JP4383869B2 - 軸索成長のｎｏｇｏのレセプターを仲介とした妨害 - Google Patents
軸索成長のｎｏｇｏのレセプターを仲介とした妨害 Download PDFInfo
- Publication number
- JP4383869B2 JP4383869B2 JP2003534444A JP2003534444A JP4383869B2 JP 4383869 B2 JP4383869 B2 JP 4383869B2 JP 2003534444 A JP2003534444 A JP 2003534444A JP 2003534444 A JP2003534444 A JP 2003534444A JP 4383869 B2 JP4383869 B2 JP 4383869B2
- Authority
- JP
- Japan
- Prior art keywords
- polypeptide
- nogo
- seq
- amino acids
- amino acid
- 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 - Fee Related
Links
- 230000003376 axonal effect Effects 0.000 title claims description 50
- 102000005781 Nogo Receptor Human genes 0.000 title claims description 32
- 108020003872 Nogo receptor Proteins 0.000 title claims description 32
- 230000001404 mediated effect Effects 0.000 title claims description 27
- 230000012010 growth Effects 0.000 title description 36
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 255
- 210000004027 cell Anatomy 0.000 claims description 222
- 102100029826 Reticulon-4 receptor Human genes 0.000 claims description 183
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 158
- 101710093481 Reticulon-4 receptor Proteins 0.000 claims description 156
- 229920001184 polypeptide Polymers 0.000 claims description 136
- 150000001413 amino acids Chemical class 0.000 claims description 107
- 238000000034 method Methods 0.000 claims description 99
- 102000006386 Myelin Proteins Human genes 0.000 claims description 84
- 108010083674 Myelin Proteins Proteins 0.000 claims description 84
- 210000005012 myelin Anatomy 0.000 claims description 81
- 210000003169 central nervous system Anatomy 0.000 claims description 79
- 210000002569 neuron Anatomy 0.000 claims description 64
- 230000014509 gene expression Effects 0.000 claims description 58
- 150000007523 nucleic acids Chemical class 0.000 claims description 56
- 230000014511 neuron projection development Effects 0.000 claims description 55
- 102000039446 nucleic acids Human genes 0.000 claims description 52
- 108020004707 nucleic acids Proteins 0.000 claims description 52
- 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 49
- 230000002401 inhibitory effect Effects 0.000 claims description 49
- 102000002260 Alkaline Phosphatase Human genes 0.000 claims description 45
- 108020004774 Alkaline Phosphatase Proteins 0.000 claims description 45
- 230000005764 inhibitory process Effects 0.000 claims description 44
- 239000013598 vector Substances 0.000 claims description 41
- 210000003050 axon Anatomy 0.000 claims description 38
- 239000000203 mixture Substances 0.000 claims description 23
- 230000008929 regeneration Effects 0.000 claims description 23
- 238000011069 regeneration method Methods 0.000 claims description 23
- 208000027418 Wounds and injury Diseases 0.000 claims description 16
- 208000014674 injury Diseases 0.000 claims description 16
- 238000006467 substitution reaction Methods 0.000 claims description 15
- 208000016192 Demyelinating disease Diseases 0.000 claims description 12
- 206010052428 Wound Diseases 0.000 claims description 12
- 210000000278 spinal cord Anatomy 0.000 claims description 12
- 230000008733 trauma Effects 0.000 claims description 12
- 238000000338 in vitro Methods 0.000 claims description 11
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 10
- 241000124008 Mammalia Species 0.000 claims description 9
- 230000002490 cerebral effect Effects 0.000 claims description 9
- 239000002773 nucleotide Substances 0.000 claims description 8
- 125000003729 nucleotide group Chemical group 0.000 claims description 8
- 239000008194 pharmaceutical composition Substances 0.000 claims description 8
- 210000004885 white matter Anatomy 0.000 claims description 8
- 208000015114 central nervous system disease Diseases 0.000 claims description 7
- 201000010099 disease Diseases 0.000 claims description 7
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 7
- 238000000520 microinjection Methods 0.000 claims description 6
- 206010012305 Demyelination Diseases 0.000 claims description 3
- 230000005856 abnormality Effects 0.000 claims description 3
- 230000007850 degeneration Effects 0.000 claims description 3
- 208000035475 disorder Diseases 0.000 claims description 3
- 238000004090 dissolution Methods 0.000 claims description 3
- 238000007911 parenteral administration Methods 0.000 claims description 3
- 208000023516 stroke disease Diseases 0.000 claims description 3
- 208000011403 Alexander disease Diseases 0.000 claims description 2
- 206010003694 Atrophy Diseases 0.000 claims description 2
- 208000022526 Canavan disease Diseases 0.000 claims description 2
- 208000010055 Globoid Cell Leukodystrophy Diseases 0.000 claims description 2
- 208000028226 Krabbe disease Diseases 0.000 claims description 2
- 208000034800 Leukoencephalopathies Diseases 0.000 claims description 2
- 102100026784 Myelin proteolipid protein Human genes 0.000 claims description 2
- 206010056332 Panencephalitis Diseases 0.000 claims description 2
- 208000017493 Pelizaeus-Merzbacher disease Diseases 0.000 claims description 2
- 230000001919 adrenal effect Effects 0.000 claims description 2
- 230000037444 atrophy Effects 0.000 claims description 2
- 201000002491 encephalomyelitis Diseases 0.000 claims description 2
- 230000003458 metachromatic effect Effects 0.000 claims description 2
- 201000006417 multiple sclerosis Diseases 0.000 claims description 2
- 102000040430 polynucleotide Human genes 0.000 claims 27
- 108091033319 polynucleotide Proteins 0.000 claims 27
- 239000002157 polynucleotide Substances 0.000 claims 27
- 102000005720 Glutathione transferase Human genes 0.000 claims 4
- 108010070675 Glutathione transferase Proteins 0.000 claims 4
- 230000001737 promoting effect Effects 0.000 claims 4
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims 2
- 238000007918 intramuscular administration Methods 0.000 claims 1
- 238000007912 intraperitoneal administration Methods 0.000 claims 1
- 238000001990 intravenous administration Methods 0.000 claims 1
- 208000036546 leukodystrophy Diseases 0.000 claims 1
- 238000007920 subcutaneous administration Methods 0.000 claims 1
- 102000010410 Nogo Proteins Human genes 0.000 description 308
- 108010077641 Nogo Proteins Proteins 0.000 description 308
- 108090000623 proteins and genes Proteins 0.000 description 208
- 102000004169 proteins and genes Human genes 0.000 description 180
- 235000018102 proteins Nutrition 0.000 description 175
- 230000027455 binding Effects 0.000 description 106
- 210000000020 growth cone Anatomy 0.000 description 90
- 210000003594 spinal ganglia Anatomy 0.000 description 77
- 101000727479 Mus musculus Reticulon-4 receptor Proteins 0.000 description 65
- 235000001014 amino acid Nutrition 0.000 description 53
- 230000000694 effects Effects 0.000 description 51
- 125000003275 alpha amino acid group Chemical group 0.000 description 46
- 239000012634 fragment Substances 0.000 description 46
- 238000003556 assay Methods 0.000 description 42
- 210000004901 leucine-rich repeat Anatomy 0.000 description 36
- 108020001507 fusion proteins Proteins 0.000 description 35
- 102000037865 fusion proteins Human genes 0.000 description 35
- 108010006444 Leucine-Rich Repeat Proteins Proteins 0.000 description 30
- 108010041199 Nogo Receptor 1 Proteins 0.000 description 27
- 239000003795 chemical substances by application Substances 0.000 description 27
- 239000002299 complementary DNA Substances 0.000 description 27
- 108020004414 DNA Proteins 0.000 description 25
- 239000003636 conditioned culture medium Substances 0.000 description 24
- 102000005962 receptors Human genes 0.000 description 24
- 108020003175 receptors Proteins 0.000 description 24
- 238000002360 preparation method Methods 0.000 description 23
- 230000006870 function Effects 0.000 description 22
- 239000013612 plasmid Substances 0.000 description 22
- 238000012217 deletion Methods 0.000 description 20
- 230000037430 deletion Effects 0.000 description 20
- 239000003446 ligand Substances 0.000 description 20
- 210000004248 oligodendroglia Anatomy 0.000 description 20
- 239000000758 substrate Substances 0.000 description 20
- 241001465754 Metazoa Species 0.000 description 18
- 239000000816 peptidomimetic Substances 0.000 description 18
- 241000699666 Mus <mouse, genus> Species 0.000 description 17
- 125000000539 amino acid group Chemical group 0.000 description 17
- 238000004458 analytical method Methods 0.000 description 17
- 238000003752 polymerase chain reaction Methods 0.000 description 17
- 238000010186 staining Methods 0.000 description 17
- 239000005557 antagonist Substances 0.000 description 16
- 230000001939 inductive effect Effects 0.000 description 16
- 239000012528 membrane Substances 0.000 description 16
- 210000004379 membrane Anatomy 0.000 description 16
- 230000011664 signaling Effects 0.000 description 16
- 241000700605 Viruses Species 0.000 description 15
- 238000007792 addition Methods 0.000 description 15
- 230000028600 axonogenesis Effects 0.000 description 15
- 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 15
- 239000000284 extract Substances 0.000 description 15
- 239000002953 phosphate buffered saline Substances 0.000 description 15
- 210000001519 tissue Anatomy 0.000 description 15
- 241000287828 Gallus gallus Species 0.000 description 14
- 108700019146 Transgenes Proteins 0.000 description 14
- 239000000427 antigen Substances 0.000 description 14
- 108091007433 antigens Proteins 0.000 description 14
- 102000036639 antigens Human genes 0.000 description 14
- 210000004556 brain Anatomy 0.000 description 14
- 235000013330 chicken meat Nutrition 0.000 description 14
- 239000013604 expression vector Substances 0.000 description 14
- 238000003119 immunoblot Methods 0.000 description 14
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 14
- 238000012360 testing method Methods 0.000 description 14
- 241000699670 Mus sp. Species 0.000 description 13
- 230000009471 action Effects 0.000 description 13
- 210000004899 c-terminal region Anatomy 0.000 description 13
- 230000002950 deficient Effects 0.000 description 13
- 239000003112 inhibitor Substances 0.000 description 13
- 230000004044 response Effects 0.000 description 13
- 210000003994 retinal ganglion cell Anatomy 0.000 description 13
- 241000700159 Rattus Species 0.000 description 12
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 12
- 238000002474 experimental method Methods 0.000 description 12
- 230000001537 neural effect Effects 0.000 description 12
- 150000001875 compounds Chemical class 0.000 description 11
- 108020004999 messenger RNA Proteins 0.000 description 11
- 230000004048 modification Effects 0.000 description 11
- 238000012986 modification Methods 0.000 description 11
- 239000000523 sample Substances 0.000 description 11
- 230000009261 transgenic effect Effects 0.000 description 11
- 241000701161 unidentified adenovirus Species 0.000 description 11
- 108091026890 Coding region Proteins 0.000 description 10
- KPKZJLCSROULON-QKGLWVMZSA-N Phalloidin Chemical compound N1C(=O)[C@@H]([C@@H](O)C)NC(=O)[C@H](C)NC(=O)[C@H](C[C@@](C)(O)CO)NC(=O)[C@H](C2)NC(=O)[C@H](C)NC(=O)[C@@H]3C[C@H](O)CN3C(=O)[C@@H]1CSC1=C2C2=CC=CC=C2N1 KPKZJLCSROULON-QKGLWVMZSA-N 0.000 description 10
- 101150006932 RTN1 gene Proteins 0.000 description 10
- 239000003814 drug Substances 0.000 description 10
- 238000002965 ELISA Methods 0.000 description 9
- 102000004190 Enzymes Human genes 0.000 description 9
- 108090000790 Enzymes Proteins 0.000 description 9
- 239000000872 buffer Substances 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- 238000003018 immunoassay Methods 0.000 description 9
- 239000003550 marker Substances 0.000 description 9
- 210000002241 neurite Anatomy 0.000 description 9
- 108010076504 Protein Sorting Signals Proteins 0.000 description 8
- 229940079593 drug Drugs 0.000 description 8
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 8
- 230000002163 immunogen Effects 0.000 description 8
- 238000003780 insertion Methods 0.000 description 8
- 230000037431 insertion Effects 0.000 description 8
- 230000002829 reductive effect Effects 0.000 description 8
- 230000010076 replication Effects 0.000 description 8
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 8
- 239000000126 substance Substances 0.000 description 8
- 238000001890 transfection Methods 0.000 description 8
- 210000002950 fibroblast Anatomy 0.000 description 7
- 239000003966 growth inhibitor Substances 0.000 description 7
- 208000015181 infectious disease Diseases 0.000 description 7
- 238000000670 ligand binding assay Methods 0.000 description 7
- 150000002632 lipids Chemical class 0.000 description 7
- 238000004519 manufacturing process Methods 0.000 description 7
- 230000001177 retroviral effect Effects 0.000 description 7
- 108700038288 rhodamine-phalloidin Proteins 0.000 description 7
- 241001430294 unidentified retrovirus Species 0.000 description 7
- 241000283690 Bos taurus Species 0.000 description 6
- 241000588724 Escherichia coli Species 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 229910019142 PO4 Inorganic materials 0.000 description 6
- 102000006486 Phosphoinositide Phospholipase C Human genes 0.000 description 6
- 108010044302 Phosphoinositide phospholipase C Proteins 0.000 description 6
- 102000013008 Semaphorin-3A Human genes 0.000 description 6
- 108010090319 Semaphorin-3A Proteins 0.000 description 6
- 230000004071 biological effect Effects 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 6
- 210000000170 cell membrane Anatomy 0.000 description 6
- 230000001419 dependent effect Effects 0.000 description 6
- 238000009826 distribution Methods 0.000 description 6
- 210000001671 embryonic stem cell Anatomy 0.000 description 6
- 230000004927 fusion Effects 0.000 description 6
- 210000004602 germ cell Anatomy 0.000 description 6
- 230000009036 growth inhibition Effects 0.000 description 6
- 230000002209 hydrophobic effect Effects 0.000 description 6
- 230000003993 interaction Effects 0.000 description 6
- 229920000729 poly(L-lysine) polymer Polymers 0.000 description 6
- 239000000725 suspension Substances 0.000 description 6
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 5
- 108091034117 Oligonucleotide Proteins 0.000 description 5
- 208000037273 Pathologic Processes Diseases 0.000 description 5
- 108010009711 Phalloidine Proteins 0.000 description 5
- 230000002411 adverse Effects 0.000 description 5
- 238000013459 approach Methods 0.000 description 5
- 230000000903 blocking effect Effects 0.000 description 5
- 229940098773 bovine serum albumin Drugs 0.000 description 5
- 230000001413 cellular effect Effects 0.000 description 5
- 238000007398 colorimetric assay Methods 0.000 description 5
- 230000006378 damage Effects 0.000 description 5
- 238000009792 diffusion process Methods 0.000 description 5
- 239000003937 drug carrier Substances 0.000 description 5
- 238000010166 immunofluorescence Methods 0.000 description 5
- 238000001727 in vivo Methods 0.000 description 5
- 238000005259 measurement Methods 0.000 description 5
- 230000009054 pathological process Effects 0.000 description 5
- 210000001428 peripheral nervous system Anatomy 0.000 description 5
- 230000003389 potentiating effect Effects 0.000 description 5
- 238000000159 protein binding assay Methods 0.000 description 5
- 238000000746 purification Methods 0.000 description 5
- 230000001105 regulatory effect Effects 0.000 description 5
- 230000019491 signal transduction Effects 0.000 description 5
- 208000020431 spinal cord injury Diseases 0.000 description 5
- 230000001225 therapeutic effect Effects 0.000 description 5
- 230000009466 transformation Effects 0.000 description 5
- 239000013603 viral vector Substances 0.000 description 5
- CQTGBCFGAAYOCY-ZCRNMIQFSA-N (3S)-3-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-acetamido-3-methylbutanoyl]amino]-3-methylbutanoyl]amino]-3-phenylpropanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-5-amino-5-oxopentanoyl]amino]-4-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-3-methyl-1-oxobutan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-oxobutanoic acid Chemical compound CC(C)C[C@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@@H](NC(C)=O)C(C)C)C(C)C)[C@@H](C)O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](C(C)C)C(N)=O CQTGBCFGAAYOCY-ZCRNMIQFSA-N 0.000 description 4
- 101100189913 Caenorhabditis elegans pept-1 gene Proteins 0.000 description 4
- 102000009193 Caveolin Human genes 0.000 description 4
- 108050000084 Caveolin Proteins 0.000 description 4
- 102000053602 DNA Human genes 0.000 description 4
- 206010059866 Drug resistance Diseases 0.000 description 4
- 101000727477 Homo sapiens Reticulon-4 receptor Proteins 0.000 description 4
- 241000283973 Oryctolagus cuniculus Species 0.000 description 4
- 241001494479 Pecora Species 0.000 description 4
- 101150001322 RTN3 gene Proteins 0.000 description 4
- 108020004511 Recombinant DNA Proteins 0.000 description 4
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 4
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 4
- 102100029831 Reticulon-4 Human genes 0.000 description 4
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 4
- -1 cationic lipid Chemical class 0.000 description 4
- 239000013592 cell lysate Substances 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
- NBQNWMBBSKPBAY-UHFFFAOYSA-N iodixanol Chemical compound IC=1C(C(=O)NCC(O)CO)=C(I)C(C(=O)NCC(O)CO)=C(I)C=1N(C(=O)C)CC(O)CN(C(C)=O)C1=C(I)C(C(=O)NCC(O)CO)=C(I)C(C(=O)NCC(O)CO)=C1I NBQNWMBBSKPBAY-UHFFFAOYSA-N 0.000 description 4
- 239000010410 layer Substances 0.000 description 4
- 230000004807 localization Effects 0.000 description 4
- 239000011159 matrix material Substances 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 210000001328 optic nerve Anatomy 0.000 description 4
- 230000001575 pathological effect Effects 0.000 description 4
- 238000010647 peptide synthesis reaction Methods 0.000 description 4
- 239000004033 plastic Substances 0.000 description 4
- 229920003023 plastic Polymers 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- 102000007469 Actins Human genes 0.000 description 3
- 108010085238 Actins Proteins 0.000 description 3
- 102000014914 Carrier Proteins Human genes 0.000 description 3
- 241000282693 Cercopithecidae Species 0.000 description 3
- 239000012981 Hank's balanced salt solution Substances 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 101000727472 Homo sapiens Reticulon-4 Proteins 0.000 description 3
- 108010025020 Nerve Growth Factor Proteins 0.000 description 3
- 238000000636 Northern blotting Methods 0.000 description 3
- 108010088535 Pep-1 peptide Proteins 0.000 description 3
- 239000013614 RNA sample Substances 0.000 description 3
- 206010038997 Retroviral infections Diseases 0.000 description 3
- 101150063599 Rtn2 gene Proteins 0.000 description 3
- 101100221606 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) COS7 gene Proteins 0.000 description 3
- 208000006011 Stroke Diseases 0.000 description 3
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 3
- 230000000890 antigenic effect Effects 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 108010005774 beta-Galactosidase Proteins 0.000 description 3
- 230000008827 biological function Effects 0.000 description 3
- 230000031018 biological processes and functions Effects 0.000 description 3
- 210000002459 blastocyst Anatomy 0.000 description 3
- 210000001109 blastomere Anatomy 0.000 description 3
- 230000037396 body weight Effects 0.000 description 3
- 239000004202 carbamide Substances 0.000 description 3
- 238000004113 cell culture Methods 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 239000011248 coating agent Substances 0.000 description 3
- 238000000576 coating method Methods 0.000 description 3
- 230000002860 competitive effect Effects 0.000 description 3
- 238000012258 culturing Methods 0.000 description 3
- 210000005220 cytoplasmic tail Anatomy 0.000 description 3
- 210000001787 dendrite Anatomy 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 210000002257 embryonic structure Anatomy 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 108700004026 gag Genes Proteins 0.000 description 3
- 239000008187 granular material Substances 0.000 description 3
- 238000013537 high throughput screening Methods 0.000 description 3
- 238000002744 homologous recombination Methods 0.000 description 3
- 230000006801 homologous recombination Effects 0.000 description 3
- 102000048720 human RTN4R Human genes 0.000 description 3
- 238000009396 hybridization Methods 0.000 description 3
- 238000002649 immunization Methods 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 210000003292 kidney cell Anatomy 0.000 description 3
- 238000002372 labelling Methods 0.000 description 3
- 210000001161 mammalian embryo Anatomy 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 210000005036 nerve Anatomy 0.000 description 3
- 238000004806 packaging method and process Methods 0.000 description 3
- 230000000144 pharmacologic effect Effects 0.000 description 3
- 238000007747 plating Methods 0.000 description 3
- 238000003127 radioimmunoassay Methods 0.000 description 3
- 239000011347 resin Substances 0.000 description 3
- 229920005989 resin Polymers 0.000 description 3
- 210000001525 retina Anatomy 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 238000002741 site-directed mutagenesis Methods 0.000 description 3
- 239000007790 solid phase Substances 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 239000004094 surface-active agent Substances 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 238000007910 systemic administration Methods 0.000 description 3
- 230000003612 virological effect Effects 0.000 description 3
- 238000001086 yeast two-hybrid system Methods 0.000 description 3
- 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 2
- 101710139410 1-phosphatidylinositol phosphodiesterase Proteins 0.000 description 2
- KUWPCJHYPSUOFW-YBXAARCKSA-N 2-nitrophenyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CC=CC=C1[N+]([O-])=O KUWPCJHYPSUOFW-YBXAARCKSA-N 0.000 description 2
- XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 2
- QRXMUCSWCMTJGU-UHFFFAOYSA-N 5-bromo-4-chloro-3-indolyl phosphate Chemical compound C1=C(Br)C(Cl)=C2C(OP(O)(=O)O)=CNC2=C1 QRXMUCSWCMTJGU-UHFFFAOYSA-N 0.000 description 2
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- 101100455506 Arabidopsis thaliana LRR2 gene Proteins 0.000 description 2
- 206010003445 Ascites Diseases 0.000 description 2
- 102100026189 Beta-galactosidase Human genes 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- 102000004127 Cytokines Human genes 0.000 description 2
- 108090000695 Cytokines Proteins 0.000 description 2
- 241000702421 Dependoparvovirus Species 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- 102000002702 GPI-Linked Proteins Human genes 0.000 description 2
- 108010043685 GPI-Linked Proteins Proteins 0.000 description 2
- 241001135569 Human adenovirus 5 Species 0.000 description 2
- 206010061216 Infarction Diseases 0.000 description 2
- 102000004289 Interferon regulatory factor 1 Human genes 0.000 description 2
- 108090000890 Interferon regulatory factor 1 Proteins 0.000 description 2
- 102000018697 Membrane Proteins Human genes 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 208000028389 Nerve injury Diseases 0.000 description 2
- 208000012902 Nervous system disease Diseases 0.000 description 2
- PXHVJJICTQNCMI-UHFFFAOYSA-N Nickel Chemical compound [Ni] PXHVJJICTQNCMI-UHFFFAOYSA-N 0.000 description 2
- 229930040373 Paraformaldehyde Natural products 0.000 description 2
- 102100037097 Protein disulfide-isomerase A3 Human genes 0.000 description 2
- 101710122684 Reticulon-1 Proteins 0.000 description 2
- 241000714474 Rous sarcoma virus Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 241000713896 Spleen necrosis virus Species 0.000 description 2
- 229930006000 Sucrose Natural products 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
- 102000007238 Transferrin Receptors Human genes 0.000 description 2
- 108010033576 Transferrin Receptors Proteins 0.000 description 2
- 239000013504 Triton X-100 Substances 0.000 description 2
- 229920004890 Triton X-100 Polymers 0.000 description 2
- 208000036142 Viral infection Diseases 0.000 description 2
- 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 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 230000001464 adherent effect Effects 0.000 description 2
- 230000003042 antagnostic effect Effects 0.000 description 2
- 229940121363 anti-inflammatory agent Drugs 0.000 description 2
- 239000002260 anti-inflammatory agent Substances 0.000 description 2
- 230000000692 anti-sense effect Effects 0.000 description 2
- 239000003146 anticoagulant agent Substances 0.000 description 2
- 230000004009 axon guidance Effects 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 239000011230 binding agent Substances 0.000 description 2
- 108091008324 binding proteins Proteins 0.000 description 2
- 210000005056 cell body Anatomy 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 238000001516 cell proliferation assay Methods 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 108700010039 chimeric receptor Proteins 0.000 description 2
- 210000000349 chromosome Anatomy 0.000 description 2
- 238000012761 co-transfection Methods 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
- 210000000805 cytoplasm Anatomy 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 230000003412 degenerative effect Effects 0.000 description 2
- 230000004069 differentiation Effects 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 108700004025 env Genes Proteins 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 108060002566 ephrin Proteins 0.000 description 2
- 102000012803 ephrin Human genes 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 210000002592 gangliocyte Anatomy 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 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 2
- 230000036541 health Effects 0.000 description 2
- 238000012203 high throughput assay Methods 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 238000010820 immunofluorescence microscopy Methods 0.000 description 2
- 238000007901 in situ hybridization Methods 0.000 description 2
- 230000007574 infarction Effects 0.000 description 2
- 230000002452 interceptive effect Effects 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 230000033001 locomotion Effects 0.000 description 2
- 229920002521 macromolecule Polymers 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000010534 mechanism of action Effects 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 230000004001 molecular interaction Effects 0.000 description 2
- 238000000302 molecular modelling Methods 0.000 description 2
- 210000003007 myelin sheath Anatomy 0.000 description 2
- 230000008764 nerve damage Effects 0.000 description 2
- 208000015122 neurodegenerative disease Diseases 0.000 description 2
- 238000006386 neutralization reaction Methods 0.000 description 2
- 229920002866 paraformaldehyde Polymers 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 238000002823 phage display Methods 0.000 description 2
- 239000013600 plasmid vector Substances 0.000 description 2
- 108700004029 pol Genes Proteins 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 230000026447 protein localization Effects 0.000 description 2
- 230000004850 protein–protein interaction Effects 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 210000001116 retinal neuron Anatomy 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 210000004116 schwann cell Anatomy 0.000 description 2
- 210000003497 sciatic nerve Anatomy 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 150000003384 small molecules Chemical class 0.000 description 2
- RDZTWEVXRGYCFV-UHFFFAOYSA-M sodium 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonate Chemical compound [Na+].OCCN1CCN(CCS([O-])(=O)=O)CC1 RDZTWEVXRGYCFV-UHFFFAOYSA-M 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 230000007480 spreading Effects 0.000 description 2
- 238000003892 spreading Methods 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 230000004960 subcellular localization Effects 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 230000002463 transducing effect Effects 0.000 description 2
- 238000010361 transduction Methods 0.000 description 2
- 230000026683 transduction Effects 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 230000009385 viral infection Effects 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- 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
- 208000024827 Alzheimer disease Diseases 0.000 description 1
- 108020005544 Antisense RNA Proteins 0.000 description 1
- BSYNRYMUTXBXSQ-UHFFFAOYSA-N Aspirin Chemical compound CC(=O)OC1=CC=CC=C1C(O)=O BSYNRYMUTXBXSQ-UHFFFAOYSA-N 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000282465 Canis Species 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 102000016289 Cell Adhesion Molecules Human genes 0.000 description 1
- 108010067225 Cell Adhesion Molecules Proteins 0.000 description 1
- 102000000844 Cell Surface Receptors Human genes 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 102000005598 Chondroitin Sulfate Proteoglycans Human genes 0.000 description 1
- 108010059480 Chondroitin Sulfate Proteoglycans Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- 238000000116 DAPI staining Methods 0.000 description 1
- 241000450599 DNA viruses Species 0.000 description 1
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
- 229920002307 Dextran Polymers 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
- LVGKNOAMLMIIKO-UHFFFAOYSA-N Elaidinsaeure-aethylester Natural products CCCCCCCCC=CCCCCCCCC(=O)OCC LVGKNOAMLMIIKO-UHFFFAOYSA-N 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 108091029865 Exogenous DNA Proteins 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 108091006020 Fc-tagged proteins Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 102000034615 Glial cell line-derived neurotrophic factor Human genes 0.000 description 1
- 108091010837 Glial cell line-derived neurotrophic factor Proteins 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101001038321 Homo sapiens Leucine-rich repeat protein 1 Proteins 0.000 description 1
- 241000701109 Human adenovirus 2 Species 0.000 description 1
- XQFRJNBWHJMXHO-RRKCRQDMSA-N IDUR Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C(I)=C1 XQFRJNBWHJMXHO-RRKCRQDMSA-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
- 108010058683 Immobilized Proteins Proteins 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- 108010025815 Kanamycin Kinase Proteins 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- 108091026898 Leader sequence (mRNA) Proteins 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 101710201625 Leucine-rich protein Proteins 0.000 description 1
- 102100040249 Leucine-rich repeat protein 1 Human genes 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 241000713862 Moloney murine sarcoma virus Species 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 108010021466 Mutant Proteins Proteins 0.000 description 1
- 102000008300 Mutant Proteins Human genes 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 102000007072 Nerve Growth Factors Human genes 0.000 description 1
- 102000008763 Neurofilament Proteins Human genes 0.000 description 1
- 108010088373 Neurofilament Proteins Proteins 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 1
- XDMCWZFLLGVIID-SXPRBRBTSA-N O-(3-O-D-galactosyl-N-acetyl-beta-D-galactosaminyl)-L-serine Chemical compound CC(=O)N[C@H]1[C@H](OC[C@H]([NH3+])C([O-])=O)O[C@H](CO)[C@H](O)[C@@H]1OC1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 XDMCWZFLLGVIID-SXPRBRBTSA-N 0.000 description 1
- 108700020796 Oncogene Proteins 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 101710132701 Protein L1 Proteins 0.000 description 1
- 101150117544 Rtn4 gene Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 101000702917 Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) CDP-abequose synthase Proteins 0.000 description 1
- 206010039491 Sarcoma Diseases 0.000 description 1
- 102000014105 Semaphorin Human genes 0.000 description 1
- 108050003978 Semaphorin Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 108010023197 Streptokinase Proteins 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 1
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 description 1
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
- 230000007488 abnormal function Effects 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- DPXJVFZANSGRMM-UHFFFAOYSA-N acetic acid;2,3,4,5,6-pentahydroxyhexanal;sodium Chemical compound [Na].CC(O)=O.OCC(O)C(O)C(O)C(O)C=O DPXJVFZANSGRMM-UHFFFAOYSA-N 0.000 description 1
- 229960001138 acetylsalicylic acid Drugs 0.000 description 1
- NIXOWILDQLNWCW-UHFFFAOYSA-N acrylic acid group Chemical group C(C=C)(=O)O NIXOWILDQLNWCW-UHFFFAOYSA-N 0.000 description 1
- 230000036982 action potential Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 210000001789 adipocyte Anatomy 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000007818 agglutination assay Methods 0.000 description 1
- 239000000556 agonist Substances 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
- 230000004075 alteration Effects 0.000 description 1
- 125000003368 amide group Chemical group 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- 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 1
- 238000000137 annealing Methods 0.000 description 1
- 230000009830 antibody antigen interaction Effects 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 229940127219 anticoagulant drug Drugs 0.000 description 1
- 229960004676 antithrombotic agent Drugs 0.000 description 1
- 230000001640 apoptogenic effect Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 238000010420 art technique Methods 0.000 description 1
- 238000013528 artificial neural network Methods 0.000 description 1
- 238000002820 assay format Methods 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000008238 biochemical pathway Effects 0.000 description 1
- 239000013060 biological fluid Substances 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 210000004952 blastocoel Anatomy 0.000 description 1
- 230000036772 blood pressure Effects 0.000 description 1
- 108010006025 bovine growth hormone Proteins 0.000 description 1
- 235000010633 broth Nutrition 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 150000001718 carbodiimides Chemical class 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 230000021164 cell adhesion Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000013043 chemical agent Substances 0.000 description 1
- 238000001311 chemical methods and process Methods 0.000 description 1
- 210000003837 chick embryo Anatomy 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000011278 co-treatment Methods 0.000 description 1
- 238000012875 competitive assay Methods 0.000 description 1
- 230000009137 competitive binding Effects 0.000 description 1
- 239000003184 complementary RNA Substances 0.000 description 1
- 238000005094 computer simulation Methods 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 238000013270 controlled release Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 210000000172 cytosol Anatomy 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 230000009025 developmental regulation Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 239000000032 diagnostic agent Substances 0.000 description 1
- 229940039227 diagnostic agent Drugs 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- 239000007884 disintegrant Substances 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 238000011978 dissolution method Methods 0.000 description 1
- 230000003291 dopaminomimetic effect Effects 0.000 description 1
- 238000009510 drug design Methods 0.000 description 1
- 230000004064 dysfunction Effects 0.000 description 1
- 230000005684 electric field Effects 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- LVGKNOAMLMIIKO-QXMHVHEDSA-N ethyl oleate Chemical compound CCCCCCCC\C=C/CCCCCCCC(=O)OCC LVGKNOAMLMIIKO-QXMHVHEDSA-N 0.000 description 1
- 229940093471 ethyl oleate Drugs 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 210000001723 extracellular space Anatomy 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000010685 fatty oil Substances 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 210000003754 fetus Anatomy 0.000 description 1
- 238000001917 fluorescence detection Methods 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 101150098622 gag gene Proteins 0.000 description 1
- 239000007903 gelatin capsule Substances 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 208000005017 glioblastoma Diseases 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 210000000569 greater omentum Anatomy 0.000 description 1
- 210000004884 grey matter Anatomy 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 230000009931 harmful effect Effects 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 230000001744 histochemical effect Effects 0.000 description 1
- 102000049797 human RTN4 Human genes 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 239000012133 immunoprecipitate Substances 0.000 description 1
- 238000012744 immunostaining Methods 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 210000003000 inclusion body Anatomy 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000031146 intracellular signal transduction Effects 0.000 description 1
- FZWBNHMXJMCXLU-BLAUPYHCSA-N isomaltotriose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@@H](OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C=O)O1 FZWBNHMXJMCXLU-BLAUPYHCSA-N 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 239000004816 latex Substances 0.000 description 1
- 229920000126 latex Polymers 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- 238000005339 levitation Methods 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000011859 microparticle Substances 0.000 description 1
- 210000004939 midgestation embryo Anatomy 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- NKAAEMMYHLFEFN-UHFFFAOYSA-M monosodium tartrate Chemical compound [Na+].OC(=O)C(O)C(O)C([O-])=O NKAAEMMYHLFEFN-UHFFFAOYSA-M 0.000 description 1
- 230000000877 morphologic effect Effects 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 239000003471 mutagenic agent Substances 0.000 description 1
- 231100000707 mutagenic chemical Toxicity 0.000 description 1
- 230000023105 myelination Effects 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 238000007857 nested PCR Methods 0.000 description 1
- 230000007372 neural signaling Effects 0.000 description 1
- 230000004770 neurodegeneration Effects 0.000 description 1
- 210000004412 neuroendocrine cell Anatomy 0.000 description 1
- 210000005044 neurofilament Anatomy 0.000 description 1
- 210000004498 neuroglial cell Anatomy 0.000 description 1
- 239000002858 neurotransmitter agent Substances 0.000 description 1
- 101150089520 ngr gene Proteins 0.000 description 1
- 229910052759 nickel Inorganic materials 0.000 description 1
- JPXMTWWFLBLUCD-UHFFFAOYSA-N nitro blue tetrazolium(2+) Chemical compound COC1=CC(C=2C=C(OC)C(=CC=2)[N+]=2N(N=C(N=2)C=2C=CC=CC=2)C=2C=CC(=CC=2)[N+]([O-])=O)=CC=C1[N+]1=NC(C=2C=CC=CC=2)=NN1C1=CC=C([N+]([O-])=O)C=C1 JPXMTWWFLBLUCD-UHFFFAOYSA-N 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 239000002853 nucleic acid probe Substances 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 210000005112 optic tract Anatomy 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 210000000578 peripheral nerve Anatomy 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 108010017843 platelet-derived growth factor A Proteins 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920002704 polyhistidine Polymers 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000009465 prokaryotic expression Effects 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 230000004952 protein activity Effects 0.000 description 1
- 230000004853 protein function Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 210000002804 pyramidal tract Anatomy 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 150000003254 radicals Chemical class 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000001172 regenerating effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 108010073863 saruplase Proteins 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 238000013391 scatchard analysis Methods 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000008159 sesame oil Substances 0.000 description 1
- 235000011803 sesame oil Nutrition 0.000 description 1
- 238000010008 shearing Methods 0.000 description 1
- 230000007781 signaling event Effects 0.000 description 1
- 239000002356 single layer Substances 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 235000019812 sodium carboxymethyl cellulose Nutrition 0.000 description 1
- 229920001027 sodium carboxymethylcellulose Polymers 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 229960005202 streptokinase Drugs 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 230000000946 synaptic effect Effects 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 238000012353 t test Methods 0.000 description 1
- 239000003826 tablet Substances 0.000 description 1
- 239000012085 test solution Substances 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 229960000187 tissue plasminogen activator Drugs 0.000 description 1
- 238000011200 topical administration Methods 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000011426 transformation method Methods 0.000 description 1
- 238000012256 transgenic experiment Methods 0.000 description 1
- 238000011830 transgenic mouse model Methods 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- 230000007306 turnover Effects 0.000 description 1
- 238000010396 two-hybrid screening Methods 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 229960005356 urokinase Drugs 0.000 description 1
- 210000004291 uterus Anatomy 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 210000002845 virion Anatomy 0.000 description 1
- 150000003722 vitamin derivatives Chemical class 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000012130 whole-cell lysate Substances 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
- 210000004340 zona pellucida Anatomy 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/286—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against neuromediator receptors, e.g. serotonin receptor, dopamine receptor
-
- 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
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/02—Drugs for disorders of the nervous system for peripheral neuropathies
-
- 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
- A61P25/04—Centrally acting analgesics, e.g. opioids
-
- 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
- A61P25/06—Antimigraine agents
-
- 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
- A61P25/14—Drugs for disorders of the nervous system for treating abnormal movements, e.g. chorea, dyskinesia
-
- 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
- A61P25/28—Drugs for disorders of the nervous system for treating neurodegenerative disorders of the central nervous system, e.g. nootropic agents, cognition enhancers, drugs for treating Alzheimer's disease or other forms of dementia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- 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
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- 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
-
- 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
- C07K14/70571—Receptors; Cell surface antigens; Cell surface determinants for neuromediators, e.g. serotonin receptor, dopamine receptor
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- 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
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
- A01K2217/05—Animals comprising random inserted nucleic acids (transgenic)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Neurology (AREA)
- Animal Behavior & Ethology (AREA)
- General Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Neurosurgery (AREA)
- Cell Biology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Pain & Pain Management (AREA)
- Food Science & Technology (AREA)
- General Physics & Mathematics (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Pathology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Rheumatology (AREA)
- Heart & Thoracic Surgery (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US09/972,599 US7119165B2 (en) | 2000-01-12 | 2001-10-06 | Nogo receptor-mediated blockade of axonal growth |
| PCT/US2002/032007 WO2003031462A2 (en) | 2001-10-06 | 2002-10-04 | Nogo receptor-mediated blockade of axonal growth |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2005508165A JP2005508165A (ja) | 2005-03-31 |
| JP2005508165A5 JP2005508165A5 (OSRAM) | 2006-01-05 |
| JP4383869B2 true JP4383869B2 (ja) | 2009-12-16 |
Family
ID=25519870
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2003534444A Expired - Fee Related JP4383869B2 (ja) | 2001-10-06 | 2002-10-04 | 軸索成長のｎｏｇｏのレセプターを仲介とした妨害 |
Country Status (6)
| Country | Link |
|---|---|
| US (6) | US7119165B2 (OSRAM) |
| EP (1) | EP1451337A4 (OSRAM) |
| JP (1) | JP4383869B2 (OSRAM) |
| AU (1) | AU2002334889B2 (OSRAM) |
| CA (1) | CA2461655A1 (OSRAM) |
| WO (1) | WO2003031462A2 (OSRAM) |
Families Citing this family (44)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2000005364A1 (en) * | 1998-07-22 | 2000-02-03 | Smithkline Beecham Plc | Protein similar to neuroendrocrine-specific protein, and encoding cdna |
| US7119165B2 (en) * | 2000-01-12 | 2006-10-10 | Yale University | Nogo receptor-mediated blockade of axonal growth |
| AU2002211539B2 (en) * | 2000-10-06 | 2007-01-25 | Biogen Idec Ma Inc. | Nogo receptor homologs |
| US7309485B2 (en) * | 2001-12-03 | 2007-12-18 | Children's Medical Center Corporation | Reducing myelin-mediated inhibition of axon regeneration |
| US7745151B2 (en) * | 2002-08-02 | 2010-06-29 | Children's Medical Center Corporation | Methods of determining binding between Nogo receptor and p75 neurotrophin receptor |
| WO2004014311A2 (en) * | 2002-08-10 | 2004-02-19 | Yale University | Nogo receptor antagonists |
| AU2003288434B2 (en) * | 2002-12-06 | 2011-03-17 | IRP Health Pty Ltd | Peptides, antibodies thereto, and their use in the treatment of central nervous system damage |
| US7842666B2 (en) * | 2002-12-20 | 2010-11-30 | Research Foundation Of City University Of New York | Inhibitors of myelin-associated glycoprotein (MAG) activity for regulating neural growth and regeneration |
| EP2902491A1 (en) | 2003-03-19 | 2015-08-05 | Biogen MA Inc. | NOGO receptor binding protein |
| AU2004227392A1 (en) * | 2003-04-04 | 2004-10-21 | University Of Rochester | Identification of novel nogo-receptors and methods related thereto |
| RS20050774A (sr) * | 2003-04-16 | 2007-12-31 | Biogen Idec Ma Inc., | Antagonisti nogo receptora za tretman stanja sa amiloidnim plakovima |
| EP1633315A4 (en) * | 2003-05-15 | 2010-09-08 | Univ Leland Stanford Junior | Novel immunomodulating peptide |
| EA008253B1 (ru) * | 2003-08-07 | 2007-04-27 | Байоджен Айдек Ма Инк. | Антагонисты nogo-рецептора |
| 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 |
| CN1946418A (zh) * | 2004-01-30 | 2007-04-11 | 比奥根艾迪克Ma公司 | 利用nogo受体拮抗剂治疗涉及多巴胺能神经元退变的疾病 |
| NZ550772A (en) * | 2004-05-21 | 2009-10-30 | Uab Research Foundation | Variable lymphocyte receptors, related polypeptides and nucleic acids, and uses thereof |
| DK1776136T3 (da) * | 2004-06-24 | 2012-12-03 | Biogen Idec Inc | Behandling af tilstande, der involverer demyelinisering |
| US7846438B2 (en) | 2004-08-03 | 2010-12-07 | Biogen Idec Ma Inc. | Methods of promoting neurite outgrowth with soluble TAJ polypeptides |
| WO2006047049A2 (en) * | 2004-10-01 | 2006-05-04 | Yale University | Nogo-a polypeptide fragments, variant nogo receptor-1 polypeptides, and uses thereof |
| US20090010873A1 (en) * | 2004-11-29 | 2009-01-08 | Yeda Research And Development Co. Ltd. | Methods of Cell Therapy, Neurogenesis and Oligodendrogenesis |
| US7893032B2 (en) * | 2005-07-07 | 2011-02-22 | Yale University | NgR variants and compositions thereof for suppressing axonal growth inhibition |
| BRPI0613387A2 (pt) | 2005-07-08 | 2011-01-11 | Biogen Idec Inc | anticorpo isolado ou fragmento de ligação de antìgeno deste e o seu uso, polinucleotìdeo isolado, composição, vetor, célula hospedeira, anticorpo anti-sp35 e método para a produção do mesmo, polipeptìdeo isolado, método in vitro para redução da inibição do crescimento axonal e método in vitro para inibição do crescimento do colapso do cone |
| WO2007014382A1 (en) * | 2005-07-28 | 2007-02-01 | Wyeth | Compositions and methods of mutant nogo-66 domain proteins |
| US7951384B2 (en) * | 2005-08-05 | 2011-05-31 | University Of Massachusetts | Virus-like particles as vaccines for paramyxovirus |
| US9216212B2 (en) | 2005-08-05 | 2015-12-22 | University Of Massachusetts | Virus-like particles as vaccines for paramyxovirus |
| JP2009505665A (ja) * | 2005-08-25 | 2009-02-12 | 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 | Ｎｏｇｏ受容体ポリペプチドおよびポリペプチドフラグメント、ならびにそれらの使用 |
| WO2007039256A2 (de) * | 2005-09-30 | 2007-04-12 | Abbott Gmbh & Co. Kg | Bindungsdomänen von proteinen der repulsive guidance molecule (rgm) proteinfamilie und funktionale fragmente davon sowie deren verwendung |
| JP5829373B2 (ja) | 2006-01-27 | 2015-12-09 | バイオジェン・エムエイ・インコーポレイテッドＢｉｏｇｅｎ ＭＡ Ｉｎｃ． | Ｎｏｇｏレセプターアンタゴニスト |
| JP2009538282A (ja) * | 2006-05-15 | 2009-11-05 | 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 | 乏突起膠細胞の生存を促進させるためのＮｏｇｏ受容体−１（ＮｇＲ１）アンタゴニストの使用 |
| EP2046828A2 (en) * | 2006-07-07 | 2009-04-15 | Wyeth | Nogo receptor functional motifs, peptide mimetics, and mutated functional motifs related thereto, and methods of using the same |
| EP2068866A4 (en) | 2006-07-24 | 2010-04-07 | Biogen Idec Inc | METHODS FOR PROMOTING MYELINIZATION, NEURONAL SURVIVAL AND DIFFERENTIATION OF OLIGODENDROCYTES BY ADMINISTERING SP35 OR TRKA ANTAGONISTS |
| EP2081429A4 (en) * | 2006-08-31 | 2010-01-06 | Biogen Idec Inc | PROCESS FOR PERIPHERAL ADMINISTRATION OF NOGO RECEPTOR POLYPEPTIDES |
| CA2701189C (en) * | 2007-10-11 | 2017-05-16 | Biogen Idec Ma Inc. | Methods for treating pressure induced optic neuropathy, preventing neuronal degeneration and promoting neuronal cell survival via administration of lingo-1 antagonists and trkb agonists |
| AU2008325107B2 (en) * | 2007-11-08 | 2015-04-23 | Biogen Ma Inc. | Use of LINGO-4 antagonists in the treatment of conditions involving demyelination |
| AU2008331854A1 (en) * | 2007-11-28 | 2009-06-11 | Yale University | Nogo receptor binding small molecules to promote axonal growth |
| US8962803B2 (en) | 2008-02-29 | 2015-02-24 | AbbVie Deutschland GmbH & Co. KG | Antibodies against the RGM A protein and uses thereof |
| WO2009114197A2 (en) * | 2008-03-13 | 2009-09-17 | Yale University | Reactivation of axon growth and recovery in chronic spinal cord injury |
| US8058406B2 (en) | 2008-07-09 | 2011-11-15 | Biogen Idec Ma Inc. | Composition comprising antibodies to LINGO or fragments thereof |
| WO2010039224A2 (en) | 2008-09-30 | 2010-04-08 | University Of Massachusetts Medical School | Respiratory syncytial virus (rsv) sequences for protein expression and vaccines |
| CA2780069C (en) | 2009-12-08 | 2018-07-17 | Abbott Gmbh & Co. Kg | Monoclonal antibodies against the rgm a protein for use in the treatment of retinal nerve fiber layer degeneration |
| MX391536B (es) | 2012-01-27 | 2025-03-21 | Abbvie Deutschland | Composicion y metodo para el diagnostico y tratamiento de enfermedades asociadas con la degeneracion de neuritas. |
| 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 |
| HK1246810A1 (zh) | 2015-01-08 | 2018-09-14 | Biogen Ma Inc. | Lingo-1对抗药及用於治疗脱髓鞘疾病的用途 |
Family Cites Families (35)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ATE124726T1 (de) | 1988-11-04 | 1995-07-15 | Zuerich Erziehungsdirektion | Wachstumsregelfaktoren für neuriten. |
| US5250414A (en) | 1988-11-04 | 1993-10-05 | Erziehungsdirektion Of The Canton Zurich | Diagnostic methods using neurite growth regulatory factors |
| CA1341050C (en) | 1988-11-04 | 2000-07-11 | Martin E. Schwab | Neurite growth regulatory factors |
| 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 |
| US7368531B2 (en) * | 1997-03-07 | 2008-05-06 | Human Genome Sciences, Inc. | Human secreted proteins |
| WO2000070050A1 (en) | 1999-05-14 | 2000-11-23 | Genentech, Inc. | Compositions and methods for the treatment of immune related diseases |
| PT1490386E (pt) | 1998-03-10 | 2008-11-24 | Genentech Inc | Novos polipéptidos e ácidos nucleicos que os codificam |
| US6962797B2 (en) * | 1998-04-15 | 2005-11-08 | Genentech, Inc. | Nucleic acids encoding PRO615 |
| AU4682999A (en) | 1998-06-16 | 2000-01-05 | Human Genome Sciences, Inc. | 94 human secreted proteins |
| WO2000005364A1 (en) | 1998-07-22 | 2000-02-03 | Smithkline Beecham Plc | Protein similar to neuroendrocrine-specific protein, and encoding cdna |
| ES2529196T3 (es) | 1998-11-06 | 2015-02-17 | University Of Zurich | Secuencias de nucleótidos y proteínas de genes Nogo y métodos basados en estas |
| US6152155A (en) | 1998-11-30 | 2000-11-28 | Milligan; Lon | Filter cleaning device |
| CA2347835A1 (en) | 1998-12-01 | 2000-06-08 | Genentech, Inc. | Promotion or inhibition of angiogenesis and cardiovascularization |
| AU768230B2 (en) | 1998-12-22 | 2003-12-04 | Genentech Inc. | Methods and compositions for inhibiting neoplastic cell growth |
| US7041474B2 (en) | 1998-12-30 | 2006-05-09 | Millennium Pharmaceuticals, Inc. | Nucleic acid encoding human tango 509 |
| AU2883600A (en) | 1999-03-08 | 2000-09-28 | Genentech Inc. | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
| JP2004516227A (ja) | 1999-03-08 | 2004-06-03 | ジェネンテック・インコーポレーテッド | 免疫関連疾患を治療するための組成物と方法 |
| CA2383592A1 (en) | 1999-03-31 | 2000-10-05 | Curagen Corporation | 2384891 acids including open reading frames encoding polypeptides; orfx |
| WO2001009162A2 (en) | 1999-07-30 | 2001-02-08 | Millennium Pharmaceuticals, Inc. | Secreted proteins and uses thereof |
| US7119165B2 (en) | 2000-01-12 | 2006-10-10 | Yale University | Nogo receptor-mediated blockade of axonal growth |
| EP1248803B1 (en) | 2000-01-12 | 2010-05-05 | Yale University | Nogo receptor-mediated blockade of axonal growth |
| AU2002211539B2 (en) | 2000-10-06 | 2007-01-25 | Biogen Idec Ma Inc. | Nogo receptor homologs |
| WO2003018631A2 (en) | 2001-08-27 | 2003-03-06 | Novartis Ag | Nogo receptor homologues and their use |
| WO2003035687A1 (en) | 2001-10-22 | 2003-05-01 | Novartis Ag | Nogo receptor homologues and their use |
| US20030113325A1 (en) * | 2001-12-03 | 2003-06-19 | Zhigang He | Reducing myelin-mediated inhibition of axon regeneration |
| US7309485B2 (en) * | 2001-12-03 | 2007-12-18 | Children's Medical Center Corporation | Reducing myelin-mediated inhibition of axon regeneration |
| EP1354892A1 (en) | 2002-04-19 | 2003-10-22 | Centre National De La Recherche Scientifique (Cnrs) | Peptides capable of inducing attraction of the axonal growth and their use for treating neurodegenerative diseases |
| US7745151B2 (en) * | 2002-08-02 | 2010-06-29 | Children's Medical Center Corporation | Methods of determining binding between Nogo receptor and p75 neurotrophin receptor |
| WO2004014311A2 (en) | 2002-08-10 | 2004-02-19 | Yale University | Nogo receptor antagonists |
| RS20050774A (sr) * | 2003-04-16 | 2007-12-31 | Biogen Idec Ma Inc., | Antagonisti nogo receptora za tretman stanja sa amiloidnim plakovima |
| EA008253B1 (ru) | 2003-08-07 | 2007-04-27 | Байоджен Айдек Ма Инк. | Антагонисты nogo-рецептора |
| BRPI0413426A (pt) | 2003-08-07 | 2006-10-17 | Biogen Idec Inc | antagonistas de receptor novo |
| CN1946418A (zh) | 2004-01-30 | 2007-04-11 | 比奥根艾迪克Ma公司 | 利用nogo受体拮抗剂治疗涉及多巴胺能神经元退变的疾病 |
| WO2009114197A2 (en) | 2008-03-13 | 2009-09-17 | Yale University | Reactivation of axon growth and recovery in chronic spinal cord injury |
-
2001
- 2001-10-06 US US09/972,599 patent/US7119165B2/en not_active Expired - Lifetime
-
2002
- 2002-10-04 AU AU2002334889A patent/AU2002334889B2/en not_active Ceased
- 2002-10-04 CA CA002461655A patent/CA2461655A1/en not_active Abandoned
- 2002-10-04 JP JP2003534444A patent/JP4383869B2/ja not_active Expired - Fee Related
- 2002-10-04 EP EP02800939A patent/EP1451337A4/en not_active Withdrawn
- 2002-10-04 WO PCT/US2002/032007 patent/WO2003031462A2/en not_active Ceased
-
2006
- 2006-09-06 US US11/516,024 patent/US20080219984A1/en not_active Abandoned
-
2010
- 2010-01-26 US US12/693,940 patent/US8394929B2/en not_active Expired - Fee Related
-
2013
- 2013-03-07 US US13/788,923 patent/US20130171157A1/en not_active Abandoned
- 2013-11-22 US US14/088,158 patent/US20140178392A1/en not_active Abandoned
-
2015
- 2015-07-13 US US14/798,125 patent/US20170174763A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| AU2002334889B2 (en) | 2006-11-09 |
| US20130171157A1 (en) | 2013-07-04 |
| US20170174763A1 (en) | 2017-06-22 |
| WO2003031462A3 (en) | 2003-12-04 |
| EP1451337A4 (en) | 2005-08-17 |
| US20140178392A1 (en) | 2014-06-26 |
| CA2461655A1 (en) | 2003-04-17 |
| US20100278831A1 (en) | 2010-11-04 |
| US20020077295A1 (en) | 2002-06-20 |
| US8394929B2 (en) | 2013-03-12 |
| US20080219984A1 (en) | 2008-09-11 |
| WO2003031462A2 (en) | 2003-04-17 |
| JP2005508165A (ja) | 2005-03-31 |
| EP1451337A2 (en) | 2004-09-01 |
| US7119165B2 (en) | 2006-10-10 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP4383869B2 (ja) | 軸索成長のｎｏｇｏのレセプターを仲介とした妨害 | |
| JP4763207B2 (ja) | 軸索成長のｎｏｇｏレセプター媒介妨害 | |
| AU2002334889A1 (en) | Nogo receptor-mediated blockade of axonal growth | |
| US20040259092A1 (en) | Nogo receptor homologues and their use | |
| WO2000075184A1 (en) | Modulation of protein levels using the scf complex | |
| JP2010506930A (ja) | Ｔｌｒ１４の活性を変調するための組成物および方法 | |
| JP2001501476A (ja) | 脊椎動物Ｓｍｏｏｔｈｅｎｅｄタンパク質 | |
| JPH10505508A (ja) | Ｉｃａｍ−４物質及び方法 | |
| AU2006200819B2 (en) | Nogo Receptor-Mediated Blockade of Axonal Growth | |
| ZA200205403B (en) | Nogo receptor-mediated blockade of axonal growth. | |
| NZ547791A (en) | Nogo receptor-mediated blockade of axonal growth | |
| US20080241168A1 (en) | Transmembrane protein amigo and uses thereof | |
| JP2001508181A (ja) | Ｉｃａｍ−４及びその診断用途 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20051004 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20051004 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20080819 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20081119 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20081127 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20081218 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20090623 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20090804 |
|
| TRDD | Decision of grant or rejection written | ||
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20090825 |
|
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20090924 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20121002 Year of fee payment: 3 |
|
| R150 | Certificate of patent or registration of utility model |
Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20131002 Year of fee payment: 4 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| LAPS | Cancellation because of no payment of annual fees |