KR20030034156A - 막 관통 펩타이드 및 이의 용도 - Google Patents
막 관통 펩타이드 및 이의 용도 Download PDFInfo
- Publication number
- KR20030034156A KR20030034156A KR10-2003-7002754A KR20037002754A KR20030034156A KR 20030034156 A KR20030034156 A KR 20030034156A KR 20037002754 A KR20037002754 A KR 20037002754A KR 20030034156 A KR20030034156 A KR 20030034156A
- Authority
- KR
- South Korea
- Prior art keywords
- protein
- cell
- peptide
- interest
- sequence
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 144
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 82
- 239000012528 membrane Substances 0.000 title claims abstract description 41
- 230000000149 penetrating effect Effects 0.000 title claims abstract description 25
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 116
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 111
- 150000001875 compounds Chemical class 0.000 claims abstract description 53
- 238000000034 method Methods 0.000 claims abstract description 34
- 238000001727 in vivo Methods 0.000 claims abstract description 15
- 238000000338 in vitro Methods 0.000 claims abstract description 11
- 210000004027 cell Anatomy 0.000 claims description 129
- 108020001507 fusion proteins Proteins 0.000 claims description 41
- 102000037865 fusion proteins Human genes 0.000 claims description 41
- 230000030648 nucleus localization Effects 0.000 claims description 30
- 229920001184 polypeptide Polymers 0.000 claims description 24
- 230000003834 intracellular effect Effects 0.000 claims description 23
- 239000004475 Arginine Substances 0.000 claims description 22
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 22
- 102000007999 Nuclear Proteins Human genes 0.000 claims description 20
- 108010089610 Nuclear Proteins Proteins 0.000 claims description 20
- 230000004927 fusion Effects 0.000 claims description 20
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims description 17
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 17
- 230000027455 binding Effects 0.000 claims description 15
- 241000282414 Homo sapiens Species 0.000 claims description 14
- 239000004472 Lysine Substances 0.000 claims description 14
- 102000040945 Transcription factor Human genes 0.000 claims description 14
- 108091023040 Transcription factor Proteins 0.000 claims description 14
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 14
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims description 12
- 210000000805 cytoplasm Anatomy 0.000 claims description 12
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims description 11
- 108010058643 Fungal Proteins Proteins 0.000 claims description 5
- 210000004748 cultured cell Anatomy 0.000 claims description 5
- 102000039446 nucleic acids Human genes 0.000 claims description 5
- 108020004707 nucleic acids Proteins 0.000 claims description 5
- 150000007523 nucleic acids Chemical class 0.000 claims description 5
- 238000005516 engineering process Methods 0.000 claims description 4
- 239000002243 precursor Substances 0.000 claims description 3
- 238000003786 synthesis reaction Methods 0.000 claims description 3
- 230000015556 catabolic process Effects 0.000 claims description 2
- 102000007001 Period Circadian Proteins Human genes 0.000 claims 4
- 108010047728 Period Circadian Proteins Proteins 0.000 claims 4
- 238000002144 chemical decomposition reaction Methods 0.000 claims 1
- 150000005829 chemical entities Chemical class 0.000 claims 1
- 108091005703 transmembrane proteins Proteins 0.000 claims 1
- 102000035160 transmembrane proteins Human genes 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 104
- 238000001167 microscope projection photolithography Methods 0.000 description 102
- 210000001357 hemopoietic progenitor cell Anatomy 0.000 description 54
- 150000001413 amino acids Chemical class 0.000 description 36
- 229940024606 amino acid Drugs 0.000 description 35
- 235000001014 amino acid Nutrition 0.000 description 34
- 210000004940 nucleus Anatomy 0.000 description 34
- 108010005774 beta-Galactosidase Proteins 0.000 description 23
- 102000005936 beta-Galactosidase Human genes 0.000 description 20
- 210000000170 cell membrane Anatomy 0.000 description 20
- 230000007246 mechanism Effects 0.000 description 20
- 230000035515 penetration Effects 0.000 description 18
- 102000005962 receptors Human genes 0.000 description 17
- 108020003175 receptors Proteins 0.000 description 17
- 101710085003 Alpha-tubulin N-acetyltransferase Proteins 0.000 description 15
- 101710085461 Alpha-tubulin N-acetyltransferase 1 Proteins 0.000 description 15
- 101710175714 Tyrosine aminotransferase Proteins 0.000 description 15
- 230000001419 dependent effect Effects 0.000 description 15
- 230000004807 localization Effects 0.000 description 15
- 102000004190 Enzymes Human genes 0.000 description 14
- 108090000790 Enzymes Proteins 0.000 description 14
- 229940088598 enzyme Drugs 0.000 description 14
- 239000002953 phosphate buffered saline Substances 0.000 description 14
- 230000001086 cytosolic effect Effects 0.000 description 13
- 230000005937 nuclear translocation Effects 0.000 description 13
- 238000012217 deletion Methods 0.000 description 12
- 230000008685 targeting Effects 0.000 description 12
- 102000003971 Fibroblast Growth Factor 1 Human genes 0.000 description 11
- 108090000386 Fibroblast Growth Factor 1 Proteins 0.000 description 11
- 125000003275 alpha amino acid group Chemical group 0.000 description 11
- 125000000539 amino acid group Chemical group 0.000 description 11
- 230000037430 deletion Effects 0.000 description 11
- 210000004492 nuclear pore Anatomy 0.000 description 11
- 230000037361 pathway Effects 0.000 description 11
- 210000003412 trans-golgi network Anatomy 0.000 description 11
- 235000004279 alanine Nutrition 0.000 description 10
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 10
- 238000010348 incorporation Methods 0.000 description 10
- 210000001519 tissue Anatomy 0.000 description 10
- 101150019028 Antp gene Proteins 0.000 description 9
- 108010076504 Protein Sorting Signals Proteins 0.000 description 9
- 101710192266 Tegument protein VP22 Proteins 0.000 description 9
- 230000000694 effects Effects 0.000 description 9
- 230000008676 import Effects 0.000 description 9
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 8
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 8
- 241000699666 Mus <mouse, genus> Species 0.000 description 8
- 108010004469 allophycocyanin Proteins 0.000 description 8
- 230000006870 function Effects 0.000 description 8
- 230000014509 gene expression Effects 0.000 description 8
- QZAYGJVTTNCVMB-UHFFFAOYSA-N serotonin Chemical compound C1=C(O)C=C2C(CCN)=CNC2=C1 QZAYGJVTTNCVMB-UHFFFAOYSA-N 0.000 description 8
- 239000013598 vector Substances 0.000 description 8
- 108020004414 DNA Proteins 0.000 description 7
- 102000003688 G-Protein-Coupled Receptors Human genes 0.000 description 7
- 108090000045 G-Protein-Coupled Receptors Proteins 0.000 description 7
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 7
- 210000004899 c-terminal region Anatomy 0.000 description 7
- 238000002474 experimental method Methods 0.000 description 7
- 235000014304 histidine Nutrition 0.000 description 7
- 230000001404 mediated effect Effects 0.000 description 7
- 230000032258 transport Effects 0.000 description 7
- 102220518383 Casein kinase I isoform gamma-2_R7A_mutation Human genes 0.000 description 6
- 101000579484 Homo sapiens Period circadian protein homolog 1 Proteins 0.000 description 6
- 108010074328 Interferon-gamma Proteins 0.000 description 6
- 238000003556 assay Methods 0.000 description 6
- 239000011575 calcium Substances 0.000 description 6
- -1 fluorescein isocyanate Chemical class 0.000 description 6
- 230000006911 nucleation Effects 0.000 description 6
- 238000010899 nucleation Methods 0.000 description 6
- 238000010186 staining Methods 0.000 description 6
- 230000005945 translocation Effects 0.000 description 6
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 6
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 5
- 108090000695 Cytokines Proteins 0.000 description 5
- 102000004127 Cytokines Human genes 0.000 description 5
- 230000004568 DNA-binding Effects 0.000 description 5
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 5
- 108010052285 Membrane Proteins Proteins 0.000 description 5
- 108091005804 Peptidases Proteins 0.000 description 5
- 239000004365 Protease Substances 0.000 description 5
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 5
- 108010007945 Smad Proteins Proteins 0.000 description 5
- 102000007374 Smad Proteins Human genes 0.000 description 5
- 230000004913 activation Effects 0.000 description 5
- 229910052791 calcium Inorganic materials 0.000 description 5
- 239000012634 fragment Substances 0.000 description 5
- 239000000203 mixture Substances 0.000 description 5
- 239000013642 negative control Substances 0.000 description 5
- 229940002612 prodrug Drugs 0.000 description 5
- 239000000651 prodrug Substances 0.000 description 5
- 102000005912 ran GTP Binding Protein Human genes 0.000 description 5
- 108010005597 ran GTP Binding Protein Proteins 0.000 description 5
- 230000004960 subcellular localization Effects 0.000 description 5
- 238000006467 substitution reaction Methods 0.000 description 5
- 238000001890 transfection Methods 0.000 description 5
- 102000049773 5-HT2A Serotonin Receptor Human genes 0.000 description 4
- 108010072564 5-HT2A Serotonin Receptor Proteins 0.000 description 4
- OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 4
- 108700031308 Antennapedia Homeodomain Proteins 0.000 description 4
- 101000897691 Homo sapiens Helix-loop-helix protein 1 Proteins 0.000 description 4
- 101000897700 Homo sapiens Helix-loop-helix protein 2 Proteins 0.000 description 4
- 101001126582 Homo sapiens Post-GPI attachment to proteins factor 3 Proteins 0.000 description 4
- 241000725303 Human immunodeficiency virus Species 0.000 description 4
- 102100037850 Interferon gamma Human genes 0.000 description 4
- 102000018697 Membrane Proteins Human genes 0.000 description 4
- 102100028293 Period circadian protein homolog 1 Human genes 0.000 description 4
- 241000700159 Rattus Species 0.000 description 4
- 108010075890 beta Karyopherins Proteins 0.000 description 4
- 102000012012 beta Karyopherins Human genes 0.000 description 4
- 230000030570 cellular localization Effects 0.000 description 4
- 230000008859 change Effects 0.000 description 4
- 230000007711 cytoplasmic localization Effects 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 230000004044 response Effects 0.000 description 4
- 229940076279 serotonin Drugs 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 238000010361 transduction Methods 0.000 description 4
- 230000026683 transduction Effects 0.000 description 4
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 3
- 102100024977 Glutamine-tRNA ligase Human genes 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- 101001001473 Homo sapiens Importin subunit alpha-4 Proteins 0.000 description 3
- 101000599940 Homo sapiens Interferon gamma Proteins 0.000 description 3
- 101000668416 Homo sapiens Regulator of chromosome condensation Proteins 0.000 description 3
- 102000003839 Human Proteins Human genes 0.000 description 3
- 108090000144 Human Proteins Proteins 0.000 description 3
- 102100036187 Importin subunit alpha-4 Human genes 0.000 description 3
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 3
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 3
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 3
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 3
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 description 3
- 102000002274 Matrix Metalloproteinases Human genes 0.000 description 3
- 108010000684 Matrix Metalloproteinases Proteins 0.000 description 3
- 102000003945 NF-kappa B Human genes 0.000 description 3
- 108010057466 NF-kappa B Proteins 0.000 description 3
- 108010077850 Nuclear Localization Signals Proteins 0.000 description 3
- 108010079246 OMPA outer membrane proteins Proteins 0.000 description 3
- 108091034117 Oligonucleotide Proteins 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 3
- 102100039977 Regulator of chromosome condensation Human genes 0.000 description 3
- 108010090804 Streptavidin Proteins 0.000 description 3
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 3
- 238000012867 alanine scanning Methods 0.000 description 3
- 108010077099 alpha Karyopherins Proteins 0.000 description 3
- 102000009899 alpha Karyopherins Human genes 0.000 description 3
- 238000013459 approach Methods 0.000 description 3
- WQZGKKKJIJFFOK-FPRJBGLDSA-N beta-D-galactose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-FPRJBGLDSA-N 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 210000000172 cytosol Anatomy 0.000 description 3
- 229940127089 cytotoxic agent Drugs 0.000 description 3
- 239000002254 cytotoxic agent Substances 0.000 description 3
- 231100000599 cytotoxic agent Toxicity 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 235000013922 glutamic acid Nutrition 0.000 description 3
- 239000004220 glutamic acid Substances 0.000 description 3
- 108010051239 glutaminyl-tRNA synthetase Proteins 0.000 description 3
- 230000002209 hydrophobic effect Effects 0.000 description 3
- 239000003446 ligand Substances 0.000 description 3
- 229920002521 macromolecule Polymers 0.000 description 3
- 210000002569 neuron Anatomy 0.000 description 3
- 210000003463 organelle Anatomy 0.000 description 3
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 3
- 230000026731 phosphorylation Effects 0.000 description 3
- 238000006366 phosphorylation reaction Methods 0.000 description 3
- 150000003212 purines Chemical class 0.000 description 3
- 238000010188 recombinant method Methods 0.000 description 3
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 238000002560 therapeutic procedure Methods 0.000 description 3
- 239000003053 toxin Substances 0.000 description 3
- 231100000765 toxin Toxicity 0.000 description 3
- 108700012359 toxins Proteins 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- 102100027833 14-3-3 protein sigma Human genes 0.000 description 2
- 108010011619 6-Phytase Proteins 0.000 description 2
- KDCGOANMDULRCW-UHFFFAOYSA-N 7H-purine Chemical compound N1=CNC2=NC=NC2=C1 KDCGOANMDULRCW-UHFFFAOYSA-N 0.000 description 2
- 241000228212 Aspergillus Species 0.000 description 2
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 108010078791 Carrier Proteins Proteins 0.000 description 2
- 108050006400 Cyclin Proteins 0.000 description 2
- 102000016736 Cyclin Human genes 0.000 description 2
- QOSSAOTZNIDXMA-UHFFFAOYSA-N Dicylcohexylcarbodiimide Chemical compound C1CCCCC1N=C=NC1CCCCC1 QOSSAOTZNIDXMA-UHFFFAOYSA-N 0.000 description 2
- 102000016607 Diphtheria Toxin Human genes 0.000 description 2
- 108010053187 Diphtheria Toxin Proteins 0.000 description 2
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 2
- 101100322030 Drosophila melanogaster Abl gene Proteins 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 108050007372 Fibroblast Growth Factor Proteins 0.000 description 2
- 102100023374 Forkhead box protein M1 Human genes 0.000 description 2
- 102100021888 Helix-loop-helix protein 1 Human genes 0.000 description 2
- 102100021889 Helix-loop-helix protein 2 Human genes 0.000 description 2
- 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 2
- 101000716088 Homo sapiens Cyclin-L1 Proteins 0.000 description 2
- 101000907578 Homo sapiens Forkhead box protein M1 Proteins 0.000 description 2
- 101001001462 Homo sapiens Importin subunit alpha-5 Proteins 0.000 description 2
- 101001073216 Homo sapiens Period circadian protein homolog 2 Proteins 0.000 description 2
- 101100107350 Homo sapiens SFN gene Proteins 0.000 description 2
- 101000897669 Homo sapiens Small RNA 2'-O-methyltransferase Proteins 0.000 description 2
- 101000837849 Homo sapiens Trans-Golgi network integral membrane protein 2 Proteins 0.000 description 2
- 241000713772 Human immunodeficiency virus 1 Species 0.000 description 2
- 102100035692 Importin subunit alpha-1 Human genes 0.000 description 2
- 102100036186 Importin subunit alpha-5 Human genes 0.000 description 2
- 101710118220 Importin subunit alpha-5 Proteins 0.000 description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- 108090000143 Mouse Proteins Proteins 0.000 description 2
- 101001044384 Mus musculus Interferon gamma Proteins 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 108010052419 NF-KappaB Inhibitor alpha Proteins 0.000 description 2
- 102100039337 NF-kappa-B inhibitor alpha Human genes 0.000 description 2
- 101150097297 Nedd4 gene Proteins 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 102000007079 Peptide Fragments Human genes 0.000 description 2
- 108010033276 Peptide Fragments Proteins 0.000 description 2
- 102100035787 Period circadian protein homolog 2 Human genes 0.000 description 2
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 2
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- 102100028621 Trans-Golgi network integral membrane protein 2 Human genes 0.000 description 2
- 102000004887 Transforming Growth Factor beta Human genes 0.000 description 2
- 108090001012 Transforming Growth Factor beta Proteins 0.000 description 2
- 239000013504 Triton X-100 Substances 0.000 description 2
- 229920004890 Triton X-100 Polymers 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Chemical compound CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 230000001800 adrenalinergic effect Effects 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 230000033228 biological regulation Effects 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 230000008632 circadian clock Effects 0.000 description 2
- 238000010226 confocal imaging Methods 0.000 description 2
- 238000004624 confocal microscopy Methods 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 231100000673 dose–response relationship Toxicity 0.000 description 2
- 210000001951 dura mater Anatomy 0.000 description 2
- 239000002158 endotoxin Substances 0.000 description 2
- 239000012091 fetal bovine serum Substances 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 229920000669 heparin Polymers 0.000 description 2
- 229960002897 heparin Drugs 0.000 description 2
- 102000045697 human NHLH1 Human genes 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 210000001739 intranuclear inclusion body Anatomy 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- 230000007762 localization of cell Effects 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 230000005012 migration Effects 0.000 description 2
- 238000013508 migration Methods 0.000 description 2
- 238000005065 mining Methods 0.000 description 2
- 230000000394 mitotic effect Effects 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 230000025308 nuclear transport Effects 0.000 description 2
- 239000011574 phosphorus Substances 0.000 description 2
- 229910052698 phosphorus Inorganic materials 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 229940085127 phytase Drugs 0.000 description 2
- INAAIJLSXJJHOZ-UHFFFAOYSA-N pibenzimol Chemical compound C1CN(C)CCN1C1=CC=C(N=C(N2)C=3C=C4NC(=NC4=CC=3)C=3C=CC(O)=CC=3)C2=C1 INAAIJLSXJJHOZ-UHFFFAOYSA-N 0.000 description 2
- 229920001282 polysaccharide Polymers 0.000 description 2
- 239000005017 polysaccharide Substances 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000000069 prophylactic effect Effects 0.000 description 2
- 230000018883 protein targeting Effects 0.000 description 2
- 230000017854 proteolysis Effects 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 230000010837 receptor-mediated endocytosis Effects 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 230000019491 signal transduction Effects 0.000 description 2
- 230000011664 signaling Effects 0.000 description 2
- 150000003384 small molecules Chemical class 0.000 description 2
- 230000009870 specific binding Effects 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical group C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 102000027257 transmembrane receptors Human genes 0.000 description 2
- 108091008578 transmembrane receptors Proteins 0.000 description 2
- 125000000430 tryptophan group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C2=C([H])C([H])=C([H])C([H])=C12 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- WEZDRVHTDXTVLT-GJZGRUSLSA-N 2-[[(2s)-2-[[(2s)-2-[(2-aminoacetyl)amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]acetic acid Chemical compound OC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)CN)CC1=CC=CC=C1 WEZDRVHTDXTVLT-GJZGRUSLSA-N 0.000 description 1
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 1
- LPBHYOYZZIFCQT-UHFFFAOYSA-N 2-methylpropyl 2-(2-methylpropoxy)-2h-quinoline-1-carboxylate Chemical compound C1=CC=C2N(C(=O)OCC(C)C)C(OCC(C)C)C=CC2=C1 LPBHYOYZZIFCQT-UHFFFAOYSA-N 0.000 description 1
- ZZGXRPGQPAPARK-UWVGGRQHSA-N 3-[(5r,6r)-1-azabicyclo[3.2.1]octan-6-yl]-4-propylsulfanyl-1,2,5-thiadiazole Chemical compound C1([C@H]2CN3C[C@@]2(CCC3)[H])=NSN=C1SCCC ZZGXRPGQPAPARK-UWVGGRQHSA-N 0.000 description 1
- QRYXYRQPMWQIDM-UHFFFAOYSA-N 3-benzoyl-3-(2,5-dioxopyrrol-1-yl)-1-hydroxypyrrolidine-2,5-dione Chemical compound O=C1N(O)C(=O)CC1(C(=O)C=1C=CC=CC=1)N1C(=O)C=CC1=O QRYXYRQPMWQIDM-UHFFFAOYSA-N 0.000 description 1
- KKADPXVIOXHVKN-UHFFFAOYSA-N 4-hydroxyphenylpyruvic acid Chemical compound OC(=O)C(=O)CC1=CC=C(O)C=C1 KKADPXVIOXHVKN-UHFFFAOYSA-N 0.000 description 1
- 102100036321 5-hydroxytryptamine receptor 2A Human genes 0.000 description 1
- 101710138091 5-hydroxytryptamine receptor 2A Proteins 0.000 description 1
- 102000040125 5-hydroxytryptamine receptor family Human genes 0.000 description 1
- 108091032151 5-hydroxytryptamine receptor family Proteins 0.000 description 1
- 102100034540 Adenomatous polyposis coli protein Human genes 0.000 description 1
- 241000219194 Arabidopsis Species 0.000 description 1
- 101100004408 Arabidopsis thaliana BIG gene Proteins 0.000 description 1
- 241000384062 Armadillo Species 0.000 description 1
- 102000016904 Armadillo Domain Proteins Human genes 0.000 description 1
- 108010014223 Armadillo Domain Proteins Proteins 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 108010027344 Basic Helix-Loop-Helix Transcription Factors Proteins 0.000 description 1
- DFOCUWZXJBAUSQ-UHFFFAOYSA-N Berbamine Natural products O1C(C(=CC=2)O)=CC=2CC(C=23)N(C)CCC3=CC(OC)=C(OC)C=2OC(=CC=23)C(OC)=CC=2CCN(C)C3CC2=CC=C1C=C2 DFOCUWZXJBAUSQ-UHFFFAOYSA-N 0.000 description 1
- 101800001415 Bri23 peptide Proteins 0.000 description 1
- 102400000107 C-terminal peptide Human genes 0.000 description 1
- 101800000655 C-terminal peptide Proteins 0.000 description 1
- OBMZMSLWNNWEJA-XNCRXQDQSA-N C1=CC=2C(C[C@@H]3NC(=O)[C@@H](NC(=O)[C@H](NC(=O)N(CC#CCN(CCCC[C@H](NC(=O)[C@@H](CC4=CC=CC=C4)NC3=O)C(=O)N)CC=C)NC(=O)[C@@H](N)C)CC3=CNC4=C3C=CC=C4)C)=CNC=2C=C1 Chemical compound C1=CC=2C(C[C@@H]3NC(=O)[C@@H](NC(=O)[C@H](NC(=O)N(CC#CCN(CCCC[C@H](NC(=O)[C@@H](CC4=CC=CC=C4)NC3=O)C(=O)N)CC=C)NC(=O)[C@@H](N)C)CC3=CNC4=C3C=CC=C4)C)=CNC=2C=C1 OBMZMSLWNNWEJA-XNCRXQDQSA-N 0.000 description 1
- 101001007681 Candida albicans (strain WO-1) Kexin Proteins 0.000 description 1
- 208000005623 Carcinogenesis Diseases 0.000 description 1
- 102220518365 Casein kinase I isoform gamma-2_R12A_mutation Human genes 0.000 description 1
- 102000004225 Cathepsin B Human genes 0.000 description 1
- 108090000712 Cathepsin B Proteins 0.000 description 1
- 102000003902 Cathepsin C Human genes 0.000 description 1
- 108090000267 Cathepsin C Proteins 0.000 description 1
- 102000003908 Cathepsin D Human genes 0.000 description 1
- 108090000258 Cathepsin D Proteins 0.000 description 1
- 102220586060 Chemerin-like receptor 2_K11A_mutation Human genes 0.000 description 1
- 102220473072 Chemerin-like receptor 2_R14Q_mutation Human genes 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 102100036274 Cyclin-L1 Human genes 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 102000052510 DNA-Binding Proteins Human genes 0.000 description 1
- 108700020911 DNA-Binding Proteins Proteins 0.000 description 1
- 244000000626 Daucus carota Species 0.000 description 1
- 235000002767 Daucus carota Nutrition 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 108700013908 Drosophila PER Proteins 0.000 description 1
- 101100485279 Drosophila melanogaster emb gene Proteins 0.000 description 1
- 101100378121 Drosophila melanogaster nAChRalpha1 gene Proteins 0.000 description 1
- GKQLYSROISKDLL-UHFFFAOYSA-N EEDQ Chemical compound C1=CC=C2N(C(=O)OCC)C(OCC)C=CC2=C1 GKQLYSROISKDLL-UHFFFAOYSA-N 0.000 description 1
- 108010059378 Endopeptidases Proteins 0.000 description 1
- 102000005593 Endopeptidases Human genes 0.000 description 1
- 102100029727 Enteropeptidase Human genes 0.000 description 1
- 108010013369 Enteropeptidase Proteins 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 102100029095 Exportin-1 Human genes 0.000 description 1
- 101710129170 Extensin Proteins 0.000 description 1
- 102000018233 Fibroblast Growth Factor Human genes 0.000 description 1
- 108091006027 G proteins Proteins 0.000 description 1
- 102000030782 GTP binding Human genes 0.000 description 1
- 108091000058 GTP-Binding Proteins 0.000 description 1
- 241000276438 Gadus morhua Species 0.000 description 1
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 1
- 102100022624 Glucoamylase Human genes 0.000 description 1
- DKEXFJVMVGETOO-LURJTMIESA-N Gly-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)CN DKEXFJVMVGETOO-LURJTMIESA-N 0.000 description 1
- 108010009504 Gly-Phe-Leu-Gly Proteins 0.000 description 1
- 102100035716 Glycophorin-A Human genes 0.000 description 1
- 108091005250 Glycophorins Proteins 0.000 description 1
- 101710149234 Helix-loop-helix protein 1 Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 108010048671 Homeodomain Proteins Proteins 0.000 description 1
- 102000009331 Homeodomain Proteins Human genes 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000924577 Homo sapiens Adenomatous polyposis coli protein Proteins 0.000 description 1
- 101001081126 Homo sapiens Homeobox protein engrailed-1 Proteins 0.000 description 1
- 101001124017 Homo sapiens Nuclear transport factor 2 Proteins 0.000 description 1
- 101000601274 Homo sapiens Period circadian protein homolog 3 Proteins 0.000 description 1
- 108010070875 Human Immunodeficiency Virus tat Gene Products Proteins 0.000 description 1
- 206010021143 Hypoxia Diseases 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 102100020881 Interleukin-1 alpha Human genes 0.000 description 1
- 108010082786 Interleukin-1alpha Proteins 0.000 description 1
- 230000004163 JAK-STAT signaling pathway Effects 0.000 description 1
- 108010062228 Karyopherins Proteins 0.000 description 1
- 102000011781 Karyopherins Human genes 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 1
- 229930182816 L-glutamine Natural products 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 101710128836 Large T antigen Proteins 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- 241000219745 Lupinus Species 0.000 description 1
- 244000045959 Lupinus luteus Species 0.000 description 1
- 235000010648 Lupinus luteus Nutrition 0.000 description 1
- 102100034184 Macrophage scavenger receptor types I and II Human genes 0.000 description 1
- 101710134306 Macrophage scavenger receptor types I and II Proteins 0.000 description 1
- 102000003939 Membrane transport proteins Human genes 0.000 description 1
- 108090000301 Membrane transport proteins Proteins 0.000 description 1
- 108060004795 Methyltransferase Proteins 0.000 description 1
- 108010006519 Molecular Chaperones Proteins 0.000 description 1
- 102000005431 Molecular Chaperones Human genes 0.000 description 1
- 101001128134 Mus musculus NACHT, LRR and PYD domains-containing protein 5 Proteins 0.000 description 1
- 101100082892 Mus musculus Per1 gene Proteins 0.000 description 1
- NQTADLQHYWFPDB-UHFFFAOYSA-N N-Hydroxysuccinimide Chemical compound ON1C(=O)CCC1=O NQTADLQHYWFPDB-UHFFFAOYSA-N 0.000 description 1
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
- 108010018525 NFATC Transcription Factors Proteins 0.000 description 1
- 102000002673 NFATC Transcription Factors Human genes 0.000 description 1
- 102100028418 Nuclear transport factor 2 Human genes 0.000 description 1
- 102000002488 Nucleoplasmin Human genes 0.000 description 1
- 108700020796 Oncogene Proteins 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 102100037630 Period circadian protein homolog 3 Human genes 0.000 description 1
- 101710092224 Phosphate propanoyltransferase Proteins 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 108010071563 Proto-Oncogene Proteins c-fos Proteins 0.000 description 1
- 102000007568 Proto-Oncogene Proteins c-fos Human genes 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 101100485284 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) CRM1 gene Proteins 0.000 description 1
- 102000049939 Smad3 Human genes 0.000 description 1
- 108700031297 Smad3 Proteins 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 102000005610 Thyroid Hormone Receptors alpha Human genes 0.000 description 1
- 108010045070 Thyroid Hormone Receptors alpha Proteins 0.000 description 1
- AUYYCJSJGJYCDS-LBPRGKRZSA-N Thyrolar Chemical class IC1=CC(C[C@H](N)C(O)=O)=CC(I)=C1OC1=CC=C(O)C(I)=C1 AUYYCJSJGJYCDS-LBPRGKRZSA-N 0.000 description 1
- 102000014172 Transforming Growth Factor-beta Type I Receptor Human genes 0.000 description 1
- 108010011702 Transforming Growth Factor-beta Type I Receptor Proteins 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 102100022596 Tyrosine-protein kinase ABL1 Human genes 0.000 description 1
- 101710098624 Tyrosine-protein kinase ABL1 Proteins 0.000 description 1
- ASCBRLGHWVZBMG-UHFFFAOYSA-N UNPD71813 Natural products COC=1C(=O)C=2C(O)=C(OC)C(OC)=CC=2OC=1C(C=C1)=CC=C1OC1OC(CO)C(O)C(O)C1O ASCBRLGHWVZBMG-UHFFFAOYSA-N 0.000 description 1
- 108010083111 Ubiquitin-Protein Ligases Proteins 0.000 description 1
- 102100020696 Ubiquitin-conjugating enzyme E2 K Human genes 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 101150094313 XPO1 gene 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
- 230000002159 abnormal effect Effects 0.000 description 1
- 230000035508 accumulation Effects 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 230000009056 active transport Effects 0.000 description 1
- 208000009956 adenocarcinoma Diseases 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 239000000074 antisense oligonucleotide Substances 0.000 description 1
- 238000012230 antisense oligonucleotides Methods 0.000 description 1
- 230000006907 apoptotic process Effects 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 125000003236 benzoyl group Chemical group [H]C1=C([H])C([H])=C(C([H])=C1[H])C(*)=O 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 238000003766 bioinformatics method Methods 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000007321 biological mechanism Effects 0.000 description 1
- 230000031018 biological processes and functions Effects 0.000 description 1
- 108091006004 biotinylated proteins Proteins 0.000 description 1
- 210000001185 bone marrow Anatomy 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 125000004063 butyryl group Chemical group O=C([*])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 230000028956 calcium-mediated signaling Effects 0.000 description 1
- 230000036952 cancer formation Effects 0.000 description 1
- 231100000504 carcinogenesis Toxicity 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 239000013553 cell monolayer Substances 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 210000000782 cerebellar granule cell Anatomy 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- BHONFOAYRQZPKZ-LCLOTLQISA-N chembl269478 Chemical compound C([C@H](NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](N)CCCNC(N)=N)[C@@H](C)CC)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(O)=O)C1=CC=CC=C1 BHONFOAYRQZPKZ-LCLOTLQISA-N 0.000 description 1
- 238000010382 chemical cross-linking Methods 0.000 description 1
- 230000002060 circadian Effects 0.000 description 1
- 230000027288 circadian rhythm Effects 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000001218 confocal laser scanning microscopy Methods 0.000 description 1
- 210000003618 cortical neuron Anatomy 0.000 description 1
- 230000001351 cycling effect Effects 0.000 description 1
- 230000002380 cytological effect Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
- 230000030609 dephosphorylation Effects 0.000 description 1
- 238000006209 dephosphorylation reaction Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 238000002224 dissection Methods 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 230000003828 downregulation Effects 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 230000001614 effect on membrane Effects 0.000 description 1
- 235000013601 eggs Nutrition 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000007515 enzymatic degradation Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 125000003754 ethoxycarbonyl group Chemical group C(=O)(OCC)* 0.000 description 1
- 108700002148 exportin 1 Proteins 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 229940126864 fibroblast growth factor Drugs 0.000 description 1
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
- 238000000799 fluorescence microscopy Methods 0.000 description 1
- 238000002825 functional assay Methods 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- YMAWOPBAYDPSLA-UHFFFAOYSA-N glycylglycine Chemical compound [NH3+]CC(=O)NCC([O-])=O YMAWOPBAYDPSLA-UHFFFAOYSA-N 0.000 description 1
- 108010050848 glycylleucine Proteins 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 150000002411 histidines Chemical group 0.000 description 1
- 102000056963 human EN1 Human genes 0.000 description 1
- 102000045698 human NHLH2 Human genes 0.000 description 1
- 102000044565 human PER1 Human genes 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 230000007954 hypoxia Effects 0.000 description 1
- 210000001822 immobilized cell Anatomy 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 238000010166 immunofluorescence Methods 0.000 description 1
- 230000002055 immunohistochemical effect Effects 0.000 description 1
- 238000000126 in silico method Methods 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 229910052816 inorganic phosphate Inorganic materials 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 229960003130 interferon gamma Drugs 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 239000012948 isocyanate Substances 0.000 description 1
- 210000003292 kidney cell Anatomy 0.000 description 1
- 150000002605 large molecules Chemical class 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 230000002132 lysosomal effect Effects 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 230000034217 membrane fusion Effects 0.000 description 1
- 230000009061 membrane transport Effects 0.000 description 1
- 125000001160 methoxycarbonyl group Chemical group [H]C([H])([H])OC(*)=O 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 239000003068 molecular probe Substances 0.000 description 1
- 210000004897 n-terminal region Anatomy 0.000 description 1
- 210000000653 nervous system Anatomy 0.000 description 1
- 230000007472 neurodevelopment Effects 0.000 description 1
- 230000004031 neuronal differentiation Effects 0.000 description 1
- 238000007797 non-conventional method Methods 0.000 description 1
- 230000004942 nuclear accumulation Effects 0.000 description 1
- 210000000633 nuclear envelope Anatomy 0.000 description 1
- 230000030147 nuclear export Effects 0.000 description 1
- 238000012758 nuclear staining Methods 0.000 description 1
- 230000000269 nucleophilic effect Effects 0.000 description 1
- 108060005597 nucleoplasmin Proteins 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 150000002894 organic compounds Chemical class 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 108010034040 pendulin Proteins 0.000 description 1
- XDKNUCQYHGFFFE-UHFFFAOYSA-N pendulin Natural products COc1cc2ccc3c(OC)c(OC)c(OC)cc3c2c(OC)c1O XDKNUCQYHGFFFE-UHFFFAOYSA-N 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 230000035699 permeability Effects 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 230000008635 plant growth Effects 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 230000034190 positive regulation of NF-kappaB transcription factor activity Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- XJMOSONTPMZWPB-UHFFFAOYSA-M propidium iodide Chemical compound [I-].[I-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CCC[N+](C)(CC)CC)=C1C1=CC=CC=C1 XJMOSONTPMZWPB-UHFFFAOYSA-M 0.000 description 1
- 238000002731 protein assay Methods 0.000 description 1
- 108020001580 protein domains Proteins 0.000 description 1
- 230000026447 protein localization Effects 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 230000021907 regulation of circadian rhythm Effects 0.000 description 1
- 230000014493 regulation of gene expression Effects 0.000 description 1
- 230000004314 regulation of intracellular transport Effects 0.000 description 1
- 230000008844 regulatory mechanism Effects 0.000 description 1
- 210000003660 reticulum Anatomy 0.000 description 1
- 102220294053 rs751463286 Human genes 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 230000000862 serotonergic effect Effects 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000007447 staining method Methods 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000001502 supplementing effect Effects 0.000 description 1
- 231100000057 systemic toxicity Toxicity 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 210000001685 thyroid gland Anatomy 0.000 description 1
- 239000005495 thyroid hormone Substances 0.000 description 1
- 229940036555 thyroid hormone Drugs 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 238000003146 transient transfection Methods 0.000 description 1
- 230000007723 transport mechanism Effects 0.000 description 1
- 108010060175 trypsinogen activation peptide Proteins 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 230000006663 ubiquitin-proteasome pathway Effects 0.000 description 1
- 241001529453 unidentified herpesvirus Species 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 210000003934 vacuole Anatomy 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 230000029812 viral genome replication Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K19/00—Hybrid peptides, i.e. peptides covalently bound to nucleic acids, or non-covalently bound protein-protein complexes
-
- 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
- C07K14/4702—Regulators; Modulating activity
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/03—Fusion polypeptide containing a localisation/targetting motif containing a transmembrane segment
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/09—Fusion polypeptide containing a localisation/targetting motif containing a nuclear localisation signal
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/10—Fusion polypeptide containing a localisation/targetting motif containing a tag for extracellular membrane crossing, e.g. TAT or VP22
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/40—Fusion polypeptide containing a tag for immunodetection, or an epitope for immunisation
- C07K2319/43—Fusion polypeptide containing a tag for immunodetection, or an epitope for immunisation containing a FLAG-tag
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—Fusion polypeptide containing protease site
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/60—Fusion polypeptide containing spectroscopic/fluorescent detection, e.g. green fluorescent protein [GFP]
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Zoology (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biophysics (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Wood Science & Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Microbiology (AREA)
- Toxicology (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- General Chemical & Material Sciences (AREA)
- Public Health (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Abstract
Description
명칭 | 아미노산 서열 | 전달펩타이드1 | 융합 단백질 상에서의핵 국재화2 |
hPER1 | GRRHHCRSKAKRSRHH | + | + |
Flag-hPER1 | GMDYKDDDDKGSRRHHCRSKAKRSHH | + | nd |
Flag-TAT | GMDYKDDDDKGYGRKKKRRQRRR | + | + |
Flag | GMDYKDDDDKGMDYKDDDDK | - | - |
안테나페디아 | GRQIKIWFQNRRMKWKK | + | nd |
9 아르기닌 | GRRRRRRRRR | + | nd |
9 라이신 | GKKKKKKKKK | + | nd |
9 히스티딘 | GHHHHHHHHH | - | nd |
NLS: | |||
SV40 | GDPKKKRKV | - | + |
hPER2 | GKKTGKNRKLKSKRVKPRD | - | + |
hPER3 | GRKGKHKRKKLP | + | + |
갑상선 A-1 | GKRVAKRKLIEQNRERRR | + | + |
HME-1 | GRKLKKKKNEKEDKRPRT | + | + |
ABL-1 | GKKTNLFSALIKKKKTA | + | + |
뉴클레오플라스민 X | GRRERNKMAAAKCRNRRR | + | + |
C-FOS | GRRERNKMAAAKCRNRRR | - | + |
GCN-4 | GKRARNTEAARRSRARKL | + | + |
[R/H/K]- [R/H/K]- [R/H/K]- [R/H/K] | |||
HEN1/NSLC1 | GRRRRATAKYRTAH | + | + |
HEN2/NSLC2 | GKRRRRATAKYRSAH | + | + |
HNF3 | GRRRRKRLSHRT | + | + |
cAMP 의존성 TF | GRRRRRERNK | + | + |
사이클린 L ania-6a | GKHRHERGHHRDRRER | - | + |
베타 Zip TF | GKKKRKLSNRESAKRSR | - | + |
GFP | - | nd | - |
Fn 1: 선택된 MPP에 대해 제시된 결과, 도 5 참조Fn 2: 선택된 MPP에 대해 제시된 결과, 도 5 참조 |
명칭 | hPER1-PTD 알라닌 치환 | 전달 펩타이드 |
hPER1-PTD | S R R H H C R S K A K R S R H H | + |
R2A | SAR H H C R S K A K R S R H H | + |
R3A | S RAH H C R S K A K R S R H H | + |
H4A | S R RAH C R S K A K R S R H H | + |
H5A | S R R HAC R S K A K R S R H H | + |
C6A | S R R H HAR S K A K R S R H H | + |
R7A | S R R H H CAS K A K R S R H H | - |
S8A | S R R H H C RAK A K R S R H H | + |
K9A | S R R H H C R SAA K R S R H H | + |
K11A | S R R H H C R S K AAR S R H H | + |
R12A | S R R H H C R S K A KAS R H H | + |
S13A | S R R H H C R S K A K RAR H H | + |
R14A | S R R H H C R S K A K R S A H H | + |
hPER1-PTD13 | R R H H C R S K A K R S R | + |
hPER1-대조군(484-503) | QELSEQIHRLLLQPV | - |
Claims (21)
- 관심 화합물에 결합되어 있는 막 관통 펩타이드를 포함하는, 관심 화합물을 세포내로 전달하기 위한 융합 단백질.
- 제1항에 있어서, 막 관통 펩타이드가 핵 국재화 서열로부터 유래되거나, 포유동물 또는 효모 단백질의 핵 국재화 서열과 중복되거나, 서열 -(X-X-X-X)n-(여기서, n은 1 내지 7의 정수이고, X는 매회 아르기닌, 히스티딘 및 라이신으로 이루어진 그룹으로부터 독립적으로 선택된다)을 포함하는 융합 단백질.
- 제2항에 있어서, 핵 국재화 서열이 핵 단백질 또는 전사 인자로부터 유래되는 융합 단백질.
- 제3항에 있어서, 전사 인자가 Period 단백질인 융합 단백질.
- 제4항에 있어서, Period 단백질이 사람 Period 단백질인 융합 단백질.
- 제5항에 있어서, 포유동물 Period 단백질이 사람 Period1 단백질인 융합 단백질.
- 제2항에 있어서, 막 관통 펩타이드가 서열 -(X-X-X-X)n-(여기서, n은 1 내지 7의 정수이고, X는 매회 아르기닌, 히스티딘 및 라이신으로 이루어진 그룹으로부터 독립적으로 선택된다)을 포함하는 융합 단백질.
- 제7항에 있어서, n이 정수 1 내지 4인 융합 단백질.
- 제8항에 있어서, n이 정수 1 또는 2인 융합 단백질.
- 제1항에 있어서, 관심 화합물이 펩타이드, 단백질, 화학적 실체, 핵산 또는 이의 모든 변형된 형태인 융합 단백질.
- 세포를 제1항에 따르는 융합 단백질과 접촉시킴을 포함하여, 관심 화합물을 세포내로 전달하는 방법.
- 배양된 세포를 제1항에 따르는 융합 단백질과 접촉시킴을 포함하여, 관심 화합물을 시험관내에서 세포내로 전달하는 방법.
- 세포를 제1항에 따르는 융합 단백질과 접촉시키고, 당해 세포를 환자의 신체에 도입함을 포함하여, 관심 화합물을 생체외에서 세포내로 전달하는 방법.
- 제1항에 따르는 융합 단백질을 환자에게 투여함을 포함하여, 관심 화합물을 생체내에서 세포내로 전달하는 방법.
- 서열 -(X-X-X-X)n-(여기서, n은 1 내지 7의 정수이고, X는 매회 아르기닌, 히스티딘 및 라이신으로 이루어진 그룹으로부터 독립적으로 선택된다)을 검출가능한 단백질과 함께 포함하는 결합 펩타이드를 생성시키고, 당해 결합 펩타이드를 세포에 외인적으로 첨가하고, 당해 결합된 펩타이드가 세포의 세포질 및/또는 핵내에 위치하는지의 여부를 측정함으로써, 서열 -(X-X-X-X)n-(여기서, n은 1 내지 7의 정수이고, X는 매회 아르기닌, 히스티딘 및 라이신으로 이루어진 그룹으로부터 독립적으로 선택된다)을 포함하는 막 관통 펩타이드를 동정하는 방법.
- 핵 국재화 서열의 부분 또는 전부를 검출가능한 단백질과 함께 포함하는 결합 펩타이드를 생성시키고, 당해 결합 펩타이드를 세포에 외인적으로 첨가하고, 당해 결합된 펩타이드가 세포의 세포질 및/또는 핵내에 위치하는지의 여부를 측정함으로써, 포유동물 또는 효모 단백질의 핵 국재화 서열로부터 유래되거나 이와 중복되는 서열을 포함하는 막 관통 펩타이드를 동정하는 방법.
- 서열 -(X-X-X-X)n-(여기서, n은 1 내지 7의 정수이고, X는 매회 아르기닌, 히스티딘 및 라이신으로 이루어진 그룹으로부터 독립적으로 선택된다)을 포함하는 막 관통 펩타이드를 포함하는 제1항에 따르는 융합 단백질을 세포에 투여함을 포함하여, 관심 화합물을 세포내로 전달하는 방법.
- 서열 -(X-X-X-X)n-(여기서, n은 1 내지 7의 정수이고, X는 매회 아르기닌, 히스티딘 및 라이신으로 이루어진 그룹으로부터 독립적으로 선택된다)을 포함하는 막 관통 펩타이드 및 관심 화합물을 포함하는, 관심 화합물을 세포내로 전달하기 위한 융합 단백질.
- 제18항에 있어서, 관심 화합물이 막 관통 펩타이드에 화학적으로 직접적으로 또는 링커에 의해 결합되어 있는 융합 단백질.
- 제19항에 있어서, 링커가 아미노산 링커 또는 폴리펩타이드 링커인 융합 단백질.
- 제18항에 있어서, 막 관통 단백질이 재조합 기술, 화학적 합성 또는 전구체 단백질의 분해에 의해 제조되는 융합 단백질.
Applications Claiming Priority (5)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US22764700P | 2000-08-25 | 2000-08-25 | |
US60/227,647 | 2000-08-25 | ||
GB0103110.3 | 2001-02-07 | ||
GBGB0103110.3A GB0103110D0 (en) | 2000-08-25 | 2001-02-07 | A membrane penetrating peptide encoded by a nuclear localization sequence from human period 1 |
PCT/US2001/026421 WO2002018572A2 (en) | 2000-08-25 | 2001-08-23 | Membrane penetrating peptides and uses thereof |
Publications (2)
Publication Number | Publication Date |
---|---|
KR20030034156A true KR20030034156A (ko) | 2003-05-01 |
KR100810927B1 KR100810927B1 (ko) | 2008-03-10 |
Family
ID=22853919
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
KR1020037002754A KR100810927B1 (ko) | 2000-08-25 | 2001-08-23 | 막 관통 펩타이드 및 이의 용도 |
Country Status (10)
Country | Link |
---|---|
US (2) | US20030229202A1 (ko) |
JP (1) | JP4896356B2 (ko) |
KR (1) | KR100810927B1 (ko) |
AR (1) | AR033834A1 (ko) |
BR (1) | BRPI0113477B8 (ko) |
DE (1) | DE60133585T2 (ko) |
GB (1) | GB0103110D0 (ko) |
IL (1) | IL154589A (ko) |
TW (1) | TWI317737B (ko) |
ZA (1) | ZA200301476B (ko) |
Families Citing this family (44)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US8128922B2 (en) * | 1999-10-20 | 2012-03-06 | Johns Hopkins University | Superior molecular vaccine linking the translocation domain of a bacterial toxin to an antigen |
KR20030062788A (ko) * | 2002-01-19 | 2003-07-28 | 포휴먼텍(주) | 생체분자 전달 펩타이드 mph1-btm 및 이것을포함하는 생명공학제품 |
WO2003086273A2 (en) * | 2002-04-08 | 2003-10-23 | Yissum Research Development Company Of The Hebrew University Of Jerusalem | Histone conjugates and uses thereof |
WO2004098526A2 (en) | 2003-05-05 | 2004-11-18 | Johns Hopkins University | Anti-cancer dna vaccine employing plasmids encoding signal sequence, mutant oncoprotein antigen, and heat shock protein |
EP1631306A4 (en) * | 2003-05-19 | 2009-08-12 | Univ Columbia | COMPOSITIONS AND METHODS OF TREATING AND PREVENTING HEART TISSUE DEGENERATION AND THEIR USE |
AU2004317501B2 (en) * | 2004-04-13 | 2011-09-01 | Emory University | Intracellular delivery of osteoinductive proteins and peptides |
CA2660661A1 (en) * | 2005-09-26 | 2007-04-05 | The Trustees Of Columbia University In The City Of New York | Side population cells in cardiac repair |
DE602006016468D1 (de) * | 2005-11-04 | 2010-10-07 | Forhumantech Co Ltd | Verfahren zur abgabe von fusionspolypeptid in eine zelle |
CN101490080A (zh) * | 2006-07-24 | 2009-07-22 | 为人技术株式会社 | 用于缓解和治疗缺血性病症的药物组合物及其输送方法 |
KR100843634B1 (ko) * | 2006-08-03 | 2008-07-03 | 연세대학교 산학협력단 | 세포막투과 전달 펩타이드 및 이를 포함하는 생물제제 |
EP2057195A4 (en) * | 2006-08-29 | 2010-05-12 | Forhumantech Co Ltd | PHARMACEUTICAL COMPOSITION FOR THE SUPPRESSION OF APOPTOSIS AND METHOD OF ADMINISTERING THE SAME |
US7981446B2 (en) * | 2007-11-26 | 2011-07-19 | Forhumantech. Co., Ltd. | Pharmaceutical compositions and methods for delivering nucleic acids into cells |
US20100297758A1 (en) * | 2008-01-25 | 2010-11-25 | Toagosei Co., Ltd | Artificial peptide and use thereof |
ES2951646T3 (es) * | 2008-02-21 | 2023-10-24 | Burnham Institute For Medical Res | Métodos y composiciones relacionados con péptidos y proteínas con elementos C-terminales |
JP5709013B2 (ja) | 2009-04-10 | 2015-04-30 | 東亞合成株式会社 | 神経分化誘導ペプチド及びその利用 |
WO2010129033A2 (en) * | 2009-04-29 | 2010-11-11 | Calmune Corporation | Modified antibodies for passive immunotherapy |
WO2011005540A1 (en) | 2009-06-22 | 2011-01-13 | Burnham Institute For Medical Research | Methods and compositions using peptides and proteins with c-terminal elements |
WO2011013700A1 (ja) * | 2009-07-29 | 2011-02-03 | 東亞合成株式会社 | キャリアペプチドフラグメント及びその利用 |
JP5858283B2 (ja) * | 2009-07-29 | 2016-02-10 | 東亞合成株式会社 | キャリアペプチドフラグメント及びその利用 |
US20120149053A1 (en) * | 2009-07-29 | 2012-06-14 | Toagosei Co. Ltd. | Carrier peptide fragment and use thereof |
WO2011052679A1 (ja) | 2009-11-02 | 2011-05-05 | 東亞合成株式会社 | 細胞増殖促進ペプチド及びその利用 |
JP5808082B2 (ja) * | 2010-04-30 | 2015-11-10 | 株式会社Adeka | 細胞への水溶性高分子量物質の導入方法及び導入剤 |
US9394535B2 (en) | 2010-05-25 | 2016-07-19 | National University Corporation Kumamoto University | Plasma irradiation device for substance introduction and substance introduction method using plasma irradiation device |
WO2011152524A1 (ja) | 2010-06-04 | 2011-12-08 | 東亞合成株式会社 | 細胞増殖促進ペプチド及びその利用 |
US9238796B2 (en) | 2010-06-04 | 2016-01-19 | Toagosei Co. Ltd. | Cell growth-promoting peptide and use thereof |
JP6202707B2 (ja) * | 2011-10-13 | 2017-09-27 | 国立大学法人鳥取大学 | 新規細胞膜透過ペプチド |
JP6066222B2 (ja) | 2012-05-28 | 2017-01-25 | 東亞合成株式会社 | 抗菌ペプチド及びその利用 |
US20140072961A1 (en) * | 2012-07-11 | 2014-03-13 | University of Nevada, Las Vegas | Method of Genome Surgery with Paired, Permeant Endonuclease Excision |
US9480727B2 (en) | 2012-10-18 | 2016-11-01 | Toagosei Co. Ltd. | Synthetic peptide for inhibiting expression of type 2 TNF receptor and use thereof |
US20150353959A1 (en) * | 2013-01-18 | 2015-12-10 | Glycotope Gmbh | Peptides for enhancing protein expression |
SG10201811729PA (en) | 2013-12-12 | 2019-02-27 | Life Technologies Corp | Membrane-penetrating peptides to enhance transfection and compositions and methods for using same |
US10456475B2 (en) | 2015-02-03 | 2019-10-29 | Kennsaw State University Research and Service Foundation, Inc. | Cell penetrating protein adaptor molecules and their application in research and medicine |
CN107207627B (zh) | 2015-02-27 | 2022-05-24 | 学校法人常翔学园 | 具有膜透过性肽链的多糖衍生物 |
WO2016136708A1 (ja) | 2015-02-27 | 2016-09-01 | 学校法人常翔学園 | 膜透過性ペプチドを側鎖に有する高分子化合物 |
US10435446B2 (en) | 2015-06-03 | 2019-10-08 | Kennesaw State University Research and Service Foundation Inc. | Cell penetrating protein adaptor molecules and their application in research and medicine |
US10654894B2 (en) | 2016-02-03 | 2020-05-19 | Keenesaw State University Research And Service Foundation, Inc. | Methods for delivering cargo into a cell by using signal molecules as cell penetration agents |
SG11201912071QA (en) | 2017-06-22 | 2020-01-30 | Catalyst Biosciences Inc | Modified membrane type serine protease 1 (mtsp-1) polypeptides and methods of use |
WO2019157089A1 (en) * | 2018-02-06 | 2019-08-15 | University Of Maryland, Baltimore | Tlr9 inhibitors to suppress inflammatory response to pathogens |
US20220009968A1 (en) * | 2018-12-27 | 2022-01-13 | Industry-University Cooperation Foundation Hanyang University | Crispr-cas-based composition for gene correction |
KR102386498B1 (ko) * | 2018-12-27 | 2022-04-15 | 한양대학교 산학협력단 | Crispr-cas를 기반으로 하는 유전자 교정용 조성물 |
PE20211664A1 (es) | 2018-12-28 | 2021-08-26 | Catalyst Biosciences Inc | Polipeptidos de activador de plasminogeno, tipo urocinasa, modificados y metodos de uso |
US11613744B2 (en) | 2018-12-28 | 2023-03-28 | Vertex Pharmaceuticals Incorporated | Modified urokinase-type plasminogen activator polypeptides and methods of use |
CN110441156A (zh) * | 2019-07-20 | 2019-11-12 | 大连理工大学 | 一种基于土体稳定状态特性测量三轴试样膜嵌入量的方法 |
CN114716569B (zh) * | 2022-04-13 | 2023-11-10 | 浙江大学 | 一种携带目标蛋白自主进入真核细胞的重组蛋白、重组表达载体和重组菌及应用 |
Family Cites Families (30)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5804604A (en) | 1989-12-21 | 1998-09-08 | Biogen, Inc. | Tat-derived transport polypeptides and fusion proteins |
US6316003B1 (en) | 1989-12-21 | 2001-11-13 | Whitehead Institute For Biomedical Research | Tat-derived transport polypeptides |
US5652122A (en) | 1989-12-21 | 1997-07-29 | Frankel; Alan | Nucleic acids encoding and methods of making tat-derived transport polypeptides |
US6197925B1 (en) * | 1991-08-22 | 2001-03-06 | Sara Lee Corporation | NF-AT polypeptides and polynucleotides |
US5843643A (en) * | 1992-02-21 | 1998-12-01 | Ratner; Paul L. | Site-specific transfection of eukaryotic cells using polypeptide-linked recombinant nucleic acid |
US5766903A (en) | 1995-08-23 | 1998-06-16 | University Technology Corporation | Circular RNA and uses thereof |
DE69635383T2 (de) * | 1996-08-09 | 2006-08-03 | Dnavec Research Inc., Tsukuba | Phage verbunden an ein nukleus lokalisierungssignal |
US5877282A (en) | 1996-09-20 | 1999-03-02 | Bristol-Myers Squibb Company | Peptide inhibitors of nuclear protein translocation having nuclear localization sequences and methods of use thereof |
US5962415A (en) | 1996-09-20 | 1999-10-05 | Bristol-Myers Squibb Co. | Compositions comprising a peptide inhibitor of nuclear protein translocation and an immunosuppressant and methods of use thereof |
US5929042A (en) | 1997-03-03 | 1999-07-27 | The Trustees Of Columbia University In The City Of New York | Antisense compounds which prevent cell death and uses thereof |
WO1998049325A1 (en) | 1997-04-28 | 1998-11-05 | Mcgill University | Reporter fusion proteins, expression vectors and transfected cell lines thereof for the analysis of nuclear transport |
FR2767323B1 (fr) | 1997-08-12 | 2001-01-05 | Synt Em | Peptides lineaires derives de peptides antibiotiques, leur preparation et leur utilisation pour vectoriser des substances actives |
US6258774B1 (en) | 1998-03-19 | 2001-07-10 | University Of Medicine And Dentistry Of New Jersey | Carrier for in vivo delivery of a therapeutic agent |
SE9801055D0 (sv) * | 1998-03-25 | 1998-03-25 | Inst Of Molecul & Cell Biology | Use of growth hormone binding protein (GHBP) |
US6248558B1 (en) | 1998-03-31 | 2001-06-19 | Vanderbilt University | Sequence and method for genetic engineering of proteins with cell membrane translocating activity |
US6436628B1 (en) * | 1998-06-19 | 2002-08-20 | The Rockefeller University | Methods of identifying an agent which modulates period and doubletime protein interaction |
MXPA01000271A (es) | 1998-07-13 | 2002-10-17 | Expression Genetics Inc | Analogo de poliester de poli-lisina como un portador para el suministro de genes, soluble, biodegradable. |
US6246558B1 (en) * | 1998-08-24 | 2001-06-12 | Leviton Manufacturing Company | Circuit interrupting device with reverse wiring protection |
FR2786398B1 (fr) | 1998-11-30 | 2002-12-27 | Synt Em | Composition pharmaceutique anti-cancereuse et anti-chimioresistance comprenant un agent anticancereux et au moins un peptide |
FR2786397B1 (fr) | 1998-11-30 | 2003-01-10 | Synt Em | Vecteurs peptidiques de substances a travers la barriere hematoencephalique pour etre utilises dans le diagnostic ou la therapie d'une affection du snc |
CA2375450C (en) * | 1999-06-08 | 2009-04-28 | Aventis Pharmaceuticals Inc. | Screening methods for altering circadian rhythm proteins |
AU785007B2 (en) | 1999-11-24 | 2006-08-24 | Mcs Micro Carrier Systems Gmbh | Polypeptides comprising multimers of nuclear localization signals or of protein transduction domains and their use for transferring molecules into cells |
JP3908425B2 (ja) * | 1999-12-24 | 2007-04-25 | アルパイン株式会社 | ナビゲーション装置 |
AU7542301A (en) | 2000-06-09 | 2001-12-17 | Teni Boulikas | Encapsulation of plasmid DNA (lipogenes<sup>TM</sup>) and therapeutic agents with nuclear localization signal/fusogenic peptide conjugates into targeted liposome complexes |
JP3686961B2 (ja) * | 2000-08-04 | 2005-08-24 | シャープ株式会社 | 液晶表示装置及びそれを用いた電子機器 |
JP2002304088A (ja) * | 2001-04-09 | 2002-10-18 | Ricoh Co Ltd | 画像形成装置 |
EP1496927A4 (en) * | 2002-01-29 | 2007-09-12 | Aventis Pasteur | IMMUNOGENES TARGETS |
US6877262B2 (en) * | 2003-07-10 | 2005-04-12 | Ronald Bianco | Perpetual calendar |
DE10341112A1 (de) * | 2003-09-05 | 2005-03-31 | Li-Li Yehhsu | Behälter mit separaten Speicherkammern |
BRPI0418273A (pt) * | 2003-12-31 | 2007-05-02 | Sanofi Pasteur Inc | imunógenos alvejados |
-
2001
- 2001-02-07 GB GBGB0103110.3A patent/GB0103110D0/en not_active Ceased
- 2001-08-21 US US09/933,780 patent/US20030229202A1/en not_active Abandoned
- 2001-08-23 DE DE60133585T patent/DE60133585T2/de not_active Expired - Fee Related
- 2001-08-23 KR KR1020037002754A patent/KR100810927B1/ko active IP Right Grant
- 2001-08-23 JP JP2002524075A patent/JP4896356B2/ja not_active Expired - Lifetime
- 2001-08-23 BR BR0113477-9 patent/BRPI0113477B8/pt not_active IP Right Cessation
- 2001-08-24 AR ARP010104056A patent/AR033834A1/es not_active Application Discontinuation
- 2001-08-24 TW TW090120788A patent/TWI317737B/zh not_active IP Right Cessation
-
2003
- 2003-02-23 IL IL154589A patent/IL154589A/en active IP Right Grant
- 2003-02-24 ZA ZA200301476A patent/ZA200301476B/en unknown
-
2005
- 2005-10-17 US US11/251,734 patent/US7754678B2/en not_active Expired - Fee Related
Also Published As
Publication number | Publication date |
---|---|
IL154589A (en) | 2011-08-31 |
US20030229202A1 (en) | 2003-12-11 |
US7754678B2 (en) | 2010-07-13 |
AR033834A1 (es) | 2004-01-07 |
BRPI0113477B1 (pt) | 2019-10-22 |
DE60133585T2 (de) | 2009-06-04 |
ZA200301476B (en) | 2004-06-22 |
JP4896356B2 (ja) | 2012-03-14 |
TWI317737B (en) | 2009-12-01 |
US20060100134A1 (en) | 2006-05-11 |
KR100810927B1 (ko) | 2008-03-10 |
DE60133585D1 (de) | 2008-05-21 |
BRPI0113477B8 (pt) | 2021-05-25 |
JP2004512275A (ja) | 2004-04-22 |
BR0113477A (pt) | 2004-04-20 |
GB0103110D0 (en) | 2001-03-28 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
KR100810927B1 (ko) | 막 관통 펩타이드 및 이의 용도 | |
CA2420350C (en) | Membrane penetrating peptides and uses thereof | |
KR100608558B1 (ko) | 세포질 잔류성 세포막 투과 펩타이드 및 이의 용도 | |
Lindgren et al. | Cell-penetrating peptides | |
EP1966240B3 (en) | Lactoferrin peptides useful as cell-penetrating peptides | |
US20180372750A1 (en) | Antibody and antibody mimetic for visualization and ablation of endogenous proteins | |
EP2351775B1 (en) | Fusion protein comprising ubiquitin or ubiquitin-like protein, membrane translocation sequence and biologically active molecule and use thereof | |
CA3017717A1 (en) | Use of pten-long leader sequence for transmembrane delivery of molecules | |
KR20180118581A (ko) | 세포막 투과 펩티드 및 이를 포함하는 세포내 전달체 | |
KR101898502B1 (ko) | 인슐린-유사 성장 인자 1 수용체 결합 펩티드 | |
CN112279921A (zh) | 用于胞内递送分子的复合物 | |
KR101636538B1 (ko) | 인간 NLBP 유래의 NP2 폴리펩티드 또는 dNP2 폴리펩티드를 포함하는 세포 투과 펩티드 및 이를 이용한 카고 전달 시스템 | |
US20170275650A1 (en) | Endosomal escape domains for delivery of macromolecules into cells | |
KR20110013365A (ko) | 세포투과성 엔도스타틴 재조합 단백질, 이를 코딩하는 폴리뉴클레오티드 및 이를 유효성분으로 함유하는 항암 조성물 | |
AU2001285249B2 (en) | Membrane penetrating peptides and uses thereof | |
KR101651330B1 (ko) | 세포투과성이 우수한 tat-a20 융합단백질의 제조방법 및 이의 용도 | |
AU2001285249A1 (en) | Membrane penetrating peptides and uses thereof | |
KR20090122769A (ko) | 세포내로 단백질을 전달하는 방법 및 이를 위한 펩타이드 | |
KR101636542B1 (ko) | 인간 nlbp 유래의 np12 폴리펩티드 또는 np21 폴리펩티드를 포함하는 세포 투과 펩티드 및 이를 이용한 카고 전달 시스템 | |
KR101461750B1 (ko) | 인간 lpin3 단백질 유래의 세포 투과 펩티드 및 이를 이용한 카고 전달 시스템 | |
KR101564752B1 (ko) | 인간 nlbp 단백질 유래의 np1 폴리펩티드를 포함하는 세포 투과 펩티드 및 이를 이용한 카고 전달 시스템 | |
WO2013148285A1 (en) | Methods of inhibiting cell proliferation | |
Imamoto et al. | Import and export of proteins at the nucleus | |
Sayi | Functional analysis of the LIM kinase 1 and its role in cell cycle progression | |
Wang | Signaling mechanism and regulation of Frizzled |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
A201 | Request for examination | ||
E902 | Notification of reason for refusal | ||
E701 | Decision to grant or registration of patent right | ||
GRNT | Written decision to grant | ||
FPAY | Annual fee payment |
Payment date: 20130201 Year of fee payment: 6 |
|
FPAY | Annual fee payment |
Payment date: 20140205 Year of fee payment: 7 |
|
FPAY | Annual fee payment |
Payment date: 20150130 Year of fee payment: 8 |
|
FPAY | Annual fee payment |
Payment date: 20160127 Year of fee payment: 9 |
|
FPAY | Annual fee payment |
Payment date: 20170201 Year of fee payment: 10 |
|
FPAY | Annual fee payment |
Payment date: 20180201 Year of fee payment: 11 |
|
FPAY | Annual fee payment |
Payment date: 20190129 Year of fee payment: 12 |
|
FPAY | Annual fee payment |
Payment date: 20200129 Year of fee payment: 13 |