM-CTHBEMJXSA-N 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 239000006199 nebulizer Substances 0.000 description 1
- 230000017997 negative regulation of axon regeneration Effects 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 230000001537 neural effect Effects 0.000 description 1
- 208000015122 neurodegenerative disease Diseases 0.000 description 1
- 210000005044 neurofilament Anatomy 0.000 description 1
- 230000014511 neuron projection development Effects 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 239000002547 new drug Substances 0.000 description 1
- 229910052759 nickel Inorganic materials 0.000 description 1
- 239000002687 nonaqueous vehicle Substances 0.000 description 1
- 230000036963 noncompetitive effect Effects 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- 210000004940 nucleus Anatomy 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 235000020824 obesity Nutrition 0.000 description 1
- HEGSGKPQLMEBJL-RKQHYHRCSA-N octyl beta-D-glucopyranoside Chemical compound CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O HEGSGKPQLMEBJL-RKQHYHRCSA-N 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- QUANRIQJNFHVEU-UHFFFAOYSA-N oxirane;propane-1,2,3-triol Chemical compound C1CO1.OCC(O)CO QUANRIQJNFHVEU-UHFFFAOYSA-N 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 244000045947 parasite Species 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 230000008447 perception Effects 0.000 description 1
- 210000000578 peripheral nerve Anatomy 0.000 description 1
- 210000001428 peripheral nervous system Anatomy 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 239000008177 pharmaceutical agent Substances 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 229960003742 phenol Drugs 0.000 description 1
- 235000021317 phosphate Nutrition 0.000 description 1
- 125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 1
- 150000003906 phosphoinositides Chemical class 0.000 description 1
- 150000008300 phosphoramidites Chemical class 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 230000010399 physical interaction Effects 0.000 description 1
- 238000000053 physical method Methods 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 231100000719 pollutant Toxicity 0.000 description 1
- 229920001983 poloxamer Polymers 0.000 description 1
- 229920000729 poly(L-lysine) polymer Polymers 0.000 description 1
- 229920000191 poly(N-vinyl pyrrolidone) Polymers 0.000 description 1
- 229920001200 poly(ethylene-vinyl acetate) Polymers 0.000 description 1
- 229920000747 poly(lactic acid) Polymers 0.000 description 1
- 229920001583 poly(oxyethylated polyols) Polymers 0.000 description 1
- 229920000447 polyanionic polymer Polymers 0.000 description 1
- 239000008389 polyethoxylated castor oil Substances 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 229930001119 polyketide Natural products 0.000 description 1
- 125000000830 polyketide group Chemical group 0.000 description 1
- 229930001118 polyketide hybrid Natural products 0.000 description 1
- 125000003308 polyketide hybrid group Chemical group 0.000 description 1
- 229920000656 polylysine Polymers 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- 230000005522 programmed cell death Effects 0.000 description 1
- 230000009465 prokaryotic expression Effects 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 239000003380 propellant Substances 0.000 description 1
- QQONPFPTGQHPMA-UHFFFAOYSA-N propylene Natural products CC=C QQONPFPTGQHPMA-UHFFFAOYSA-N 0.000 description 1
- 125000004805 propylene group Chemical group [H]C([H])([H])C([H])([*:1])C([H])([H])[*:2] 0.000 description 1
- QELSKZZBTMNZEB-UHFFFAOYSA-N propylparaben Chemical compound CCCOC(=O)C1=CC=C(O)C=C1 QELSKZZBTMNZEB-UHFFFAOYSA-N 0.000 description 1
- 229960003415 propylparaben Drugs 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 108020001580 protein domains Proteins 0.000 description 1
- 230000006920 protein precipitation Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 238000000734 protein sequencing Methods 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 208000020016 psychiatric disease Diseases 0.000 description 1
- 235000021251 pulses Nutrition 0.000 description 1
- 239000000376 reactant Substances 0.000 description 1
- 101150079601 recA gene Proteins 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000006722 reduction reaction Methods 0.000 description 1
- 238000005932 reductive alkylation reaction Methods 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 238000007894 restriction fragment length polymorphism technique Methods 0.000 description 1
- 210000001525 retina Anatomy 0.000 description 1
- 230000001177 retroviral effect Effects 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- CVHZOJJKTDOEJC-UHFFFAOYSA-N saccharin Chemical compound C1=CC=C2C(=O)NS(=O)(=O)C2=C1 CVHZOJJKTDOEJC-UHFFFAOYSA-N 0.000 description 1
- 229940081974 saccharin Drugs 0.000 description 1
- 235000019204 saccharin Nutrition 0.000 description 1
- 239000000901 saccharin and its Na,K and Ca salt Substances 0.000 description 1
- 229960001860 salicylate Drugs 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 238000003345 scintillation counting Methods 0.000 description 1
- 238000012106 screening analysis Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000005204 segregation Methods 0.000 description 1
- 238000010187 selection method Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 230000003393 splenic effect Effects 0.000 description 1
- 238000003153 stable transfection Methods 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 229940124530 sulfonamide Drugs 0.000 description 1
- 150000003456 sulfonamides Chemical class 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 239000003765 sweetening agent Substances 0.000 description 1
- 230000000946 synaptic effect Effects 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 239000000454 talc Substances 0.000 description 1
- 235000012222 talc Nutrition 0.000 description 1
- 229910052623 talc Inorganic materials 0.000 description 1
- 229940033134 talc Drugs 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 208000001608 teratocarcinoma Diseases 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 238000011285 therapeutic regimen Methods 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
- ZEMGGZBWXRYJHK-UHFFFAOYSA-N thiouracil Chemical compound O=C1C=CNC(=S)N1 ZEMGGZBWXRYJHK-UHFFFAOYSA-N 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 108091006106 transcriptional activators Proteins 0.000 description 1
- 108091006107 transcriptional repressors Proteins 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 238000011269 treatment regimen Methods 0.000 description 1
- 230000004614 tumor growth Effects 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- ORHBXUUXSCNDEV-UHFFFAOYSA-N umbelliferone Chemical compound C1=CC(=O)OC2=CC(O)=CC=C21 ORHBXUUXSCNDEV-UHFFFAOYSA-N 0.000 description 1
- HFTAFOQKODTIJY-UHFFFAOYSA-N umbelliferone Natural products Cc1cc2C=CC(=O)Oc2cc1OCC=CC(C)(C)O HFTAFOQKODTIJY-UHFFFAOYSA-N 0.000 description 1
- 241001529453 unidentified herpesvirus Species 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 229940035893 uracil Drugs 0.000 description 1
- 150000003672 ureas Chemical class 0.000 description 1
- 229960005486 vaccine Drugs 0.000 description 1
- 238000001291 vacuum drying Methods 0.000 description 1
- 230000004862 vasculogenesis Effects 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000008215 water for injection Substances 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 210000004885 white matter Anatomy 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
- 229940075420 xanthine Drugs 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- 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
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
-
- 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
- G01N33/6896—Neurological disorders, e.g. Alzheimer's disease
-
- 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
- G01N33/74—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving hormones or other non-cytokine intercellular protein regulatory factors such as growth factors, including receptors to hormones and growth factors
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2500/00—Screening for compounds of potential therapeutic value
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Hematology (AREA)
- Biochemistry (AREA)
- Urology & Nephrology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Cell Biology (AREA)
- Physics & Mathematics (AREA)
- Pathology (AREA)
- General Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Food Science & Technology (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Neurology (AREA)
- Neurosurgery (AREA)
- Animal Behavior & Ethology (AREA)
- Zoology (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Veterinary Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Public Health (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Gastroenterology & Hepatology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Toxicology (AREA)
- Endocrinology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US23836100P | 2000-10-06 | 2000-10-06 | |
| US238361P | 2000-10-06 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2341608T3 true ES2341608T3 (es) | 2010-06-23 |
Family
ID=22897532
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES01979595T Expired - Lifetime ES2341608T3 (es) | 2000-10-06 | 2001-10-06 | Homologos del receptor de nogo. |
Country Status (12)
| Country | Link |
|---|---|
| US (5) | US20030124704A1 (enExample) |
| EP (1) | EP1325130B1 (enExample) |
| JP (2) | JP4465148B2 (enExample) |
| AT (1) | ATE458815T1 (enExample) |
| AU (2) | AU2002211539B2 (enExample) |
| CA (1) | CA2424834A1 (enExample) |
| DE (1) | DE60141409D1 (enExample) |
| DK (1) | DK1325130T3 (enExample) |
| ES (1) | ES2341608T3 (enExample) |
| NZ (1) | NZ525422A (enExample) |
| PT (1) | PT1325130E (enExample) |
| WO (1) | WO2002029059A2 (enExample) |
Families Citing this family (37)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7119165B2 (en) | 2000-01-12 | 2006-10-10 | Yale University | Nogo receptor-mediated blockade of axonal growth |
| DE60141409D1 (de) * | 2000-10-06 | 2010-04-08 | Biogen Idec Inc | Homologe des nogo rezeptors |
| JP2005507246A (ja) * | 2001-08-27 | 2005-03-17 | ノバルティス アクチエンゲゼルシャフト | Ｎｏｇｏレセプターホモログおよびそれらの使用 |
| JP2005519584A (ja) * | 2001-10-22 | 2005-07-07 | ノバルティス アクチエンゲゼルシャフト | Ｎｏｇｏレセプターホモログおよびそれらの使用 |
| US7309485B2 (en) * | 2001-12-03 | 2007-12-18 | Children's Medical Center Corporation | Reducing myelin-mediated inhibition of axon regeneration |
| JPWO2004005510A1 (ja) * | 2002-07-05 | 2005-11-04 | 塩野義製薬株式会社 | 新規Ｎｏｇｏ受容体様ポリペプチドおよびそのＤＮＡ |
| MXPA05001615A (es) | 2002-08-10 | 2005-08-19 | Biogen Idec Inc | Antagonistas del nogo receptor. |
| EP2248899B8 (en) * | 2003-03-19 | 2015-07-15 | Biogen MA Inc. | NOGO receptor binding protein |
| US7541335B2 (en) | 2003-04-04 | 2009-06-02 | University Of Rochester | Nogo-receptors and methods of use |
| AU2004231742A1 (en) * | 2003-04-16 | 2004-11-04 | Biogen Idec Ma Inc. | Nogo-receptor antagonists for the treatment of conditions involving amyloid plaques |
| US20080274112A1 (en) * | 2003-08-07 | 2008-11-06 | Lee Daniel H S | Nogo Receptor Antagonists |
| US8912144B2 (en) * | 2003-12-16 | 2014-12-16 | Children's Medical Center Corporation | Method for treating stroke via administration of NEP1-40 and inosine |
| WO2005059515A2 (en) * | 2003-12-16 | 2005-06-30 | Children's Medical Center Corporation | Method for treating neurological disorders |
| AU2005210621B2 (en) * | 2004-01-30 | 2009-10-01 | Biogen Idec Ma Inc. | Treatment of conditions involving dopaminergic neuronal degeneration using nogo receptor antagonists |
| EP2474317A1 (en) | 2004-06-24 | 2012-07-11 | Biogen Idec MA Inc. | Treatment of conditions involving demyelination |
| WO2006047049A2 (en) * | 2004-10-01 | 2006-05-04 | Yale University | Nogo-a polypeptide fragments, variant nogo receptor-1 polypeptides, and uses thereof |
| EP1904091A4 (en) * | 2005-07-07 | 2009-12-23 | Univ Yale | COMPOSITIONS AND METHODS FOR SUPPRESSING THE INHIBITION OF AXON GROWTH |
| WO2007008547A2 (en) | 2005-07-08 | 2007-01-18 | Biogen Idec Ma Inc. | Sp35 antibodies and uses thereof |
| WO2007025219A2 (en) * | 2005-08-25 | 2007-03-01 | Biogen Idec Ma Inc. | Nogo receptor polypeptides and polypeptide fragments and uses thereof |
| WO2007089601A2 (en) | 2006-01-27 | 2007-08-09 | Biogen Idec Ma Inc. | Nogo receptor antagonists |
| EP2023735A4 (en) * | 2006-05-15 | 2011-05-25 | Biogen Idec Inc | USE OF ANTAGONISTS OF THE NOGO RECEPTOR 1 (NGR1) TO PROMOTE THE SURVIVAL OF OLIGODENDROCYTES |
| US20080025959A1 (en) * | 2006-05-24 | 2008-01-31 | Richard Daneman | Permeability of blood-brain barrier |
| KR20090082480A (ko) | 2006-11-14 | 2009-07-30 | 제넨테크, 인크. | 뉴런 재생의 조절인자 |
| US20100047232A1 (en) * | 2006-11-14 | 2010-02-25 | Jasvinder Atwal | Modulators of neuronal regeneration |
| WO2009009743A2 (en) * | 2007-07-12 | 2009-01-15 | Institute For Advance Study | Sequence optimization for expression of a foreign gene |
| AU2008335245A1 (en) * | 2007-12-11 | 2009-06-18 | Genentech, Inc. | Modulators of neuronal regeneration |
| US8992918B2 (en) | 2008-03-13 | 2015-03-31 | Yale University | Reactivation of axon growth and recovery in chronic spinal cord injury |
| US20090285803A1 (en) * | 2008-05-13 | 2009-11-19 | Jasvinder Atwal | ANTI-PirB ANTIBODIES |
| JP2011527572A (ja) | 2008-07-09 | 2011-11-04 | 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 | Ｌｉｎｇｏ抗体または断片を含む組成物 |
| EP2392208B1 (en) * | 2010-06-07 | 2016-05-04 | Helmholtz Zentrum München Deutsches Forschungszentrum für Gesundheit und Umwelt (GmbH) | Fusion proteins comprising a DNA-binding domain of a Tal effector protein and a non-specific cleavage domain of a restriction nuclease and their use |
| US9120111B2 (en) | 2012-02-24 | 2015-09-01 | Rain Bird Corporation | Arc adjustable rotary sprinkler having full-circle operation and automatic matched precipitation |
| JP2015518829A (ja) | 2012-05-14 | 2015-07-06 | バイオジェン・エムエイ・インコーポレイテッドＢｉｏｇｅｎ ＭＡ Ｉｎｃ． | 運動ニューロンに関する状態の処置のためのｌｉｎｇｏ−２アンタゴニスト |
| US9156043B2 (en) | 2012-07-13 | 2015-10-13 | Rain Bird Corporation | Arc adjustable rotary sprinkler with automatic matched precipitation |
| AU2016205197B2 (en) | 2015-01-08 | 2021-10-21 | Biogen Ma Inc. | LINGO-1 antagonists and uses for treatment of demyelinating disorders |
| US12343748B2 (en) | 2021-03-16 | 2025-07-01 | Rain Bird Corporation | Multi-mode rotor sprinkler apparatus and method |
| US12434252B2 (en) | 2022-04-20 | 2025-10-07 | Rain Bird Corporation | Full-circle and part-circle rotor sprinkler |
| US12440855B2 (en) | 2022-10-27 | 2025-10-14 | Rain Bird Corporation | Multi-mode rotor sprinkler apparatus and method |
Family Cites Families (27)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5250414A (en) | 1988-11-04 | 1993-10-05 | Erziehungsdirektion Of The Canton Zurich | Diagnostic methods using neurite growth regulatory factors |
| AU652537B2 (en) | 1988-11-04 | 1994-09-01 | Erziehungsdirektion Of The Canton Zurich | Neurite growth regulatory factors |
| CA1341050C (en) | 1988-11-04 | 2000-07-11 | Martin E. Schwab | Neurite growth regulatory factors |
| EP0634939A1 (en) | 1993-02-11 | 1995-01-25 | Erziehungsdirektion Of The Canton Zurich | A combination of neurotrophin and antibody directed toward myelin-associated neurite growth inhibitory protein promotes central nervous system regeneration |
| WO2000073452A2 (en) | 1999-06-02 | 2000-12-07 | Genentech, Inc. | Compositions and methods for the treatment of immune related diseases |
| US5858708A (en) | 1996-08-12 | 1999-01-12 | Bandman; Olga | Polynucleotides encoding two novel human neuroendocrine-specific proteins |
| WO1999066041A1 (en) | 1998-06-16 | 1999-12-23 | Human Genome Sciences, Inc. | 94 human secreted proteins |
| WO2000070050A1 (en) | 1999-05-14 | 2000-11-23 | Genentech, Inc. | Compositions and methods for the treatment of immune related diseases |
| EP1002132A4 (en) * | 1997-08-05 | 2005-04-27 | Human Genome Sciences Inc | HUMAN SECRETED PROTEINS |
| DK1490386T3 (da) | 1998-03-10 | 2008-12-15 | Genentech Inc | Nyt polypeptid og nukleinsyrer kodende for dette |
| EP2264174A3 (en) | 1998-07-22 | 2012-03-07 | SmithKline Beecham Limited | Protein similar to neuroendocrine-specific protein, and encoding CDNA |
| HUP0301829A3 (en) * | 1998-11-06 | 2009-03-30 | Schwab | Nucleotidok and protein sequences of nogo genes and methods based thereon |
| ATE458050T1 (de) | 1998-12-01 | 2010-03-15 | Genentech Inc | Promotion oder inhibition von angiogenese und kardiovaskularisation |
| JP3993746B2 (ja) | 1998-12-22 | 2007-10-17 | ジェネンテック・インコーポレーテッド | 腫瘍性細胞成長阻害のための組成物及び方法 |
| AU2883600A (en) | 1999-03-08 | 2000-09-28 | Genentech Inc. | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
| KR20010103046A (ko) | 1999-03-08 | 2001-11-17 | 제넨테크, 인크. | 면역 관련 질환 치료용 조성물 및 치료 방법 |
| JP2004507202A (ja) | 1999-03-31 | 2004-03-11 | キュラジェン コーポレイション | ポリペプチドをコードするオープンリーディングフレームを含む核酸；「ｏｒｆｘ」 |
| AU6394400A (en) | 1999-07-30 | 2001-02-19 | Millennium Pharmaceuticals, Inc. | Secreted proteins and uses thereof |
| WO2001042286A2 (en) | 1999-12-08 | 2001-06-14 | Millennium Pharmaceuticals, Inc. | Human leucine rich repeat-containing polypeptide and uses therefor |
| PL356887A1 (en) * | 2000-01-12 | 2004-07-12 | Yale University | Nogo receptor-mediated blockade of axonal growth |
| US7119165B2 (en) * | 2000-01-12 | 2006-10-10 | Yale University | Nogo receptor-mediated blockade of axonal growth |
| US6436703B1 (en) * | 2000-03-31 | 2002-08-20 | Hyseq, Inc. | Nucleic acids and polypeptides |
| EP1275411A4 (en) | 2000-04-18 | 2006-04-05 | Teijin Ltd | OXYGEN |
| DE60141409D1 (de) * | 2000-10-06 | 2010-04-08 | Biogen Idec Inc | Homologe des nogo rezeptors |
| JP2005507246A (ja) | 2001-08-27 | 2005-03-17 | ノバルティス アクチエンゲゼルシャフト | Ｎｏｇｏレセプターホモログおよびそれらの使用 |
| JP2005519584A (ja) | 2001-10-22 | 2005-07-07 | ノバルティス アクチエンゲゼルシャフト | Ｎｏｇｏレセプターホモログおよびそれらの使用 |
| MXPA05001615A (es) | 2002-08-10 | 2005-08-19 | Biogen Idec Inc | Antagonistas del nogo receptor. |
-
2001
- 2001-10-06 DE DE60141409T patent/DE60141409D1/de not_active Expired - Lifetime
- 2001-10-06 ES ES01979595T patent/ES2341608T3/es not_active Expired - Lifetime
- 2001-10-06 AU AU2002211539A patent/AU2002211539B2/en not_active Ceased
- 2001-10-06 JP JP2002532629A patent/JP4465148B2/ja not_active Expired - Fee Related
- 2001-10-06 PT PT01979595T patent/PT1325130E/pt unknown
- 2001-10-06 DK DK01979595.4T patent/DK1325130T3/da active
- 2001-10-06 US US09/972,546 patent/US20030124704A1/en not_active Abandoned
- 2001-10-06 WO PCT/US2001/031488 patent/WO2002029059A2/en not_active Ceased
- 2001-10-06 AT AT01979595T patent/ATE458815T1/de active
- 2001-10-06 NZ NZ525422A patent/NZ525422A/en unknown
- 2001-10-06 EP EP01979595A patent/EP1325130B1/en not_active Expired - Lifetime
- 2001-10-06 CA CA002424834A patent/CA2424834A1/en not_active Abandoned
- 2001-10-06 AU AU1153902A patent/AU1153902A/xx active Pending
-
2003
- 2003-12-12 US US10/735,256 patent/US7173118B2/en not_active Expired - Lifetime
-
2006
- 2006-10-06 US US11/544,013 patent/US7456255B2/en not_active Expired - Lifetime
-
2008
- 2008-11-24 US US12/277,187 patent/US20090175850A1/en not_active Abandoned
-
2009
- 2009-02-02 JP JP2009022063A patent/JP2009100767A/ja not_active Withdrawn
-
2010
- 2010-11-23 US US12/952,747 patent/US20110129477A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| WO2002029059A2 (en) | 2002-04-11 |
| JP2009100767A (ja) | 2009-05-14 |
| EP1325130B1 (en) | 2010-02-24 |
| DK1325130T3 (da) | 2010-05-25 |
| US20050048520A1 (en) | 2005-03-03 |
| WO2002029059A3 (en) | 2003-01-23 |
| ATE458815T1 (de) | 2010-03-15 |
| AU1153902A (en) | 2002-04-15 |
| US20110129477A1 (en) | 2011-06-02 |
| US7173118B2 (en) | 2007-02-06 |
| WO2002029059A9 (en) | 2003-05-15 |
| US20030124704A1 (en) | 2003-07-03 |
| JP4465148B2 (ja) | 2010-05-19 |
| DE60141409D1 (de) | 2010-04-08 |
| AU2002211539B2 (en) | 2007-01-25 |
| JP2004528809A (ja) | 2004-09-24 |
| CA2424834A1 (en) | 2002-04-11 |
| US7456255B2 (en) | 2008-11-25 |
| EP1325130A2 (en) | 2003-07-09 |
| US20090175850A1 (en) | 2009-07-09 |
| NZ525422A (en) | 2006-09-29 |
| PT1325130E (pt) | 2010-05-31 |
| US20070104713A1 (en) | 2007-05-10 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2341608T3 (es) | Homologos del receptor de nogo. | |
| AU2002211539A1 (en) | Nogo receptor homologs | |
| ES2284214T3 (es) | Nuevas moleculas de la familia de las proteinas tango-77 y usos de las mismas. | |
| CA2431891A1 (en) | Mutations in neuronal gene sodium-channel alpha 1-subunit and their polypeptides and their treatment of generalised epilepsy with febrile seizures plus | |
| JP2005229804A (ja) | 新規なメラニンコンセントレーティングホルモン受容体 | |
| AU770018B2 (en) | Human N-type calcium channel isoform and uses thereof | |
| JP4447826B2 (ja) | 変異アンドロゲン受容体、それを発現する癌細胞、それらの作出方法およびそれらの用途 | |
| JPWO2003055507A1 (ja) | 拒食症又は生活習慣病治療薬及びそのスクリーニング方法 | |
| ES2319386T3 (es) | Proteina 2 del canal del calcio de tipo trp (tlcc-2) humana. | |
| JPWO2006068326A1 (ja) | 新規ポリペプチドおよびその用途 | |
| ES2311601T3 (es) | Receptores acoplado a proteina que se une a trifosfato de guanosina place 6002312 y su gen y produccion y uso del mismo. | |
| CA2446838A1 (en) | Novel mutation | |
| JPH1175866A (ja) | マウスＦｒｉｚｚｌｅｄ−６ 遺伝子に類似したヒト７ＴＭ受容体 | |
| JP4004767B2 (ja) | 新規ｇ蛋白質共役型レセプター蛋白質およびそのｄｎａ | |
| JP2010051322A (ja) | 新規タンパク質およびそのｄｎａ | |
| US20030166155A1 (en) | Isolated human transporter proteins, nucleic acid molecules encoding human transporter proteins, and uses thereof | |
| JP4535670B2 (ja) | 新規ポリペプチド、そのｄｎａおよびそれらの用途 | |
| JP4378415B2 (ja) | 変異アンドロゲン受容体、それを発現する癌細胞、それらの作出方法およびそれらの用途 | |
| JP2004073179A (ja) | 新規タンパク質、そのｄｎａおよび用途 | |
| WO2004084945A1 (ja) | 摂食調節剤 | |
| JP2002335976A (ja) | 新規生理活性ペプチドおよびその用途 | |
| JP2003000275A (ja) | 新規膜貫通型レセプター様タンパク質およびそのｄｎａ | |
| CA2454427A1 (en) | A novel g protein-coupled receptor, gave8 | |
| JP2004115394A (ja) | 免疫疾患予防・治療剤 | |
| JP2002355072A (ja) | 新規ｇタンパク質共役型レセプタータンパク質およびそのｄｎａ |