EA004256B1 - БЕЛОК, СВЯЗЫВАЮЩИЙСЯ С β-АМИЛОИДНЫМ ПЕПТИДОМ, КОДИРУЮЩИЙ ЕГО ПОЛИНУКЛЕОТИД И СПОСОБЫ ИХ ИСПОЛЬЗОВАНИЯ - Google Patents
БЕЛОК, СВЯЗЫВАЮЩИЙСЯ С β-АМИЛОИДНЫМ ПЕПТИДОМ, КОДИРУЮЩИЙ ЕГО ПОЛИНУКЛЕОТИД И СПОСОБЫ ИХ ИСПОЛЬЗОВАНИЯ Download PDFInfo
- Publication number
- EA004256B1 EA004256B1 EA199900941A EA199900941A EA004256B1 EA 004256 B1 EA004256 B1 EA 004256B1 EA 199900941 A EA199900941 A EA 199900941A EA 199900941 A EA199900941 A EA 199900941A EA 004256 B1 EA004256 B1 EA 004256B1
- Authority
- EA
- Eurasian Patent Office
- Prior art keywords
- protein
- fragment
- cdna molecule
- sequence
- polynucleotide
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 176
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 168
- 108091033319 polynucleotide Proteins 0.000 title claims abstract description 77
- 102000040430 polynucleotide Human genes 0.000 title claims abstract description 77
- 239000002157 polynucleotide Substances 0.000 title claims abstract description 77
- 238000000034 method Methods 0.000 title claims abstract description 44
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 27
- 230000027455 binding Effects 0.000 title claims description 24
- 239000002299 complementary DNA Substances 0.000 claims abstract description 65
- 239000012634 fragment Substances 0.000 claims abstract description 59
- 239000002773 nucleotide Substances 0.000 claims abstract description 51
- 125000003729 nucleotide group Chemical group 0.000 claims abstract description 50
- 210000004027 cell Anatomy 0.000 claims abstract description 48
- 230000014509 gene expression Effects 0.000 claims abstract description 45
- 150000001413 amino acids Chemical class 0.000 claims abstract description 37
- 102000037865 fusion proteins Human genes 0.000 claims abstract description 35
- 108020001507 fusion proteins Proteins 0.000 claims abstract description 35
- 239000000523 sample Substances 0.000 claims abstract description 33
- DZHSAHHDTRWUTF-SIQRNXPUSA-N amyloid-beta polypeptide 42 Chemical compound C([C@@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)NCC(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(O)=O)[C@@H](C)CC)C(C)C)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@@H](NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC(O)=O)C(C)C)C(C)C)C1=CC=CC=C1 DZHSAHHDTRWUTF-SIQRNXPUSA-N 0.000 claims abstract description 16
- 210000004556 brain Anatomy 0.000 claims abstract description 16
- 230000002068 genetic effect Effects 0.000 claims abstract description 10
- 108091034117 Oligonucleotide Proteins 0.000 claims abstract description 9
- 239000001963 growth medium Substances 0.000 claims abstract description 5
- 230000000295 complement effect Effects 0.000 claims abstract description 4
- 210000003527 eukaryotic cell Anatomy 0.000 claims abstract 2
- 210000001236 prokaryotic cell Anatomy 0.000 claims abstract 2
- 238000009396 hybridization Methods 0.000 claims description 20
- 238000009825 accumulation Methods 0.000 claims description 3
- 239000003112 inhibitor Substances 0.000 claims description 2
- 101150056371 BBR1 gene Proteins 0.000 claims 1
- 230000002401 inhibitory effect Effects 0.000 claims 1
- 102100032067 TM2 domain-containing protein 1 Human genes 0.000 abstract description 31
- 101000638018 Homo sapiens TM2 domain-containing protein 1 Proteins 0.000 abstract description 24
- 230000008569 process Effects 0.000 abstract description 3
- 101150111117 BBP1 gene Proteins 0.000 abstract description 2
- 230000007082 Aβ accumulation Effects 0.000 abstract 1
- 229940122498 Gene expression inhibitor Drugs 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 125
- 101710145783 TATA-box-binding protein Proteins 0.000 description 78
- 102100031156 Prohibitin-2 Human genes 0.000 description 75
- 238000012360 testing method Methods 0.000 description 41
- 239000013612 plasmid Substances 0.000 description 40
- 108020004414 DNA Proteins 0.000 description 36
- 241000282414 Homo sapiens Species 0.000 description 34
- 235000001014 amino acid Nutrition 0.000 description 33
- 229940024606 amino acid Drugs 0.000 description 31
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 26
- 241000283984 Rodentia Species 0.000 description 26
- 125000003275 alpha amino acid group Chemical group 0.000 description 25
- 239000000047 product Substances 0.000 description 23
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 22
- 239000000203 mixture Substances 0.000 description 22
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 20
- 238000003752 polymerase chain reaction Methods 0.000 description 19
- 230000003993 interaction Effects 0.000 description 18
- 239000013598 vector Substances 0.000 description 18
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 17
- 241000894007 species Species 0.000 description 17
- 108020004705 Codon Proteins 0.000 description 16
- 102000004196 processed proteins & peptides Human genes 0.000 description 14
- 210000001519 tissue Anatomy 0.000 description 13
- 108020004999 messenger RNA Proteins 0.000 description 12
- 229920001184 polypeptide Polymers 0.000 description 12
- 230000004044 response Effects 0.000 description 12
- 238000006467 substitution reaction Methods 0.000 description 12
- 101000836873 Homo sapiens Nucleotide exchange factor SIL1 Proteins 0.000 description 11
- 102000052329 human SIL1 Human genes 0.000 description 11
- 238000010367 cloning Methods 0.000 description 10
- 238000012216 screening Methods 0.000 description 10
- 239000000243 solution Substances 0.000 description 10
- 108091008146 restriction endonucleases Proteins 0.000 description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 238000004458 analytical method Methods 0.000 description 8
- 230000000692 anti-sense effect Effects 0.000 description 8
- 239000000872 buffer Substances 0.000 description 8
- 239000003153 chemical reaction reagent Substances 0.000 description 8
- 150000001875 compounds Chemical class 0.000 description 8
- 230000000694 effects Effects 0.000 description 8
- 239000002609 medium Substances 0.000 description 8
- 208000024827 Alzheimer disease Diseases 0.000 description 7
- 230000004568 DNA-binding Effects 0.000 description 7
- 101100382264 Mus musculus Ca14 gene Proteins 0.000 description 7
- 235000019441 ethanol Nutrition 0.000 description 7
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 6
- 241000700159 Rattus Species 0.000 description 6
- 230000004913 activation Effects 0.000 description 6
- 238000006243 chemical reaction Methods 0.000 description 6
- 239000012153 distilled water Substances 0.000 description 6
- 230000003834 intracellular effect Effects 0.000 description 6
- 239000003550 marker Substances 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 238000000746 purification Methods 0.000 description 6
- 208000037259 Amyloid Plaque Diseases 0.000 description 5
- 101710117545 C protein Proteins 0.000 description 5
- 241000238631 Hexapoda Species 0.000 description 5
- 108091092195 Intron Proteins 0.000 description 5
- 206010029350 Neurotoxicity Diseases 0.000 description 5
- 108700008625 Reporter Genes Proteins 0.000 description 5
- 206010044221 Toxic encephalopathy Diseases 0.000 description 5
- 239000012190 activator Substances 0.000 description 5
- 230000002776 aggregation Effects 0.000 description 5
- 238000004220 aggregation Methods 0.000 description 5
- 230000003321 amplification Effects 0.000 description 5
- 230000012010 growth Effects 0.000 description 5
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 5
- 231100000228 neurotoxicity Toxicity 0.000 description 5
- 230000007135 neurotoxicity Effects 0.000 description 5
- 238000003199 nucleic acid amplification method Methods 0.000 description 5
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 4
- 108091026890 Coding region Proteins 0.000 description 4
- 241000701959 Escherichia virus Lambda Species 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
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 4
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 4
- 241001465754 Metazoa Species 0.000 description 4
- 241000699666 Mus <mouse, genus> Species 0.000 description 4
- 238000000636 Northern blotting Methods 0.000 description 4
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 4
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 4
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 239000000839 emulsion Substances 0.000 description 4
- 230000001605 fetal effect Effects 0.000 description 4
- 230000000971 hippocampal effect Effects 0.000 description 4
- 210000001320 hippocampus Anatomy 0.000 description 4
- 238000007654 immersion Methods 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- 238000002955 isolation Methods 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 210000002569 neuron Anatomy 0.000 description 4
- 239000011541 reaction mixture Substances 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 238000013518 transcription Methods 0.000 description 4
- 230000035897 transcription Effects 0.000 description 4
- WFDIJRYMOXRFFG-UHFFFAOYSA-N Acetic anhydride Chemical compound CC(=O)OC(C)=O WFDIJRYMOXRFFG-UHFFFAOYSA-N 0.000 description 3
- KLSJWNVTNUYHDU-UHFFFAOYSA-N Amitrole Chemical compound NC1=NC=NN1 KLSJWNVTNUYHDU-UHFFFAOYSA-N 0.000 description 3
- 238000001712 DNA sequencing Methods 0.000 description 3
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 3
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 3
- 102100034343 Integrase Human genes 0.000 description 3
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 3
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 3
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 3
- 101100165188 Schizophyllum commune BBR1 gene Proteins 0.000 description 3
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 description 3
- 239000007983 Tris buffer Substances 0.000 description 3
- 230000002159 abnormal effect Effects 0.000 description 3
- 239000002671 adjuvant Substances 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 230000033228 biological regulation Effects 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 210000003710 cerebral cortex Anatomy 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 238000009826 distribution Methods 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 238000006206 glycosylation reaction Methods 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 230000000977 initiatory effect Effects 0.000 description 3
- -1 lysolecithin Chemical compound 0.000 description 3
- 230000007246 mechanism Effects 0.000 description 3
- 238000002844 melting Methods 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 229930182817 methionine Natural products 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 150000007523 nucleic acids Chemical class 0.000 description 3
- 239000002751 oligonucleotide probe Substances 0.000 description 3
- 230000008506 pathogenesis Effects 0.000 description 3
- 230000037361 pathway Effects 0.000 description 3
- 239000002243 precursor Substances 0.000 description 3
- 230000037452 priming Effects 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 231100000331 toxic Toxicity 0.000 description 3
- 230000002588 toxic effect Effects 0.000 description 3
- 230000009261 transgenic effect Effects 0.000 description 3
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
- 210000004881 tumor cell Anatomy 0.000 description 3
- 102100022900 Actin, cytoplasmic 1 Human genes 0.000 description 2
- 108010085238 Actins Proteins 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- 241000972773 Aulopiformes Species 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 102100021257 Beta-secretase 1 Human genes 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 241000867607 Chlorocebus sabaeus Species 0.000 description 2
- 241000699802 Cricetulus griseus Species 0.000 description 2
- 102000012410 DNA Ligases Human genes 0.000 description 2
- 108010061982 DNA Ligases Proteins 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- 229920002527 Glycogen Polymers 0.000 description 2
- WZUVPPKBWHMQCE-UHFFFAOYSA-N Haematoxylin Chemical compound C12=CC(O)=C(O)C=C2CC2(O)C1C1=CC=C(O)C(O)=C1OC2 WZUVPPKBWHMQCE-UHFFFAOYSA-N 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 101000894895 Homo sapiens Beta-secretase 1 Proteins 0.000 description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 2
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 241001494479 Pecora Species 0.000 description 2
- 102000001708 Protein Isoforms Human genes 0.000 description 2
- 108010029485 Protein Isoforms Proteins 0.000 description 2
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 2
- 238000002441 X-ray diffraction Methods 0.000 description 2
- 239000008186 active pharmaceutical agent Substances 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 125000003118 aryl group Chemical group 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 239000012472 biological sample Substances 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 210000004958 brain cell Anatomy 0.000 description 2
- 230000003915 cell function Effects 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 210000003169 central nervous system Anatomy 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 238000012411 cloning technique Methods 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 125000004122 cyclic group Chemical group 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 210000001787 dendrite Anatomy 0.000 description 2
- 238000001514 detection method 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
- 239000013613 expression plasmid Substances 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 235000013922 glutamic acid Nutrition 0.000 description 2
- 239000004220 glutamic acid Substances 0.000 description 2
- 229940096919 glycogen Drugs 0.000 description 2
- 230000013595 glycosylation Effects 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 210000004408 hybridoma Anatomy 0.000 description 2
- PHTQWCKDNZKARW-UHFFFAOYSA-N isoamylol Chemical compound CC(C)CCO PHTQWCKDNZKARW-UHFFFAOYSA-N 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 208000032839 leukemia Diseases 0.000 description 2
- KWGKDLIKAYFUFQ-UHFFFAOYSA-M lithium chloride Chemical compound [Li+].[Cl-] KWGKDLIKAYFUFQ-UHFFFAOYSA-M 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 201000001441 melanoma Diseases 0.000 description 2
- 230000008018 melting Effects 0.000 description 2
- 230000009456 molecular mechanism Effects 0.000 description 2
- 230000002887 neurotoxic effect Effects 0.000 description 2
- 230000008520 organization Effects 0.000 description 2
- 210000001672 ovary Anatomy 0.000 description 2
- 230000035515 penetration Effects 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 108020001580 protein domains Proteins 0.000 description 2
- 238000001742 protein purification Methods 0.000 description 2
- 230000004850 protein–protein interaction Effects 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 235000019515 salmon Nutrition 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 238000013207 serial dilution Methods 0.000 description 2
- 239000001509 sodium citrate Substances 0.000 description 2
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 2
- 102000013498 tau Proteins Human genes 0.000 description 2
- 108010026424 tau Proteins Proteins 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 239000011534 wash buffer Substances 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- 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
- DURPTKYDGMDSBL-UHFFFAOYSA-N 1-butoxybutane Chemical compound CCCCOCCCC DURPTKYDGMDSBL-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
- OSBLTNPMIGYQGY-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;2-[2-[bis(carboxymethyl)amino]ethyl-(carboxymethyl)amino]acetic acid;boric acid Chemical compound OB(O)O.OCC(N)(CO)CO.OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O OSBLTNPMIGYQGY-UHFFFAOYSA-N 0.000 description 1
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 description 1
- 102100029510 26S proteasome regulatory subunit 6A Human genes 0.000 description 1
- 208000036762 Acute promyelocytic leukaemia Diseases 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
- 239000005695 Ammonium acetate Substances 0.000 description 1
- 108010090849 Amyloid beta-Peptides Proteins 0.000 description 1
- 102000013455 Amyloid beta-Peptides Human genes 0.000 description 1
- 102000014303 Amyloid beta-Protein Precursor Human genes 0.000 description 1
- 108010079054 Amyloid beta-Protein Precursor Proteins 0.000 description 1
- 101710151993 Amyloid-beta precursor protein Proteins 0.000 description 1
- 241001276061 Anisotremus davidsonii Species 0.000 description 1
- 208000032791 BCR-ABL1 positive chronic myelogenous leukemia Diseases 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 208000011691 Burkitt lymphomas Diseases 0.000 description 1
- 241000219357 Cactaceae Species 0.000 description 1
- 101100018996 Caenorhabditis elegans lfe-2 gene Proteins 0.000 description 1
- 101100408682 Caenorhabditis elegans pmt-2 gene Proteins 0.000 description 1
- 101100086436 Caenorhabditis elegans rap-1 gene Proteins 0.000 description 1
- 241000824799 Canis lupus dingo Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 208000010833 Chronic myeloid leukaemia Diseases 0.000 description 1
- 206010052360 Colorectal adenocarcinoma Diseases 0.000 description 1
- 108010062580 Concanavalin A Proteins 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 102000004594 DNA Polymerase I Human genes 0.000 description 1
- 108010017826 DNA Polymerase I Proteins 0.000 description 1
- 206010012289 Dementia Diseases 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 241000282575 Gorilla Species 0.000 description 1
- 101001125540 Homo sapiens 26S proteasome regulatory subunit 6A Proteins 0.000 description 1
- 101000823051 Homo sapiens Amyloid-beta precursor protein Proteins 0.000 description 1
- 101000891654 Homo sapiens TATA-box-binding protein Proteins 0.000 description 1
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 1
- 241000282620 Hylobates sp. Species 0.000 description 1
- 241001026509 Kata Species 0.000 description 1
- 241000288904 Lemur Species 0.000 description 1
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 1
- 241000282553 Macaca Species 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 101100073975 Mus musculus Krt33b gene Proteins 0.000 description 1
- 208000033761 Myelogenous Chronic BCR-ABL Positive Leukemia Diseases 0.000 description 1
- 241000244206 Nematoda Species 0.000 description 1
- 241000772415 Neovison vison Species 0.000 description 1
- 206010029260 Neuroblastoma Diseases 0.000 description 1
- 101100420081 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) rps-0 gene Proteins 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 241000282577 Pan troglodytes Species 0.000 description 1
- 108020002230 Pancreatic Ribonuclease Proteins 0.000 description 1
- 102000005891 Pancreatic ribonuclease Human genes 0.000 description 1
- 241001504519 Papio ursinus Species 0.000 description 1
- 229930040373 Paraformaldehyde Natural products 0.000 description 1
- 241000282405 Pongo abelii Species 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 108020005144 RNA 5' Terminal Oligopyrimidine Sequence Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 239000008051 TBE buffer Substances 0.000 description 1
- DSGIVWSDDRDJIO-ZXXMMSQZSA-N Thr-Thr Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(O)=O DSGIVWSDDRDJIO-ZXXMMSQZSA-N 0.000 description 1
- 102000004357 Transferases Human genes 0.000 description 1
- 108090000992 Transferases Proteins 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- 239000007984 Tris EDTA buffer Substances 0.000 description 1
- 102100025836 Voltage-dependent L-type calcium channel subunit beta-4 Human genes 0.000 description 1
- 101710176693 Voltage-dependent L-type calcium channel subunit beta-4 Proteins 0.000 description 1
- 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 1
- 230000005856 abnormality Effects 0.000 description 1
- YRKCREAYFQTBPV-UHFFFAOYSA-N acetylacetone Chemical compound CC(=O)CC(C)=O YRKCREAYFQTBPV-UHFFFAOYSA-N 0.000 description 1
- 108091006088 activator proteins Proteins 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- 229940043376 ammonium acetate Drugs 0.000 description 1
- 235000019257 ammonium acetate Nutrition 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- 210000001130 astrocyte Anatomy 0.000 description 1
- 238000011888 autopsy Methods 0.000 description 1
- 238000000211 autoradiogram Methods 0.000 description 1
- 210000003050 axon Anatomy 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 101150105454 bap gene Proteins 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 210000005013 brain tissue Anatomy 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 238000010805 cDNA synthesis kit Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 210000004720 cerebrum Anatomy 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 210000001072 colon Anatomy 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 230000037011 constitutive activity Effects 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 210000001947 dentate gyrus Anatomy 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000012631 diagnostic technique Methods 0.000 description 1
- FFYPMLJYZAEMQB-UHFFFAOYSA-N diethyl pyrocarbonate Chemical compound CCOC(=O)OC(=O)OCC FFYPMLJYZAEMQB-UHFFFAOYSA-N 0.000 description 1
- USIUVYZYUHIAEV-UHFFFAOYSA-N diphenyl ether Chemical compound C=1C=CC=CC=1OC1=CC=CC=C1 USIUVYZYUHIAEV-UHFFFAOYSA-N 0.000 description 1
- 210000001840 diploid cell Anatomy 0.000 description 1
- POLCUAVZOMRGSN-UHFFFAOYSA-N dipropyl ether Chemical compound CCCOCCC POLCUAVZOMRGSN-UHFFFAOYSA-N 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 235000013601 eggs Nutrition 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 210000001339 epidermal cell Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 238000010448 genetic screening Methods 0.000 description 1
- 210000004602 germ cell Anatomy 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- 229940094991 herring sperm dna Drugs 0.000 description 1
- 230000001744 histochemical effect Effects 0.000 description 1
- 102000046783 human APP Human genes 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 230000005965 immune activity Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000037189 immune system physiology Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 210000003292 kidney cell Anatomy 0.000 description 1
- 101150011910 lfe-2 gene Proteins 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 230000002197 limbic effect Effects 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- PWPJGUXAGUPAHP-UHFFFAOYSA-N lufenuron Chemical compound C1=C(Cl)C(OC(F)(F)C(C(F)(F)F)F)=CC(Cl)=C1NC(=O)NC(=O)C1=C(F)C=CC=C1F PWPJGUXAGUPAHP-UHFFFAOYSA-N 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 201000005296 lung carcinoma Diseases 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 210000005075 mammary gland Anatomy 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 210000000274 microglia Anatomy 0.000 description 1
- 102000021160 microtubule binding proteins Human genes 0.000 description 1
- 108091011150 microtubule binding proteins Proteins 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
- 239000011707 mineral Substances 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 210000002682 neurofibrillary tangle Anatomy 0.000 description 1
- 210000004498 neuroglial cell Anatomy 0.000 description 1
- 230000000926 neurological effect Effects 0.000 description 1
- 238000007899 nucleic acid hybridization Methods 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 229920002866 paraformaldehyde Polymers 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 229920001983 poloxamer Polymers 0.000 description 1
- 229920000447 polyanionic polymer Polymers 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 230000000750 progressive effect Effects 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 230000004952 protein activity Effects 0.000 description 1
- 230000006916 protein interaction Effects 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 238000004445 quantitative analysis Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 239000011435 rock Substances 0.000 description 1
- 230000009834 selective interaction Effects 0.000 description 1
- 239000003001 serine protease inhibitor Substances 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 230000007727 signaling mechanism Effects 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 101150106357 slc32a1 gene Proteins 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 229910001415 sodium ion Inorganic materials 0.000 description 1
- AKHNMLFCWUSKQB-UHFFFAOYSA-L sodium thiosulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=S AKHNMLFCWUSKQB-UHFFFAOYSA-L 0.000 description 1
- 235000019345 sodium thiosulphate Nutrition 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 210000001082 somatic cell Anatomy 0.000 description 1
- 230000000392 somatic effect Effects 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 230000000946 synaptic effect Effects 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 101150020633 tbp-1 gene Proteins 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 238000002604 ultrasonography Methods 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 229940035893 uracil Drugs 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
-
- 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
-
- 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
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4711—Alzheimer's disease; Amyloid plaque core protein
-
- 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
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Neurology (AREA)
- Biomedical Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Public Health (AREA)
- Neurosurgery (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Animal Behavior & Ethology (AREA)
- Hospice & Palliative Care (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Psychiatry (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Immunology (AREA)
- Epidemiology (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US6458397P | 1997-04-16 | 1997-04-16 | |
| PCT/US1998/007462 WO1998046636A2 (en) | 1997-04-16 | 1998-04-14 | β-AMYLOID PEPTIDE-BINDING PROTEINS AND POLYNUCLEOTIDES ENCODING THE SAME |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EA199900941A1 EA199900941A1 (ru) | 2000-06-26 |
| EA004256B1 true EA004256B1 (ru) | 2004-02-26 |
Family
ID=22056941
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EA199900941A EA004256B1 (ru) | 1997-04-16 | 1998-04-14 | БЕЛОК, СВЯЗЫВАЮЩИЙСЯ С β-АМИЛОИДНЫМ ПЕПТИДОМ, КОДИРУЮЩИЙ ЕГО ПОЛИНУКЛЕОТИД И СПОСОБЫ ИХ ИСПОЛЬЗОВАНИЯ |
Country Status (18)
| Country | Link |
|---|---|
| EP (1) | EP0975753A2 (enExample) |
| JP (3) | JP2001523093A (enExample) |
| KR (1) | KR20010006393A (enExample) |
| CN (2) | CN1196785C (enExample) |
| AU (1) | AU740445B2 (enExample) |
| BR (1) | BR9808562A (enExample) |
| CA (1) | CA2286484A1 (enExample) |
| EA (1) | EA004256B1 (enExample) |
| EE (1) | EE9900482A (enExample) |
| GE (1) | GEP20043386B (enExample) |
| HU (1) | HUP0003116A3 (enExample) |
| ID (1) | ID24914A (enExample) |
| IL (3) | IL132236A0 (enExample) |
| NO (1) | NO995062L (enExample) |
| NZ (1) | NZ500216A (enExample) |
| SK (1) | SK143299A3 (enExample) |
| UA (1) | UA72875C2 (enExample) |
| WO (1) | WO1998046636A2 (enExample) |
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7005295B1 (en) | 1997-04-16 | 2006-02-28 | Wyeth | β-amyloid peptide-binding proteins and polynucleotides encoding the same |
| US6787319B2 (en) * | 1997-04-16 | 2004-09-07 | American Home Products Corp. | β-amyloid peptide-binding proteins and polynucleotides encoding the same |
| NZ510997A (en) * | 1998-10-13 | 2004-01-30 | Wyeth Corp | G-protein-coupled receptor-like proteins, polynucleotides encoded by them, and methods of using same |
| US6455082B1 (en) * | 1999-04-26 | 2002-09-24 | Nestec S.A. | Shelf-stable calcium fortified milk and dairy products |
| WO2001029225A1 (en) * | 1999-10-21 | 2001-04-26 | Panorama Research, Inc. | A general method for optimizing the expression of heterologous proteins |
| US8663650B2 (en) | 2003-02-21 | 2014-03-04 | Ac Immune Sa | Methods and compositions comprising supramolecular constructs |
| US7807171B2 (en) | 2003-07-25 | 2010-10-05 | Ac Immune Sa | Therapeutic vaccine targeted against P-glycoprotein 170 for inhibiting multidrug resistance in the treatment of cancers |
| WO2012020124A1 (en) | 2010-08-12 | 2012-02-16 | Ac Immune S.A. | Vaccine engineering |
| JP6027011B2 (ja) | 2010-10-26 | 2016-11-16 | エーシー イミューン ソシエテ アノニム | 疎水性部分によって修飾されたペプチドを含むリポソームベースの構築物 |
| CN102060912B (zh) * | 2010-11-22 | 2012-11-14 | 清华大学 | 淀粉样蛋白寡聚体构象型抗原表位多肽及其应用 |
| CN111320678B (zh) * | 2020-03-09 | 2023-06-09 | 安亭生物有限责任公司 | 抗菌肽突变体及其应用 |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0332640A1 (en) * | 1986-11-17 | 1989-09-20 | California Biotechnology, Inc. | Recombinant alzheimer's amyloid protein |
| IL115743A0 (en) * | 1994-10-28 | 1996-01-19 | American Nat Red Cross | A mammal with cells containing a transgene and its production |
| US5786180A (en) * | 1995-02-14 | 1998-07-28 | Bayer Corporation | Monoclonal antibody 369.2B specific for β A4 peptide |
-
1998
- 1998-04-14 WO PCT/US1998/007462 patent/WO1998046636A2/en not_active Ceased
- 1998-04-14 IL IL13223698A patent/IL132236A0/xx active IP Right Grant
- 1998-04-14 AU AU71156/98A patent/AU740445B2/en not_active Ceased
- 1998-04-14 EP EP98918186A patent/EP0975753A2/en not_active Withdrawn
- 1998-04-14 ID IDW991187D patent/ID24914A/id unknown
- 1998-04-14 GE GE3744A patent/GEP20043386B/en unknown
- 1998-04-14 UA UA99116193A patent/UA72875C2/uk unknown
- 1998-04-14 SK SK1432-99A patent/SK143299A3/sk unknown
- 1998-04-14 CN CNB988043173A patent/CN1196785C/zh not_active Expired - Fee Related
- 1998-04-14 JP JP54419698A patent/JP2001523093A/ja active Pending
- 1998-04-14 EE EEP199900482A patent/EE9900482A/xx unknown
- 1998-04-14 CA CA002286484A patent/CA2286484A1/en not_active Abandoned
- 1998-04-14 EA EA199900941A patent/EA004256B1/ru not_active IP Right Cessation
- 1998-04-14 HU HU0003116A patent/HUP0003116A3/hu unknown
- 1998-04-14 KR KR1019997009480A patent/KR20010006393A/ko not_active Ceased
- 1998-04-14 BR BR9808562-0A patent/BR9808562A/pt not_active Application Discontinuation
- 1998-04-14 CN CNA200510052975XA patent/CN1690203A/zh active Pending
- 1998-04-14 NZ NZ500216A patent/NZ500216A/xx unknown
-
1999
- 1999-10-06 IL IL132236A patent/IL132236A/en not_active IP Right Cessation
- 1999-10-15 NO NO995062A patent/NO995062L/no not_active Application Discontinuation
-
2006
- 2006-11-05 IL IL179047A patent/IL179047A0/en unknown
-
2007
- 2007-12-28 JP JP2007339660A patent/JP2008104465A/ja active Pending
-
2008
- 2008-06-18 JP JP2008159606A patent/JP2008253275A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| CN1196785C (zh) | 2005-04-13 |
| NO995062L (no) | 1999-12-14 |
| JP2008104465A (ja) | 2008-05-08 |
| ID24914A (id) | 2000-08-31 |
| HUP0003116A3 (en) | 2003-03-28 |
| CN1268973A (zh) | 2000-10-04 |
| EA199900941A1 (ru) | 2000-06-26 |
| IL132236A0 (en) | 2001-03-19 |
| EE9900482A (enExample) | 2000-06-15 |
| KR20010006393A (ko) | 2001-01-26 |
| HUP0003116A2 (hu) | 2001-01-29 |
| BR9808562A (pt) | 2000-05-23 |
| GEP20043386B (en) | 2004-02-10 |
| JP2001523093A (ja) | 2001-11-20 |
| NZ500216A (en) | 2001-06-29 |
| CN1690203A (zh) | 2005-11-02 |
| NO995062D0 (no) | 1999-10-15 |
| JP2008253275A (ja) | 2008-10-23 |
| AU7115698A (en) | 1998-11-11 |
| AU740445B2 (en) | 2001-11-01 |
| IL179047A0 (en) | 2007-03-08 |
| WO1998046636A3 (en) | 1999-01-28 |
| CA2286484A1 (en) | 1998-10-22 |
| SK143299A3 (en) | 2000-09-12 |
| WO1998046636A2 (en) | 1998-10-22 |
| UA72875C2 (uk) | 2005-05-16 |
| IL132236A (en) | 2007-03-08 |
| EP0975753A2 (en) | 2000-02-02 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| KR100499600B1 (ko) | 신생 세포 성장을 억제하기 위한 방법 및 조성물 | |
| AU2003200722B2 (en) | Compositions and methods for the treatment of tumor | |
| JP6144247B2 (ja) | ヒト非小細胞肺癌における転座および変異ｒｏｓキナーゼ | |
| EP1220905A2 (en) | Composition and methods for the treatment of immune related diseases | |
| JP4252501B2 (ja) | 腫瘍の治療のための組成物と方法 | |
| JP2002518010A (ja) | ９４個のヒト分泌タンパク質 | |
| JP2010501175A (ja) | ヒト固形腫瘍における遺伝子欠失及び突然変異ａｌｋキナーゼ | |
| WO2004110345A2 (en) | Differentially expressed genes involved in cancer, the polypeptides encoded thereby, and methods of using the same | |
| JP2002533058A (ja) | ９７個のヒト分泌タンパク質 | |
| CA2378182C (en) | Compositions and methods for the treatment of tumors | |
| JP2002506627A (ja) | ９５個のヒト分泌タンパク質 | |
| EA004256B1 (ru) | БЕЛОК, СВЯЗЫВАЮЩИЙСЯ С β-АМИЛОИДНЫМ ПЕПТИДОМ, КОДИРУЮЩИЙ ЕГО ПОЛИНУКЛЕОТИД И СПОСОБЫ ИХ ИСПОЛЬЗОВАНИЯ | |
| KR20020008123A (ko) | 종양 치료용 조성물 및 방법 | |
| CA2341304A1 (en) | Compositions and methods for the treatment of tumors | |
| JP2000511765A (ja) | 精製ＳＲ―ｐ７０タンパク質 | |
| EP1854881B1 (en) | METHODS FOR IDENTIFYING PURKINJE CELLS USING THE Corl2 GENE AS A TARGET | |
| WO2003102028A1 (fr) | Proteine induite par le gene rb1 (rb1cc1) et gene | |
| JP2002504361A (ja) | ３６個のヒト分泌タンパク質 | |
| JP6740172B2 (ja) | ヒト固形腫瘍における遺伝子欠失及び突然変異ａｌｋキナーゼ | |
| JP6141224B2 (ja) | ヒト固形腫瘍における遺伝子欠失及び突然変異ａｌｋキナーゼ | |
| AU776063C (en) | Compositions and methods for the treatment of tumor | |
| WO2001005836A1 (en) | Polypeptidic compositions and methods for the treatment of tumors | |
| AU2003200721B2 (en) | Compositions and methods for the treatment of tumor | |
| JP2020156481A (ja) | ヒト固形腫瘍における遺伝子欠失及び突然変異ａｌｋキナーゼ | |
| EP1870464A2 (en) | Methods and compositions for inhibiting neoplastic cell growth |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM4A | Lapse of a eurasian patent due to non-payment of renewal fees within the time limit in the following designated state(s) |
Designated state(s): AM AZ BY KZ KG MD TJ TM RU |