JP2003514765A - 新規形質導入分子およびその使用方法 - Google Patents
新規形質導入分子およびその使用方法Info
- Publication number
- JP2003514765A JP2003514765A JP2000611079A JP2000611079A JP2003514765A JP 2003514765 A JP2003514765 A JP 2003514765A JP 2000611079 A JP2000611079 A JP 2000611079A JP 2000611079 A JP2000611079 A JP 2000611079A JP 2003514765 A JP2003514765 A JP 2003514765A
- Authority
- JP
- Japan
- Prior art keywords
- protein
- mammal
- fusion
- cells
- molecule
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 238000000034 method Methods 0.000 title claims abstract description 183
- 230000002463 transducing effect Effects 0.000 title claims description 56
- 230000004927 fusion Effects 0.000 claims abstract description 235
- 210000000056 organ Anatomy 0.000 claims abstract description 33
- 210000004027 cell Anatomy 0.000 claims description 439
- 108090000623 proteins and genes Proteins 0.000 claims description 286
- 235000018102 proteins Nutrition 0.000 claims description 282
- 102000004169 proteins and genes Human genes 0.000 claims description 282
- 108020001507 fusion proteins Proteins 0.000 claims description 272
- 102000037865 fusion proteins Human genes 0.000 claims description 270
- 238000010361 transduction Methods 0.000 claims description 230
- 230000026683 transduction Effects 0.000 claims description 218
- 238000003776 cleavage reaction Methods 0.000 claims description 172
- 230000007017 scission Effects 0.000 claims description 171
- 239000004365 Protease Substances 0.000 claims description 146
- 102000035195 Peptidases Human genes 0.000 claims description 140
- 108091005804 Peptidases Proteins 0.000 claims description 140
- 241000124008 Mammalia Species 0.000 claims description 129
- 235000001014 amino acid Nutrition 0.000 claims description 120
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 115
- 150000001413 amino acids Chemical class 0.000 claims description 113
- 244000052769 pathogen Species 0.000 claims description 112
- 241000725303 Human immunodeficiency virus Species 0.000 claims description 102
- 230000001717 pathogenic effect Effects 0.000 claims description 86
- 239000003814 drug Substances 0.000 claims description 70
- 230000001472 cytotoxic effect Effects 0.000 claims description 69
- 231100000433 cytotoxic Toxicity 0.000 claims description 68
- 102000010911 Enzyme Precursors Human genes 0.000 claims description 67
- 108010062466 Enzyme Precursors Proteins 0.000 claims description 67
- 229940079593 drug Drugs 0.000 claims description 62
- 108020004414 DNA Proteins 0.000 claims description 47
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 46
- 210000001519 tissue Anatomy 0.000 claims description 45
- 102100029855 Caspase-3 Human genes 0.000 claims description 44
- 239000012634 fragment Substances 0.000 claims description 43
- 102000004190 Enzymes Human genes 0.000 claims description 39
- 108090000790 Enzymes Proteins 0.000 claims description 39
- 229940088598 enzyme Drugs 0.000 claims description 39
- 241000700605 Viruses Species 0.000 claims description 35
- 238000011282 treatment Methods 0.000 claims description 34
- 208000015181 infectious disease Diseases 0.000 claims description 33
- 108010010369 HIV Protease Proteins 0.000 claims description 31
- 230000001225 therapeutic effect Effects 0.000 claims description 31
- 239000004475 Arginine Substances 0.000 claims description 29
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 29
- 201000010099 disease Diseases 0.000 claims description 27
- 230000002147 killing effect Effects 0.000 claims description 25
- 231100000599 cytotoxic agent Toxicity 0.000 claims description 24
- 239000002619 cytotoxin Substances 0.000 claims description 24
- 238000012360 testing method Methods 0.000 claims description 24
- 101000793880 Homo sapiens Caspase-3 Proteins 0.000 claims description 23
- 108090000397 Caspase 3 Proteins 0.000 claims description 22
- 230000002708 enhancing effect Effects 0.000 claims description 22
- 235000004279 alanine Nutrition 0.000 claims description 21
- 230000027455 binding Effects 0.000 claims description 20
- 210000003169 central nervous system Anatomy 0.000 claims description 20
- 238000001727 in vivo Methods 0.000 claims description 20
- 241000288906 Primates Species 0.000 claims description 18
- 208000035475 disorder Diseases 0.000 claims description 18
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims description 17
- 238000003556 assay Methods 0.000 claims description 17
- 230000006378 damage Effects 0.000 claims description 17
- 102000011727 Caspases Human genes 0.000 claims description 16
- 108010076667 Caspases Proteins 0.000 claims description 16
- 210000004556 brain Anatomy 0.000 claims description 15
- 238000000338 in vitro Methods 0.000 claims description 15
- 230000003834 intracellular effect Effects 0.000 claims description 15
- 210000001428 peripheral nervous system Anatomy 0.000 claims description 15
- 101710112752 Cytotoxin Proteins 0.000 claims description 14
- 241000283984 Rodentia Species 0.000 claims description 13
- 230000035772 mutation Effects 0.000 claims description 13
- 241000699666 Mus <mouse, genus> Species 0.000 claims description 12
- 229960005486 vaccine Drugs 0.000 claims description 12
- -1 Mch5) Proteins 0.000 claims description 10
- 210000004369 blood Anatomy 0.000 claims description 10
- 239000008280 blood Substances 0.000 claims description 10
- 230000003197 catalytic effect Effects 0.000 claims description 10
- 208000024827 Alzheimer disease Diseases 0.000 claims description 9
- 241000700588 Human alphaherpesvirus 1 Species 0.000 claims description 9
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 9
- 239000003242 anti bacterial agent Substances 0.000 claims description 9
- 239000002246 antineoplastic agent Substances 0.000 claims description 9
- 244000005700 microbiome Species 0.000 claims description 9
- 239000000137 peptide hydrolase inhibitor Substances 0.000 claims description 9
- 108091032973 (ribonucleotides)n+m Proteins 0.000 claims description 8
- 241000894006 Bacteria Species 0.000 claims description 8
- 102000004091 Caspase-8 Human genes 0.000 claims description 8
- 108090000538 Caspase-8 Proteins 0.000 claims description 8
- 208000031886 HIV Infections Diseases 0.000 claims description 8
- 241000711549 Hepacivirus C Species 0.000 claims description 8
- 230000002924 anti-infective effect Effects 0.000 claims description 8
- 102100035904 Caspase-1 Human genes 0.000 claims description 7
- 108090000426 Caspase-1 Proteins 0.000 claims description 7
- 102100025064 Cellular tumor antigen p53 Human genes 0.000 claims description 7
- 241000701022 Cytomegalovirus Species 0.000 claims description 7
- 241001465754 Metazoa Species 0.000 claims description 7
- 241000283973 Oryctolagus cuniculus Species 0.000 claims description 7
- 238000010171 animal model Methods 0.000 claims description 7
- 230000001580 bacterial effect Effects 0.000 claims description 7
- 230000003115 biocidal effect Effects 0.000 claims description 7
- 239000003795 chemical substances by application Substances 0.000 claims description 7
- 108700031308 Antennapedia Homeodomain Proteins 0.000 claims description 6
- 102100038902 Caspase-7 Human genes 0.000 claims description 6
- 241000713772 Human immunodeficiency virus 1 Species 0.000 claims description 6
- 208000023105 Huntington disease Diseases 0.000 claims description 6
- 208000018737 Parkinson disease Diseases 0.000 claims description 6
- 102000006601 Thymidine Kinase Human genes 0.000 claims description 6
- 108020004440 Thymidine kinase Proteins 0.000 claims description 6
- 229960005475 antiinfective agent Drugs 0.000 claims description 6
- 230000008499 blood brain barrier function Effects 0.000 claims description 6
- 210000001218 blood-brain barrier Anatomy 0.000 claims description 6
- 229940002612 prodrug Drugs 0.000 claims description 6
- 239000000651 prodrug Substances 0.000 claims description 6
- 230000003612 virological effect Effects 0.000 claims description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 6
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 5
- 241000233866 Fungi Species 0.000 claims description 5
- 101710192266 Tegument protein VP22 Proteins 0.000 claims description 5
- 239000004599 antimicrobial Substances 0.000 claims description 5
- 230000001413 cellular effect Effects 0.000 claims description 5
- 238000011160 research Methods 0.000 claims description 5
- 208000030507 AIDS Diseases 0.000 claims description 4
- 208000000044 Amnesia Diseases 0.000 claims description 4
- 108090000567 Caspase 7 Proteins 0.000 claims description 4
- 102100025597 Caspase-4 Human genes 0.000 claims description 4
- 208000026139 Memory disease Diseases 0.000 claims description 4
- 241000244206 Nematoda Species 0.000 claims description 4
- 208000012902 Nervous system disease Diseases 0.000 claims description 4
- 241000223960 Plasmodium falciparum Species 0.000 claims description 4
- 206010036631 Presenile dementia Diseases 0.000 claims description 4
- 206010038997 Retroviral infections Diseases 0.000 claims description 4
- 230000036983 biotransformation Effects 0.000 claims description 4
- 244000000013 helminth Species 0.000 claims description 4
- 239000012678 infectious agent Substances 0.000 claims description 4
- 230000006984 memory degeneration Effects 0.000 claims description 4
- 208000023060 memory loss Diseases 0.000 claims description 4
- 238000001742 protein purification Methods 0.000 claims description 4
- 238000012216 screening Methods 0.000 claims description 4
- 241001529453 unidentified herpesvirus Species 0.000 claims description 4
- 230000009385 viral infection Effects 0.000 claims description 4
- 102000000311 Cytosine Deaminase Human genes 0.000 claims description 3
- 108010080611 Cytosine Deaminase Proteins 0.000 claims description 3
- 102000001398 Granzyme Human genes 0.000 claims description 3
- 108060005986 Granzyme Proteins 0.000 claims description 3
- 241000713340 Human immunodeficiency virus 2 Species 0.000 claims description 3
- 229930182555 Penicillin Natural products 0.000 claims description 3
- 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 claims description 3
- 108091000054 Prion Proteins 0.000 claims description 3
- 102000029797 Prion Human genes 0.000 claims description 3
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 claims description 3
- 101710102803 Tumor suppressor ARF Proteins 0.000 claims description 3
- 208000036142 Viral infection Diseases 0.000 claims description 3
- 230000006399 behavior Effects 0.000 claims description 3
- 238000005520 cutting process Methods 0.000 claims description 3
- 208000006454 hepatitis Diseases 0.000 claims description 3
- 231100000283 hepatitis Toxicity 0.000 claims description 3
- 239000005556 hormone Substances 0.000 claims description 3
- 229940088597 hormone Drugs 0.000 claims description 3
- 239000003550 marker Substances 0.000 claims description 3
- 229940049954 penicillin Drugs 0.000 claims description 3
- 230000002265 prevention Effects 0.000 claims description 3
- 101150047706 CASP6 gene Proteins 0.000 claims description 2
- 102000004018 Caspase 6 Human genes 0.000 claims description 2
- 108090000425 Caspase 6 Proteins 0.000 claims description 2
- 102000004068 Caspase-10 Human genes 0.000 claims description 2
- 108090000572 Caspase-10 Proteins 0.000 claims description 2
- 102000004046 Caspase-2 Human genes 0.000 claims description 2
- 108090000552 Caspase-2 Proteins 0.000 claims description 2
- 101710090338 Caspase-4 Proteins 0.000 claims description 2
- 102100038916 Caspase-5 Human genes 0.000 claims description 2
- 101710090333 Caspase-5 Proteins 0.000 claims description 2
- 102100026550 Caspase-9 Human genes 0.000 claims description 2
- 108090000566 Caspase-9 Proteins 0.000 claims description 2
- 101000933112 Homo sapiens Caspase-4 Proteins 0.000 claims description 2
- 101000741014 Homo sapiens Caspase-7 Proteins 0.000 claims description 2
- 201000009906 Meningitis Diseases 0.000 claims description 2
- 206010027202 Meningitis bacterial Diseases 0.000 claims description 2
- 239000004098 Tetracycline Substances 0.000 claims description 2
- 108090000190 Thrombin Proteins 0.000 claims description 2
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 claims description 2
- 229960000723 ampicillin Drugs 0.000 claims description 2
- 230000000202 analgesic effect Effects 0.000 claims description 2
- 210000004102 animal cell Anatomy 0.000 claims description 2
- 230000003110 anti-inflammatory effect Effects 0.000 claims description 2
- 229940034982 antineoplastic agent Drugs 0.000 claims description 2
- 201000009904 bacterial meningitis Diseases 0.000 claims description 2
- 230000004071 biological effect Effects 0.000 claims description 2
- 230000007812 deficiency Effects 0.000 claims description 2
- 238000007877 drug screening Methods 0.000 claims description 2
- 230000002526 effect on cardiovascular system Effects 0.000 claims description 2
- 206010014599 encephalitis Diseases 0.000 claims description 2
- 239000002095 exotoxin Substances 0.000 claims description 2
- 231100000776 exotoxin Toxicity 0.000 claims description 2
- 210000000987 immune system Anatomy 0.000 claims description 2
- 230000004941 influx Effects 0.000 claims description 2
- 229920002704 polyhistidine Polymers 0.000 claims description 2
- 239000003419 rna directed dna polymerase inhibitor Substances 0.000 claims description 2
- 241000894007 species Species 0.000 claims description 2
- 238000010998 test method Methods 0.000 claims description 2
- 229960002180 tetracycline Drugs 0.000 claims description 2
- 229930101283 tetracycline Natural products 0.000 claims description 2
- 235000019364 tetracycline Nutrition 0.000 claims description 2
- 150000003522 tetracyclines Chemical class 0.000 claims description 2
- 229960004072 thrombin Drugs 0.000 claims description 2
- ULGZDMOVFRHVEP-RWJQBGPGSA-N Erythromycin Chemical compound O([C@@H]1[C@@H](C)C(=O)O[C@@H]([C@@]([C@H](O)[C@@H](C)C(=O)[C@H](C)C[C@@](C)(O)[C@H](O[C@H]2[C@@H]([C@H](C[C@@H](C)O2)N(C)C)O)[C@H]1C)(C)O)CC)[C@H]1C[C@@](C)(OC)[C@@H](O)[C@H](C)O1 ULGZDMOVFRHVEP-RWJQBGPGSA-N 0.000 claims 4
- 241000282693 Cercopithecidae Species 0.000 claims 3
- 239000003443 antiviral agent Substances 0.000 claims 3
- 101710132601 Capsid protein Proteins 0.000 claims 2
- 229930186147 Cephalosporin Natural products 0.000 claims 2
- 101710094648 Coat protein Proteins 0.000 claims 2
- 206010010904 Convulsion Diseases 0.000 claims 2
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 claims 2
- 108010034145 Helminth Proteins Proteins 0.000 claims 2
- 241000577090 Human DNA virus Species 0.000 claims 2
- 241001502974 Human gammaherpesvirus 8 Species 0.000 claims 2
- 101710125418 Major capsid protein Proteins 0.000 claims 2
- 101710141454 Nucleoprotein Proteins 0.000 claims 2
- 241000282577 Pan troglodytes Species 0.000 claims 2
- 101710083689 Probable capsid protein Proteins 0.000 claims 2
- 206010002026 amyotrophic lateral sclerosis Diseases 0.000 claims 2
- 229940124587 cephalosporin Drugs 0.000 claims 2
- 150000001780 cephalosporins Chemical class 0.000 claims 2
- 229940127089 cytotoxic agent Drugs 0.000 claims 2
- 241001493065 dsRNA viruses Species 0.000 claims 2
- 206010015037 epilepsy Diseases 0.000 claims 2
- 229960003276 erythromycin Drugs 0.000 claims 2
- OTLLEIBWKHEHGU-UHFFFAOYSA-N 2-[5-[[5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy]-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3,5-dihydroxy-4-phosphonooxyhexanedioic acid Chemical compound C1=NC=2C(N)=NC=NC=2N1C(C(C1O)O)OC1COC1C(CO)OC(OC(C(O)C(OP(O)(O)=O)C(O)C(O)=O)C(O)=O)C(O)C1O OTLLEIBWKHEHGU-UHFFFAOYSA-N 0.000 claims 1
- 241000224489 Amoeba Species 0.000 claims 1
- 108010001478 Bacitracin Proteins 0.000 claims 1
- 208000035143 Bacterial infection Diseases 0.000 claims 1
- 206010027260 Meningitis viral Diseases 0.000 claims 1
- 229940122313 Nucleoside reverse transcriptase inhibitor Drugs 0.000 claims 1
- 241000282579 Pan Species 0.000 claims 1
- 241001631646 Papillomaviridae Species 0.000 claims 1
- 241000282520 Papio Species 0.000 claims 1
- 241000282405 Pongo abelii Species 0.000 claims 1
- 229940122803 Vinca alkaloid Drugs 0.000 claims 1
- 229940126575 aminoglycoside Drugs 0.000 claims 1
- LSQZJLSUYDQPKJ-NJBDSQKTSA-N amoxicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=C(O)C=C1 LSQZJLSUYDQPKJ-NJBDSQKTSA-N 0.000 claims 1
- 229960003022 amoxicillin Drugs 0.000 claims 1
- 239000003098 androgen Substances 0.000 claims 1
- 239000000921 anthelmintic agent Substances 0.000 claims 1
- 230000000843 anti-fungal effect Effects 0.000 claims 1
- 230000000340 anti-metabolite Effects 0.000 claims 1
- 230000000259 anti-tumor effect Effects 0.000 claims 1
- 239000000059 antiamebic agent Substances 0.000 claims 1
- 229940121375 antifungal agent Drugs 0.000 claims 1
- 230000000890 antigenic effect Effects 0.000 claims 1
- 239000003409 antileprotic agent Substances 0.000 claims 1
- 229940100197 antimetabolite Drugs 0.000 claims 1
- 239000002256 antimetabolite Substances 0.000 claims 1
- 229960003071 bacitracin Drugs 0.000 claims 1
- 229930184125 bacitracin Natural products 0.000 claims 1
- CLKOFPXJLQSYAH-ABRJDSQDSA-N bacitracin A Chemical compound C1SC([C@@H](N)[C@@H](C)CC)=N[C@@H]1C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]1C(=O)N[C@H](CCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2N=CNC=2)C(=O)N[C@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)NCCCC1 CLKOFPXJLQSYAH-ABRJDSQDSA-N 0.000 claims 1
- 208000022362 bacterial infectious disease Diseases 0.000 claims 1
- 239000003782 beta lactam antibiotic agent Substances 0.000 claims 1
- 230000000975 bioactive effect Effects 0.000 claims 1
- 210000004958 brain cell Anatomy 0.000 claims 1
- 208000015114 central nervous system disease Diseases 0.000 claims 1
- 230000000295 complement effect Effects 0.000 claims 1
- 230000003412 degenerative effect Effects 0.000 claims 1
- 206010013932 dyslexia Diseases 0.000 claims 1
- 210000003238 esophagus Anatomy 0.000 claims 1
- 229940011871 estrogen Drugs 0.000 claims 1
- 239000000262 estrogen Substances 0.000 claims 1
- 230000009395 genetic defect Effects 0.000 claims 1
- 230000002068 genetic effect Effects 0.000 claims 1
- 239000003667 hormone antagonist Substances 0.000 claims 1
- 231100000745 invertebrate toxin Toxicity 0.000 claims 1
- 210000004324 lymphatic system Anatomy 0.000 claims 1
- 229940042402 non-nucleoside reverse transcriptase inhibitor Drugs 0.000 claims 1
- 239000002726 nonnucleoside reverse transcriptase inhibitor Substances 0.000 claims 1
- LSQZJLSUYDQPKJ-UHFFFAOYSA-N p-Hydroxyampicillin Natural products O=C1N2C(C(O)=O)C(C)(C)SC2C1NC(=O)C(N)C1=CC=C(O)C=C1 LSQZJLSUYDQPKJ-UHFFFAOYSA-N 0.000 claims 1
- 208000020016 psychiatric disease Diseases 0.000 claims 1
- 150000003212 purines Chemical class 0.000 claims 1
- 150000003230 pyrimidines Chemical class 0.000 claims 1
- LISFMEBWQUVKPJ-UHFFFAOYSA-N quinolin-2-ol Chemical compound C1=CC=C2NC(=O)C=CC2=C1 LISFMEBWQUVKPJ-UHFFFAOYSA-N 0.000 claims 1
- 208000008864 scrapie Diseases 0.000 claims 1
- 229940124530 sulfonamide Drugs 0.000 claims 1
- 150000003456 sulfonamides Chemical class 0.000 claims 1
- IEDVJHCEMCRBQM-UHFFFAOYSA-N trimethoprim Chemical compound COC1=C(OC)C(OC)=CC(CC=2C(=NC(N)=NC=2)N)=C1 IEDVJHCEMCRBQM-UHFFFAOYSA-N 0.000 claims 1
- 229960001082 trimethoprim Drugs 0.000 claims 1
- 201000010044 viral meningitis Diseases 0.000 claims 1
- 239000002132 β-lactam antibiotic Substances 0.000 claims 1
- 229940124586 β-lactam antibiotics Drugs 0.000 claims 1
- IUCJMVBFZDHPDX-UHFFFAOYSA-N tretamine Chemical group C1CN1C1=NC(N2CC2)=NC(N2CC2)=N1 IUCJMVBFZDHPDX-UHFFFAOYSA-N 0.000 description 110
- 229940024606 amino acid Drugs 0.000 description 88
- 235000019419 proteases Nutrition 0.000 description 84
- 101710085003 Alpha-tubulin N-acetyltransferase Proteins 0.000 description 73
- 101710085461 Alpha-tubulin N-acetyltransferase 1 Proteins 0.000 description 73
- 101710175714 Tyrosine aminotransferase Proteins 0.000 description 73
- 102000004196 processed proteins & peptides Human genes 0.000 description 48
- 230000001775 anti-pathogenic effect Effects 0.000 description 38
- 239000013598 vector Substances 0.000 description 37
- 230000002223 anti-pathogen Effects 0.000 description 35
- 125000003275 alpha amino acid group Chemical group 0.000 description 34
- 210000001744 T-lymphocyte Anatomy 0.000 description 31
- 238000003752 polymerase chain reaction Methods 0.000 description 31
- 230000006907 apoptotic process Effects 0.000 description 29
- 230000000694 effects Effects 0.000 description 28
- 239000000203 mixture Substances 0.000 description 26
- 239000013615 primer Substances 0.000 description 24
- 238000004458 analytical method Methods 0.000 description 22
- 229920001184 polypeptide Polymers 0.000 description 22
- 235000009697 arginine Nutrition 0.000 description 21
- 125000005647 linker group Chemical group 0.000 description 21
- 150000007523 nucleic acids Chemical class 0.000 description 21
- 102100033254 Tumor suppressor ARF Human genes 0.000 description 20
- 150000001875 compounds Chemical class 0.000 description 20
- 241000699670 Mus sp. Species 0.000 description 18
- 102000039446 nucleic acids Human genes 0.000 description 18
- 108020004707 nucleic acids Proteins 0.000 description 18
- 230000004913 activation Effects 0.000 description 17
- 231100000331 toxic Toxicity 0.000 description 17
- 230000002588 toxic effect Effects 0.000 description 17
- NCDNCNXCDXHOMX-XGKFQTDJSA-N ritonavir Chemical compound N([C@@H](C(C)C)C(=O)N[C@H](C[C@H](O)[C@H](CC=1C=CC=CC=1)NC(=O)OCC=1SC=NC=1)CC=1C=CC=CC=1)C(=O)N(C)CC1=CSC(C(C)C)=N1 NCDNCNXCDXHOMX-XGKFQTDJSA-N 0.000 description 16
- 238000006467 substitution reaction Methods 0.000 description 16
- NCDNCNXCDXHOMX-UHFFFAOYSA-N Ritonavir Natural products C=1C=CC=CC=1CC(NC(=O)OCC=1SC=NC=1)C(O)CC(CC=1C=CC=CC=1)NC(=O)C(C(C)C)NC(=O)N(C)CC1=CSC(C(C)C)=N1 NCDNCNXCDXHOMX-UHFFFAOYSA-N 0.000 description 15
- 230000006870 function Effects 0.000 description 15
- 229960000311 ritonavir Drugs 0.000 description 15
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 14
- 125000000539 amino acid group Chemical group 0.000 description 14
- 230000003013 cytotoxicity Effects 0.000 description 14
- 231100000135 cytotoxicity Toxicity 0.000 description 14
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 14
- 101150100916 Casp3 gene Proteins 0.000 description 13
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 11
- 241000700584 Simplexvirus Species 0.000 description 11
- 239000002253 acid Substances 0.000 description 11
- 238000007792 addition Methods 0.000 description 11
- 238000013459 approach Methods 0.000 description 11
- 239000002299 complementary DNA Substances 0.000 description 11
- 238000007796 conventional method Methods 0.000 description 11
- 238000004519 manufacturing process Methods 0.000 description 11
- 101150019028 Antp gene Proteins 0.000 description 10
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 10
- 230000008901 benefit Effects 0.000 description 10
- 238000010367 cloning Methods 0.000 description 10
- 210000000653 nervous system Anatomy 0.000 description 10
- 230000000144 pharmacologic effect Effects 0.000 description 10
- 239000002953 phosphate buffered saline Substances 0.000 description 10
- 238000010561 standard procedure Methods 0.000 description 10
- 239000000758 substrate Substances 0.000 description 10
- 241000282412 Homo Species 0.000 description 9
- 230000030833 cell death Effects 0.000 description 9
- 239000002609 medium Substances 0.000 description 9
- 125000003729 nucleotide group Chemical group 0.000 description 9
- 239000013612 plasmid Substances 0.000 description 9
- 238000002360 preparation method Methods 0.000 description 9
- 238000000746 purification Methods 0.000 description 9
- 239000000126 substance Substances 0.000 description 9
- 108010077850 Nuclear Localization Signals Proteins 0.000 description 8
- 108091034117 Oligonucleotide Proteins 0.000 description 8
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 8
- 230000022534 cell killing Effects 0.000 description 8
- 239000003153 chemical reaction reagent Substances 0.000 description 8
- 210000000805 cytoplasm Anatomy 0.000 description 8
- 230000001419 dependent effect Effects 0.000 description 8
- 238000002474 experimental method Methods 0.000 description 8
- 230000009931 harmful effect Effects 0.000 description 8
- 210000004962 mammalian cell Anatomy 0.000 description 8
- 239000002773 nucleotide Substances 0.000 description 8
- 238000002560 therapeutic procedure Methods 0.000 description 8
- 241000588724 Escherichia coli Species 0.000 description 7
- 206010028980 Neoplasm Diseases 0.000 description 7
- GLNADSQYFUSGOU-GPTZEZBUSA-J Trypan blue Chemical compound [Na+].[Na+].[Na+].[Na+].C1=C(S([O-])(=O)=O)C=C2C=C(S([O-])(=O)=O)C(/N=N/C3=CC=C(C=C3C)C=3C=C(C(=CC=3)\N=N\C=3C(=CC4=CC(=CC(N)=C4C=3O)S([O-])(=O)=O)S([O-])(=O)=O)C)=C(O)C2=C1N GLNADSQYFUSGOU-GPTZEZBUSA-J 0.000 description 7
- MKUXAQIIEYXACX-UHFFFAOYSA-N aciclovir Chemical compound N1C(N)=NC(=O)C2=C1N(COCCO)C=N2 MKUXAQIIEYXACX-UHFFFAOYSA-N 0.000 description 7
- 239000000872 buffer Substances 0.000 description 7
- 239000004202 carbamide Substances 0.000 description 7
- 230000003833 cell viability Effects 0.000 description 7
- 238000006243 chemical reaction Methods 0.000 description 7
- 235000018417 cysteine Nutrition 0.000 description 7
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 7
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 7
- 230000006337 proteolytic cleavage Effects 0.000 description 7
- 230000010076 replication Effects 0.000 description 7
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 6
- 101000721661 Homo sapiens Cellular tumor antigen p53 Proteins 0.000 description 6
- 239000004472 Lysine Substances 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 101710149951 Protein Tat Proteins 0.000 description 6
- 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 6
- 229960004150 aciclovir Drugs 0.000 description 6
- 229940041181 antineoplastic drug Drugs 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 6
- 238000004587 chromatography analysis Methods 0.000 description 6
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 6
- 230000007717 exclusion Effects 0.000 description 6
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 6
- 230000006698 induction Effects 0.000 description 6
- 230000001939 inductive effect Effects 0.000 description 6
- 210000004072 lung Anatomy 0.000 description 6
- 201000004792 malaria Diseases 0.000 description 6
- 238000005259 measurement Methods 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 239000002777 nucleoside Substances 0.000 description 6
- 239000000523 sample Substances 0.000 description 6
- 208000037357 HIV infectious disease Diseases 0.000 description 5
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 5
- 230000036436 anti-hiv Effects 0.000 description 5
- 229940124599 anti-inflammatory drug Drugs 0.000 description 5
- 229940088710 antibiotic agent Drugs 0.000 description 5
- 239000007864 aqueous solution Substances 0.000 description 5
- 201000011510 cancer Diseases 0.000 description 5
- 239000002327 cardiovascular agent Substances 0.000 description 5
- 229940125692 cardiovascular agent Drugs 0.000 description 5
- 230000008859 change Effects 0.000 description 5
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 5
- 230000034994 death Effects 0.000 description 5
- 231100000517 death Toxicity 0.000 description 5
- 239000013604 expression vector Substances 0.000 description 5
- 238000000684 flow cytometry Methods 0.000 description 5
- 208000033519 human immunodeficiency virus infectious disease Diseases 0.000 description 5
- 230000002458 infectious effect Effects 0.000 description 5
- 239000003112 inhibitor Substances 0.000 description 5
- 229920002521 macromolecule Polymers 0.000 description 5
- 229930182817 methionine Natural products 0.000 description 5
- 238000000386 microscopy Methods 0.000 description 5
- 210000003205 muscle Anatomy 0.000 description 5
- 210000004940 nucleus Anatomy 0.000 description 5
- 239000002245 particle Substances 0.000 description 5
- 238000012545 processing Methods 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 150000003431 steroids Chemical class 0.000 description 5
- 230000014616 translation Effects 0.000 description 5
- 230000035899 viability Effects 0.000 description 5
- 239000011782 vitamin Substances 0.000 description 5
- 229940088594 vitamin Drugs 0.000 description 5
- 235000013343 vitamin Nutrition 0.000 description 5
- 229930003231 vitamin Natural products 0.000 description 5
- 208000035473 Communicable disease Diseases 0.000 description 4
- 102000053602 DNA Human genes 0.000 description 4
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 4
- 241000238631 Hexapoda Species 0.000 description 4
- 239000013543 active substance Substances 0.000 description 4
- 230000003321 amplification Effects 0.000 description 4
- 229940035676 analgesics Drugs 0.000 description 4
- 229940035674 anesthetics Drugs 0.000 description 4
- 239000000730 antalgic agent Substances 0.000 description 4
- 102000055102 bcl-2-Associated X Human genes 0.000 description 4
- 230000015556 catabolic process Effects 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 230000003196 chaotropic effect Effects 0.000 description 4
- 210000004748 cultured cell Anatomy 0.000 description 4
- 238000006731 degradation reaction Methods 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 230000018109 developmental process Effects 0.000 description 4
- 238000009472 formulation Methods 0.000 description 4
- 239000003193 general anesthetic agent Substances 0.000 description 4
- 239000004030 hiv protease inhibitor Substances 0.000 description 4
- 238000003119 immunoblot Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007928 intraperitoneal injection Substances 0.000 description 4
- 238000012933 kinetic analysis Methods 0.000 description 4
- 150000002632 lipids Chemical class 0.000 description 4
- 239000002502 liposome Substances 0.000 description 4
- 230000035800 maturation Effects 0.000 description 4
- 238000003199 nucleic acid amplification method Methods 0.000 description 4
- 150000003833 nucleoside derivatives Chemical class 0.000 description 4
- 230000036961 partial effect Effects 0.000 description 4
- 239000000813 peptide hormone Substances 0.000 description 4
- 230000001737 promoting effect Effects 0.000 description 4
- 230000017854 proteolysis Effects 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 210000000952 spleen Anatomy 0.000 description 4
- 239000003270 steroid hormone Substances 0.000 description 4
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 3
- 108700000712 BH3 Interacting Domain Death Agonist Proteins 0.000 description 3
- 102000055105 BH3 Interacting Domain Death Agonist Human genes 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 241000196324 Embryophyta Species 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 102000003886 Glycoproteins Human genes 0.000 description 3
- 108090000288 Glycoproteins Proteins 0.000 description 3
- 239000007995 HEPES buffer Substances 0.000 description 3
- 229940122440 HIV protease inhibitor Drugs 0.000 description 3
- 208000007514 Herpes zoster Diseases 0.000 description 3
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 3
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 3
- 241000208474 Protea Species 0.000 description 3
- 108050002653 Retinoblastoma protein Proteins 0.000 description 3
- 230000009471 action Effects 0.000 description 3
- 239000008186 active pharmaceutical agent Substances 0.000 description 3
- 239000000427 antigen Substances 0.000 description 3
- 108010008124 aspartyl-glutamyl-valyl-aspartyl-7-amino-4-trifluoromethylcoumarin Proteins 0.000 description 3
- 108010005774 beta-Galactosidase Proteins 0.000 description 3
- 210000000601 blood cell Anatomy 0.000 description 3
- 230000037396 body weight Effects 0.000 description 3
- 229940098773 bovine serum albumin Drugs 0.000 description 3
- 210000003855 cell nucleus Anatomy 0.000 description 3
- 238000003570 cell viability assay Methods 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 238000004440 column chromatography Methods 0.000 description 3
- 238000004624 confocal microscopy Methods 0.000 description 3
- 238000004132 cross linking Methods 0.000 description 3
- 230000001086 cytosolic effect Effects 0.000 description 3
- 238000004925 denaturation Methods 0.000 description 3
- 230000036425 denaturation Effects 0.000 description 3
- 238000003745 diagnosis Methods 0.000 description 3
- 229940088679 drug related substance Drugs 0.000 description 3
- 210000003527 eukaryotic cell Anatomy 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 238000001502 gel electrophoresis Methods 0.000 description 3
- 210000002865 immune cell Anatomy 0.000 description 3
- 230000036039 immunity Effects 0.000 description 3
- 210000003000 inclusion body Anatomy 0.000 description 3
- 150000002605 large molecules Chemical class 0.000 description 3
- 230000007246 mechanism Effects 0.000 description 3
- 230000000813 microbial effect Effects 0.000 description 3
- 230000007935 neutral effect Effects 0.000 description 3
- 238000010647 peptide synthesis reaction Methods 0.000 description 3
- 230000008092 positive effect Effects 0.000 description 3
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 3
- 230000000069 prophylactic effect Effects 0.000 description 3
- 230000002285 radioactive effect Effects 0.000 description 3
- 230000006798 recombination Effects 0.000 description 3
- 238000005215 recombination Methods 0.000 description 3
- 239000002904 solvent Substances 0.000 description 3
- 238000000527 sonication Methods 0.000 description 3
- 238000001228 spectrum Methods 0.000 description 3
- 239000003381 stabilizer Substances 0.000 description 3
- 230000004083 survival effect Effects 0.000 description 3
- 208000024891 symptom Diseases 0.000 description 3
- 229940124597 therapeutic agent Drugs 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 238000001890 transfection Methods 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- 238000013519 translation Methods 0.000 description 3
- 241001430294 unidentified retrovirus Species 0.000 description 3
- RAVVEEJGALCVIN-AGVBWZICSA-N (2s)-2-[[(2s)-2-[[(2s)-2-[[(2s)-5-amino-2-[[(2s)-2-[[(2s)-2-[[(2s)-6-amino-2-[[(2s)-6-amino-2-[[(2s)-2-[[2-[[(2s)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]hexanoyl]amino]hexanoyl]amino]-5-(diamino Chemical compound NC(N)=NCCC[C@@H](C(O)=O)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCN=C(N)N)NC(=O)CNC(=O)[C@@H](N)CC1=CC=C(O)C=C1 RAVVEEJGALCVIN-AGVBWZICSA-N 0.000 description 2
- 101710112984 20 kDa protein Proteins 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 241000282472 Canis lupus familiaris Species 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 102000003910 Cyclin D Human genes 0.000 description 2
- 108090000259 Cyclin D Proteins 0.000 description 2
- 102000013701 Cyclin-Dependent Kinase 4 Human genes 0.000 description 2
- 108010025464 Cyclin-Dependent Kinase 4 Proteins 0.000 description 2
- 102100038026 DNA fragmentation factor subunit alpha Human genes 0.000 description 2
- 101710182628 DNA fragmentation factor subunit alpha Proteins 0.000 description 2
- 102100038023 DNA fragmentation factor subunit beta Human genes 0.000 description 2
- 239000003155 DNA primer Substances 0.000 description 2
- 230000007018 DNA scission Effects 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 2
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 2
- 208000009889 Herpes Simplex Diseases 0.000 description 2
- 101000619542 Homo sapiens E3 ubiquitin-protein ligase parkin Proteins 0.000 description 2
- 241000598436 Human T-cell lymphotropic virus Species 0.000 description 2
- 241000701085 Human alphaherpesvirus 3 Species 0.000 description 2
- 108010016183 Human immunodeficiency virus 1 p16 protease Proteins 0.000 description 2
- 206010061598 Immunodeficiency Diseases 0.000 description 2
- 208000029462 Immunodeficiency disease Diseases 0.000 description 2
- 102000015696 Interleukins Human genes 0.000 description 2
- 108010063738 Interleukins Proteins 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
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- 101710159910 Movement protein Proteins 0.000 description 2
- 101000802812 Mus musculus BH3-interacting domain death agonist Proteins 0.000 description 2
- 108010021466 Mutant Proteins Proteins 0.000 description 2
- 102000008300 Mutant Proteins Human genes 0.000 description 2
- 206010028851 Necrosis Diseases 0.000 description 2
- 238000012408 PCR amplification Methods 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 241000224016 Plasmodium Species 0.000 description 2
- LOUPRKONTZGTKE-WZBLMQSHSA-N Quinine Chemical compound C([C@H]([C@H](C1)C=C)C2)C[N@@]1[C@@H]2[C@H](O)C1=CC=NC2=CC=C(OC)C=C21 LOUPRKONTZGTKE-WZBLMQSHSA-N 0.000 description 2
- 239000012979 RPMI medium Substances 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 108010039491 Ricin Proteins 0.000 description 2
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 2
- 206010052779 Transplant rejections Diseases 0.000 description 2
- 101710090398 Viral interleukin-10 homolog Proteins 0.000 description 2
- 239000012190 activator Substances 0.000 description 2
- 239000000443 aerosol Substances 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 239000002259 anti human immunodeficiency virus agent Substances 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 239000003430 antimalarial agent Substances 0.000 description 2
- 239000012062 aqueous buffer Substances 0.000 description 2
- 101150016874 asp3 gene Proteins 0.000 description 2
- 210000001185 bone marrow Anatomy 0.000 description 2
- 239000007975 buffered saline Substances 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 239000002775 capsule Substances 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 239000006143 cell culture medium Substances 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 230000012292 cell migration Effects 0.000 description 2
- 238000010382 chemical cross-linking Methods 0.000 description 2
- 238000007385 chemical modification Methods 0.000 description 2
- OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical compound NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 2
- 230000007123 defense Effects 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000011033 desalting Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- 239000000975 dye Substances 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 210000000981 epithelium Anatomy 0.000 description 2
- 238000013401 experimental design Methods 0.000 description 2
- 229930195729 fatty acid Natural products 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
- 210000002950 fibroblast Anatomy 0.000 description 2
- 239000007850 fluorescent dye Substances 0.000 description 2
- 239000003205 fragrance Substances 0.000 description 2
- 210000001035 gastrointestinal tract Anatomy 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 2
- 239000005090 green fluorescent protein Substances 0.000 description 2
- 230000009848 hypophosphorylation Effects 0.000 description 2
- 230000037451 immune surveillance Effects 0.000 description 2
- 230000007813 immunodeficiency Effects 0.000 description 2
- 230000001976 improved effect Effects 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 230000001965 increasing effect Effects 0.000 description 2
- 230000006882 induction of apoptosis Effects 0.000 description 2
- 201000006747 infectious mononucleosis Diseases 0.000 description 2
- 206010022000 influenza Diseases 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 239000008101 lactose Substances 0.000 description 2
- 231100000518 lethal Toxicity 0.000 description 2
- 230000001665 lethal effect Effects 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 230000004807 localization Effects 0.000 description 2
- 230000033001 locomotion Effects 0.000 description 2
- 210000004698 lymphocyte Anatomy 0.000 description 2
- HQKMJHAJHXVSDF-UHFFFAOYSA-L magnesium stearate Chemical compound [Mg+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O HQKMJHAJHXVSDF-UHFFFAOYSA-L 0.000 description 2
- 238000007726 management method Methods 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
- 235000013336 milk Nutrition 0.000 description 2
- 239000008267 milk Substances 0.000 description 2
- 210000004080 milk Anatomy 0.000 description 2
- 210000003470 mitochondria Anatomy 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 230000017074 necrotic cell death Effects 0.000 description 2
- 125000003835 nucleoside group Chemical group 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- 230000036407 pain Effects 0.000 description 2
- 102000045222 parkin Human genes 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 235000019833 protease Nutrition 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 208000028172 protozoa infectious disease Diseases 0.000 description 2
- 238000011002 quantification Methods 0.000 description 2
- 238000010188 recombinant method Methods 0.000 description 2
- 230000003362 replicative effect Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 238000004062 sedimentation Methods 0.000 description 2
- 235000012239 silicon dioxide Nutrition 0.000 description 2
- 150000003384 small molecules Chemical class 0.000 description 2
- 210000004989 spleen cell Anatomy 0.000 description 2
- 238000010911 splenectomy Methods 0.000 description 2
- 238000007447 staining method Methods 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 239000000454 talc Substances 0.000 description 2
- 229910052623 talc Inorganic materials 0.000 description 2
- 235000012222 talc Nutrition 0.000 description 2
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- 210000002845 virion Anatomy 0.000 description 2
- WHTVZRBIWZFKQO-AWEZNQCLSA-N (S)-chloroquine Chemical compound ClC1=CC=C2C(N[C@@H](C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-AWEZNQCLSA-N 0.000 description 1
- LDVVTQMJQSCDMK-UHFFFAOYSA-N 1,3-dihydroxypropan-2-yl formate Chemical compound OCC(CO)OC=O LDVVTQMJQSCDMK-UHFFFAOYSA-N 0.000 description 1
- BJFILYACUCTLKB-UHFFFAOYSA-N 2-chloroguanidine Chemical compound NC(N)=NCl BJFILYACUCTLKB-UHFFFAOYSA-N 0.000 description 1
- HVCOBJNICQPDBP-UHFFFAOYSA-N 3-[3-[3,5-dihydroxy-6-methyl-4-(3,4,5-trihydroxy-6-methyloxan-2-yl)oxyoxan-2-yl]oxydecanoyloxy]decanoic acid;hydrate Chemical compound O.OC1C(OC(CC(=O)OC(CCCCCCC)CC(O)=O)CCCCCCC)OC(C)C(O)C1OC1C(O)C(O)C(O)C(C)O1 HVCOBJNICQPDBP-UHFFFAOYSA-N 0.000 description 1
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
- 108010066676 Abrin Proteins 0.000 description 1
- 208000029483 Acquired immunodeficiency Diseases 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 108020005544 Antisense RNA Proteins 0.000 description 1
- 241000269350 Anura Species 0.000 description 1
- 102000007272 Apoptosis Inducing Factor Human genes 0.000 description 1
- 108010033604 Apoptosis Inducing Factor Proteins 0.000 description 1
- 102000010565 Apoptosis Regulatory Proteins Human genes 0.000 description 1
- 108010063104 Apoptosis Regulatory Proteins Proteins 0.000 description 1
- 102100021569 Apoptosis regulator Bcl-2 Human genes 0.000 description 1
- 101800001109 Assemblin Proteins 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 231100000699 Bacterial toxin Toxicity 0.000 description 1
- 101150017888 Bcl2 gene Proteins 0.000 description 1
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 208000011691 Burkitt lymphomas Diseases 0.000 description 1
- 108090000994 Catalytic RNA Proteins 0.000 description 1
- 102000053642 Catalytic RNA Human genes 0.000 description 1
- 102000009016 Cholera Toxin Human genes 0.000 description 1
- 108010049048 Cholera Toxin Proteins 0.000 description 1
- 206010008748 Chorea Diseases 0.000 description 1
- 108010077544 Chromatin Proteins 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 235000001258 Cinchona calisaya Nutrition 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 229920002261 Corn starch Polymers 0.000 description 1
- 102100030497 Cytochrome c Human genes 0.000 description 1
- 108010075031 Cytochromes c Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 108020001019 DNA Primers Proteins 0.000 description 1
- 230000005778 DNA damage Effects 0.000 description 1
- 231100000277 DNA damage Toxicity 0.000 description 1
- 230000004543 DNA replication Effects 0.000 description 1
- 102000052510 DNA-Binding Proteins Human genes 0.000 description 1
- 101710096438 DNA-binding protein Proteins 0.000 description 1
- 101100382568 Danio rerio caspa gene Proteins 0.000 description 1
- 206010011906 Death Diseases 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 108010053187 Diphtheria Toxin Proteins 0.000 description 1
- 102000016607 Diphtheria Toxin Human genes 0.000 description 1
- 101800000585 Diphtheria toxin fragment A Proteins 0.000 description 1
- 241000255925 Diptera Species 0.000 description 1
- 101100284769 Drosophila melanogaster hemo gene Proteins 0.000 description 1
- 206010059866 Drug resistance Diseases 0.000 description 1
- 108050002772 E3 ubiquitin-protein ligase Mdm2 Proteins 0.000 description 1
- 102000012199 E3 ubiquitin-protein ligase Mdm2 Human genes 0.000 description 1
- 241000709661 Enterovirus Species 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 108091092566 Extrachromosomal DNA Proteins 0.000 description 1
- 241000701087 Felid alphaherpesvirus 1 Species 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 102000009123 Fibrin Human genes 0.000 description 1
- 108010073385 Fibrin Proteins 0.000 description 1
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 1
- 201000008808 Fibrosarcoma Diseases 0.000 description 1
- 241000710781 Flaviviridae Species 0.000 description 1
- 241000710831 Flavivirus Species 0.000 description 1
- 101710177291 Gag polyprotein Proteins 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 108700004714 Gelonium multiflorum GEL Proteins 0.000 description 1
- 241001272178 Glires Species 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 229930186217 Glycolipid Natural products 0.000 description 1
- 208000027814 HTLV-2 infection Diseases 0.000 description 1
- 241000125500 Hedypnois rhagadioloides Species 0.000 description 1
- 208000004898 Herpes Labialis Diseases 0.000 description 1
- 208000000903 Herpes simplex encephalitis Diseases 0.000 description 1
- 208000037018 Herpes simplex virus encephalitis Diseases 0.000 description 1
- 208000029433 Herpesviridae infectious disease Diseases 0.000 description 1
- 108010048671 Homeodomain Proteins Proteins 0.000 description 1
- 102000009331 Homeodomain Proteins Human genes 0.000 description 1
- 101000950965 Homo sapiens DNA fragmentation factor subunit beta Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 108010070875 Human Immunodeficiency Virus tat Gene Products Proteins 0.000 description 1
- 241000714260 Human T-lymphotropic virus 1 Species 0.000 description 1
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 1
- 241000701027 Human herpesvirus 6 Species 0.000 description 1
- 108700000788 Human immunodeficiency virus 1 tat peptide (47-57) Proteins 0.000 description 1
- 102100034343 Integrase Human genes 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 102000000588 Interleukin-2 Human genes 0.000 description 1
- 108010002350 Interleukin-2 Proteins 0.000 description 1
- 241001138401 Kluyveromyces lactis Species 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- 241000254158 Lampyridae Species 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- HLFSDGLLUJUHTE-SNVBAGLBSA-N Levamisole Chemical compound C1([C@H]2CN3CCSC3=N2)=CC=CC=C1 HLFSDGLLUJUHTE-SNVBAGLBSA-N 0.000 description 1
- 241000406668 Loxodonta cyclotis Species 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- 102000004317 Lyases Human genes 0.000 description 1
- 108090000856 Lyases Proteins 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- 101800000577 Maturation protease Proteins 0.000 description 1
- 208000002454 Nasopharyngeal Carcinoma Diseases 0.000 description 1
- 206010061306 Nasopharyngeal cancer Diseases 0.000 description 1
- 208000009869 Neu-Laxova syndrome Diseases 0.000 description 1
- 108091005461 Nucleic proteins Proteins 0.000 description 1
- 206010067152 Oral herpes Diseases 0.000 description 1
- 241000282376 Panthera tigris Species 0.000 description 1
- 229930040373 Paraformaldehyde Natural products 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- JNTOCHDNEULJHD-UHFFFAOYSA-N Penciclovir Chemical compound N1C(N)=NC(=O)C2=C1N(CCC(CO)CO)C=N2 JNTOCHDNEULJHD-UHFFFAOYSA-N 0.000 description 1
- 241000287463 Phalacrocorax Species 0.000 description 1
- 102000015439 Phospholipases Human genes 0.000 description 1
- 108010064785 Phospholipases Proteins 0.000 description 1
- 101000777480 Phyllodiscus semoni DELTA-alicitoxin-Pse1b Proteins 0.000 description 1
- 231100000742 Plant toxin Toxicity 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 108090000568 Plasmepsin II Proteins 0.000 description 1
- 241000223821 Plasmodium malariae Species 0.000 description 1
- 206010035501 Plasmodium malariae infection Diseases 0.000 description 1
- 241001505293 Plasmodium ovale Species 0.000 description 1
- 206010035502 Plasmodium ovale infection Diseases 0.000 description 1
- 101150005409 Pmch gene Proteins 0.000 description 1
- 229920000776 Poly(Adenosine diphosphate-ribose) polymerase Polymers 0.000 description 1
- 239000004698 Polyethylene Substances 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 108010076039 Polyproteins Proteins 0.000 description 1
- 101710127332 Protease I Proteins 0.000 description 1
- 101000762949 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) Exotoxin A Proteins 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 101100256174 Rattus norvegicus Olah gene Proteins 0.000 description 1
- 206010038910 Retinitis Diseases 0.000 description 1
- 102100030852 Run domain Beclin-1-interacting and cysteine-rich domain-containing protein Human genes 0.000 description 1
- 101710179516 Run domain Beclin-1-interacting and cysteine-rich domain-containing protein Proteins 0.000 description 1
- 241000231739 Rutilus rutilus Species 0.000 description 1
- 108010084592 Saporins Proteins 0.000 description 1
- 206010070834 Sensitisation Diseases 0.000 description 1
- 241000270295 Serpentes Species 0.000 description 1
- 101710137500 T7 RNA polymerase Proteins 0.000 description 1
- 101150003725 TK gene Proteins 0.000 description 1
- 238000012288 TUNEL assay Methods 0.000 description 1
- 101710137710 Thioesterase 1/protease 1/lysophospholipase L1 Proteins 0.000 description 1
- 108010046075 Thymosin Proteins 0.000 description 1
- 102000007501 Thymosin Human genes 0.000 description 1
- 240000002657 Thymus vulgaris Species 0.000 description 1
- 235000007303 Thymus vulgaris Nutrition 0.000 description 1
- 241000656145 Thyrsites atun Species 0.000 description 1
- 102000004357 Transferases Human genes 0.000 description 1
- 108090000992 Transferases Proteins 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108010079351 Tumor Suppressor Protein p14ARF Proteins 0.000 description 1
- 102000014384 Type C Phospholipases Human genes 0.000 description 1
- 108010079194 Type C Phospholipases Proteins 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- 241000710772 Yellow fever virus Species 0.000 description 1
- RLAHNGKRJJEIJL-RFZPGFLSSA-N [(2r,4r)-4-(2,6-diaminopurin-9-yl)-1,3-dioxolan-2-yl]methanol Chemical compound C12=NC(N)=NC(N)=C2N=CN1[C@H]1CO[C@@H](CO)O1 RLAHNGKRJJEIJL-RFZPGFLSSA-N 0.000 description 1
- WMHSRBZIJNQHKT-FFKFEZPRSA-N abacavir sulfate Chemical compound OS(O)(=O)=O.C=12N=CN([C@H]3C=C[C@@H](CO)C3)C2=NC(N)=NC=1NC1CC1.C=12N=CN([C@H]3C=C[C@@H](CO)C3)C2=NC(N)=NC=1NC1CC1 WMHSRBZIJNQHKT-FFKFEZPRSA-N 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 239000000556 agonist Substances 0.000 description 1
- 230000006229 amino acid addition Effects 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 230000003444 anaesthetic effect Effects 0.000 description 1
- 230000036592 analgesia Effects 0.000 description 1
- 231100000659 animal toxin Toxicity 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 239000003945 anionic surfactant Substances 0.000 description 1
- 230000003288 anthiarrhythmic effect Effects 0.000 description 1
- 230000003466 anti-cipated effect Effects 0.000 description 1
- 229940127003 anti-diabetic drug Drugs 0.000 description 1
- 230000000078 anti-malarial effect Effects 0.000 description 1
- 230000000845 anti-microbial effect Effects 0.000 description 1
- 230000000118 anti-neoplastic effect Effects 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 239000002220 antihypertensive agent Substances 0.000 description 1
- 229940030600 antihypertensive agent Drugs 0.000 description 1
- 230000005756 apoptotic signaling Effects 0.000 description 1
- 239000010692 aromatic oil Substances 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 150000001510 aspartic acids Chemical class 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000003190 augmentative effect Effects 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 239000000688 bacterial toxin Substances 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 150000001607 bioavailable molecules Chemical class 0.000 description 1
- 239000003139 biocide Substances 0.000 description 1
- 239000013060 biological fluid Substances 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 238000004159 blood analysis Methods 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 230000003139 buffering effect Effects 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 238000009924 canning Methods 0.000 description 1
- 239000012876 carrier material Substances 0.000 description 1
- 108010042238 caspase-activated deoxyribonuclease Proteins 0.000 description 1
- 230000006652 catabolic pathway Effects 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 101150055276 ced-3 gene Proteins 0.000 description 1
- 238000012832 cell culture technique Methods 0.000 description 1
- 230000022131 cell cycle Effects 0.000 description 1
- 230000012820 cell cycle checkpoint Effects 0.000 description 1
- 230000005779 cell damage Effects 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 208000037887 cell injury Diseases 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 238000013043 cell viability test Methods 0.000 description 1
- 230000004700 cellular uptake Effects 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- 229960003677 chloroquine Drugs 0.000 description 1
- WHTVZRBIWZFKQO-UHFFFAOYSA-N chloroquine Natural products ClC1=CC=C2C(NC(C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-UHFFFAOYSA-N 0.000 description 1
- 208000012601 choreatic disease Diseases 0.000 description 1
- 210000003483 chromatin Anatomy 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- VYVRIXWNTVOIRD-UHFFFAOYSA-N ciguatoxin Natural products O1C(C(C(C)C2OC3CC(C)CC4OC5(C)C(O)CC6OC7C=CC8OC9CC%10C(C(C%11OC(C=CCC%11O%10)C=CC(O)CO)O)OC9C=CC8OC7CC=CCC6OC5CC4OC3CC2O2)O)C2C(C)C(C)C21CC(O)CO2 VYVRIXWNTVOIRD-UHFFFAOYSA-N 0.000 description 1
- LOUPRKONTZGTKE-UHFFFAOYSA-N cinchonine Natural products C1C(C(C2)C=C)CCN2C1C(O)C1=CC=NC2=CC=C(OC)C=C21 LOUPRKONTZGTKE-UHFFFAOYSA-N 0.000 description 1
- 238000012411 cloning technique Methods 0.000 description 1
- 238000011260 co-administration Methods 0.000 description 1
- 238000000975 co-precipitation Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 239000003184 complementary RNA Substances 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 238000007596 consolidation process Methods 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 239000008120 corn starch Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 125000004122 cyclic group Chemical group 0.000 description 1
- 208000031513 cyst Diseases 0.000 description 1
- 208000020023 cytomegalovirus pneumonia Diseases 0.000 description 1
- 229940104302 cytosine Drugs 0.000 description 1
- 238000002784 cytotoxicity assay Methods 0.000 description 1
- 231100000263 cytotoxicity test Toxicity 0.000 description 1
- 230000006735 deficit Effects 0.000 description 1
- 210000004268 dentin Anatomy 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 239000005546 dideoxynucleotide Substances 0.000 description 1
- 230000001079 digestive effect Effects 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
- 230000008034 disappearance Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000008298 dragée Substances 0.000 description 1
- 229940000406 drug candidate Drugs 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 238000009509 drug development Methods 0.000 description 1
- 238000007876 drug discovery Methods 0.000 description 1
- 230000004064 dysfunction Effects 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 238000001976 enzyme digestion Methods 0.000 description 1
- 238000011067 equilibration Methods 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 239000003777 experimental drug Substances 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 238000001125 extrusion Methods 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- LLYJISDUHFXOHK-GOCONZMPSA-N ferroptocide Chemical compound C[C@@H]1CC[C@@]23C[C@@H](C(=O)[C@]2([C@@]1([C@@H](C[C@H]([C@@H]3C)C4=CCN5C(=O)N(C(=O)N5C4)C6=CC=CC=C6)OC(=O)CCl)C)O)O LLYJISDUHFXOHK-GOCONZMPSA-N 0.000 description 1
- 229950003499 fibrin Drugs 0.000 description 1
- 238000000799 fluorescence microscopy Methods 0.000 description 1
- 238000001215 fluorescent labelling Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 125000002485 formyl group Chemical group [H]C(*)=O 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- ZZUFCTLCJUWOSV-UHFFFAOYSA-N furosemide Chemical compound C1=C(Cl)C(S(=O)(=O)N)=CC(C(O)=O)=C1NCC1=CC=CO1 ZZUFCTLCJUWOSV-UHFFFAOYSA-N 0.000 description 1
- 108010027225 gag-pol Fusion Proteins Proteins 0.000 description 1
- 229960002963 ganciclovir Drugs 0.000 description 1
- IRSCQMHQWWYFCW-UHFFFAOYSA-N ganciclovir Chemical compound O=C1NC(N)=NC2=C1N=CN2COC(CO)CO IRSCQMHQWWYFCW-UHFFFAOYSA-N 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 108060003196 globin Proteins 0.000 description 1
- 102000018146 globin Human genes 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 210000002216 heart Anatomy 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 206010073071 hepatocellular carcinoma Diseases 0.000 description 1
- 231100000844 hepatocellular carcinoma Toxicity 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 102000056454 human CASP3 Human genes 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 244000052637 human pathogen Species 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000006058 immune tolerance Effects 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000002055 immunohistochemical effect Effects 0.000 description 1
- 239000002955 immunomodulating agent Substances 0.000 description 1
- 229940121354 immunomodulator Drugs 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 238000012744 immunostaining Methods 0.000 description 1
- 229960003444 immunosuppressant agent Drugs 0.000 description 1
- 239000003018 immunosuppressive agent Substances 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 238000012750 in vivo screening Methods 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 208000037797 influenza A Diseases 0.000 description 1
- 208000037798 influenza B Diseases 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 230000004068 intracellular signaling Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 239000002563 ionic surfactant Substances 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 206010023332 keratitis Diseases 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 229960001614 levamisole Drugs 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 239000000314 lubricant Substances 0.000 description 1
- 230000001926 lymphatic effect Effects 0.000 description 1
- 238000010841 mRNA extraction Methods 0.000 description 1
- 235000019359 magnesium stearate Nutrition 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 206010025482 malaise Diseases 0.000 description 1
- 210000005171 mammalian brain Anatomy 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000008774 maternal effect Effects 0.000 description 1
- 101150024647 mch gene Proteins 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- TWXDDNPPQUTEOV-FVGYRXGTSA-N methamphetamine hydrochloride Chemical compound Cl.CN[C@@H](C)CC1=CC=CC=C1 TWXDDNPPQUTEOV-FVGYRXGTSA-N 0.000 description 1
- TWBTYFFJJKWART-UHFFFAOYSA-N methyl 2-[[4,6-bis(propan-2-ylamino)-1,3,5-triazin-2-yl]oxy]benzoate Chemical compound COC(=O)C1=CC=CC=C1OC1=NC(NC(C)C)=NC(NC(C)C)=N1 TWBTYFFJJKWART-UHFFFAOYSA-N 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 238000007431 microscopic evaluation Methods 0.000 description 1
- 230000002438 mitochondrial effect Effects 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 210000005087 mononuclear cell Anatomy 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 201000011216 nasopharynx carcinoma Diseases 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- 238000006396 nitration reaction Methods 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- QJGQUHMNIGDVPM-UHFFFAOYSA-N nitrogen group Chemical group [N] QJGQUHMNIGDVPM-UHFFFAOYSA-N 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 238000002515 oligonucleotide synthesis Methods 0.000 description 1
- 229940127240 opiate Drugs 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 239000012188 paraffin wax Substances 0.000 description 1
- 229920002866 paraformaldehyde Polymers 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 229960001179 penciclovir Drugs 0.000 description 1
- MCYTYTUNNNZWOK-LCLOTLQISA-N penetratin 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(N)=O)C1=CC=CC=C1 MCYTYTUNNNZWOK-LCLOTLQISA-N 0.000 description 1
- 108010043655 penetratin Proteins 0.000 description 1
- 239000000816 peptidomimetic Substances 0.000 description 1
- 230000008447 perception Effects 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 230000002085 persistent effect Effects 0.000 description 1
- 239000003208 petroleum Substances 0.000 description 1
- 239000008177 pharmaceutical agent Substances 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 238000001050 pharmacotherapy Methods 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000003123 plant toxin Substances 0.000 description 1
- 108010020708 plasmepsin Proteins 0.000 description 1
- 108700028325 pokeweed antiviral Proteins 0.000 description 1
- 108010089520 pol Gene Products Proteins 0.000 description 1
- 238000000711 polarimetry Methods 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 231100000683 possible toxicity Toxicity 0.000 description 1
- 229920001592 potato starch Polymers 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 238000003825 pressing Methods 0.000 description 1
- 150000003141 primary amines Chemical class 0.000 description 1
- 210000005238 principal cell Anatomy 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000002062 proliferating effect Effects 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 239000012474 protein marker Substances 0.000 description 1
- 230000030788 protein refolding Effects 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 230000012743 protein tagging Effects 0.000 description 1
- 230000005180 public health Effects 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 239000010453 quartz Substances 0.000 description 1
- 229960000948 quinine Drugs 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000011514 reflex Effects 0.000 description 1
- 230000001850 reproductive effect Effects 0.000 description 1
- 230000008261 resistance mechanism Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 108091092562 ribozyme Proteins 0.000 description 1
- 239000012266 salt solution Substances 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 150000003335 secondary amines Chemical class 0.000 description 1
- 230000008313 sensitization Effects 0.000 description 1
- 230000001953 sensory effect Effects 0.000 description 1
- 230000001568 sexual effect Effects 0.000 description 1
- RMAQACBXLXPBSY-UHFFFAOYSA-N silicic acid Chemical compound O[Si](O)(O)O RMAQACBXLXPBSY-UHFFFAOYSA-N 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N silicon dioxide Inorganic materials O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 238000004513 sizing Methods 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 239000002708 spider venom Substances 0.000 description 1
- 210000000278 spinal cord Anatomy 0.000 description 1
- 238000009987 spinning Methods 0.000 description 1
- 210000004988 splenocyte Anatomy 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- GECHUMIMRBOMGK-UHFFFAOYSA-N sulfapyridine Chemical compound C1=CC(N)=CC=C1S(=O)(=O)NC1=CC=CC=N1 GECHUMIMRBOMGK-UHFFFAOYSA-N 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 239000000829 suppository Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 238000013268 sustained release Methods 0.000 description 1
- 239000012730 sustained-release form Substances 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 239000003826 tablet Substances 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 150000003512 tertiary amines Chemical class 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- LCJVIYPJPCBWKS-NXPQJCNCSA-N thymosin Chemical compound SC[C@@H](N)C(=O)N[C@H](CO)C(=O)N[C@H](CC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@H](C(C)C)C(=O)N[C@H](CC(O)=O)C(=O)N[C@H](C(C)C)C(=O)N[C@H](CO)C(=O)N[C@H](CO)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@H]([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](CCCCN)C(=O)N[C@H](CC(O)=O)C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@H](CCCCN)C(=O)N[C@H](CCCCN)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@H](C(C)C)C(=O)N[C@H](C(C)C)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@H](CCC(O)=O)C(O)=O LCJVIYPJPCBWKS-NXPQJCNCSA-N 0.000 description 1
- 239000001585 thymus vulgaris Substances 0.000 description 1
- 238000003325 tomography Methods 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 210000003437 trachea Anatomy 0.000 description 1
- 229940043263 traditional drug Drugs 0.000 description 1
- 238000003151 transfection method Methods 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 239000003656 tris buffered saline Substances 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 238000005199 ultracentrifugation Methods 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 210000003934 vacuole Anatomy 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- 235000015112 vegetable and seed oil Nutrition 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 230000029812 viral genome replication Effects 0.000 description 1
- 238000012800 visualization Methods 0.000 description 1
- 150000003722 vitamin derivatives Chemical class 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- 239000012130 whole-cell lysate Substances 0.000 description 1
- 229940051021 yellow-fever virus Drugs 0.000 description 1
- 239000010457 zeolite Substances 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- 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
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K67/00—Rearing or breeding animals, not otherwise provided for; New or modified breeds of animals
- A01K67/027—New or modified breeds of vertebrates
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/51—Medicinal preparations containing antigens or antibodies comprising whole cells, viruses or DNA/RNA
- A61K2039/525—Virus
-
- 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
- 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
- C07K2319/50—Fusion polypeptide containing protease site
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/55—Fusion polypeptide containing a fusion with a toxin, e.g. diphteria toxin
-
- 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]
-
- 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
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/16011—Human Immunodeficiency Virus, HIV
- C12N2740/16311—Human Immunodeficiency Virus, HIV concerning HIV regulatory proteins
- C12N2740/16322—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Animal Behavior & Ethology (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- Biomedical Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Wood Science & Technology (AREA)
- Biophysics (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Environmental Sciences (AREA)
- Physics & Mathematics (AREA)
- Neurosurgery (AREA)
- Neurology (AREA)
- Plant Pathology (AREA)
- Microbiology (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Heart & Thoracic Surgery (AREA)
- Pain & Pain Management (AREA)
- Rheumatology (AREA)
- Virology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Animal Husbandry (AREA)
- Biodiversity & Conservation Biology (AREA)
Applications Claiming Priority (5)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US12275799P | 1999-02-28 | 1999-02-28 | |
US60/122,757 | 1999-02-28 | ||
US15129199P | 1999-08-29 | 1999-08-29 | |
US60/151,291 | 1999-08-29 | ||
PCT/US2000/005097 WO2000062067A1 (en) | 1999-02-28 | 2000-02-28 | Novel transduction molecules and methods for using same |
Publications (1)
Publication Number | Publication Date |
---|---|
JP2003514765A true JP2003514765A (ja) | 2003-04-22 |
Family
ID=26820859
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2000611079A Pending JP2003514765A (ja) | 1999-02-28 | 2000-02-28 | 新規形質導入分子およびその使用方法 |
Country Status (5)
Country | Link |
---|---|
EP (1) | EP1157275A4 (de) |
JP (1) | JP2003514765A (de) |
AU (1) | AU7497000A (de) |
CA (1) | CA2364690A1 (de) |
WO (1) | WO2000062067A1 (de) |
Cited By (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2007099707A (ja) * | 2005-10-05 | 2007-04-19 | Toagosei Co Ltd | 神経分化抑制ペプチド及びその利用 |
JP2007527856A (ja) * | 2003-06-30 | 2007-10-04 | ユニベルシテ ド ローザンヌ | 癌細胞を選択的に死滅させるRasGAP由来ペプチド |
JP2009532045A (ja) * | 2006-04-07 | 2009-09-10 | ゲオルク−アウグスト−ウニヴェルジテート・ゲッティンゲン・シュティフトゥング・エッフェントリヒェン・レッヒツ | タンパク質置換治療のための合成mecp2配列 |
JP2010226992A (ja) * | 2009-03-26 | 2010-10-14 | Nihon Univ | レチノイン酸受容体αを含む融合タンパク質 |
JP5817038B2 (ja) * | 2009-06-22 | 2015-11-18 | 洋孝 松尾 | 尿酸トランスポーター、並びに、尿酸輸送関連疾患素因及び炎症関連疾患素因の評価方法及び評価キット、検査体及び薬 |
Families Citing this family (37)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
ATE319447T1 (de) | 1999-08-16 | 2006-03-15 | Revaax Pharmaceuticals Llc | Pharmazeutische zubereitungen die clavulansäure oder derivate enthalten zur behandlund von neurologischen störungen |
US6881825B1 (en) | 1999-09-01 | 2005-04-19 | University Of Pittsburgh Of The Commonwealth System Of Higher Education | Identication of peptides that facilitate uptake and cytoplasmic and/or nuclear transport of proteins, DNA and virues |
FR2816845B1 (fr) | 2000-11-20 | 2006-10-20 | Centre Nat Rech Scient | Vecteurs de transport a travers un epithelium a jonctions serrees |
US20020073441A1 (en) * | 2000-12-13 | 2002-06-13 | Ross Brian D. | Compositions and methods for detecting proteolytic activity |
FR2818982B1 (fr) * | 2000-12-29 | 2003-10-31 | Univ Rennes | Inhibiteur specifique du systeme ubiquitine-proteasome et applications therapeutiques correspondantes |
AU2002320460A1 (en) * | 2001-07-13 | 2003-01-29 | Clf Medical Technology Acceleration Program, Inc | Calcineurin modulators |
FR2829940A1 (fr) * | 2001-09-27 | 2003-03-28 | Synt Em | Compositions pour la vectorisation d'anticorps a travers la barriere hematoencephalique et leur utilisation pour le diagnostic ou le traitement des maladies du systeme nerveux central |
ATE500842T1 (de) | 2002-05-04 | 2011-03-15 | Acorda Therapeutics Inc | Zusammensetzungen und verfahren zur förderung des neuronalen wachstums |
US20040126366A1 (en) * | 2002-06-04 | 2004-07-01 | Rima Kaddurah-Daouk | Methods of treating cognitive dysfunction by modulating brain energy metabolism |
EP1947116B1 (de) * | 2003-02-10 | 2017-06-21 | 2-BBB Medicines B.V. | Differenziell exprimierte Nukleinsäuren der Blut-Hirnschranke bei einer Entzündung |
US7166692B2 (en) | 2003-03-04 | 2007-01-23 | Canbrex Bio Science Walkersville, Inc. | Intracellular delivery of small molecules, proteins, and nucleic acids |
US7959914B2 (en) | 2003-05-16 | 2011-06-14 | Acorda Therapeutics, Inc. | Methods of reducing extravasation of inflammatory cells |
MX348062B (es) | 2003-05-16 | 2017-05-26 | Acorda Therapeutics Inc | Mutantes que degradan proteoglicanos para tratamiento del snc. |
AU2004247025B8 (en) * | 2003-05-16 | 2011-06-30 | Acorda Therapeutics, Inc. | Fusion proteins for the treatment of CNS |
CN1648135A (zh) * | 2004-01-20 | 2005-08-03 | 中国人民解放军军事医学科学院毒物药物研究所 | 转导肽-人源胆碱乙酰基转移酶融合蛋白及其应用 |
MXPA06013345A (es) | 2004-05-18 | 2008-10-31 | Acorda Therapeutics Inc | Metodos para purificar condrointinasa y sus formulaciones estables. |
DK1988167T3 (da) * | 2005-02-17 | 2020-07-13 | Univ Sorbonne | Intracellulære inhiberende peptider |
EP2264458A1 (de) | 2005-04-05 | 2010-12-22 | Allergan, Inc. | Clostridintoxinaktivitätsassays |
EP1928490B8 (de) | 2005-09-26 | 2012-10-03 | Acorda Therapeutics, Inc. | Zusammensetzungen und verfahren zur verwendung von chondroitinase-abci-mutanten |
IL286053B2 (en) | 2005-10-18 | 2023-03-01 | Nat Jewish Health | A process for making red blood cells using immortal hematopoietic stem cells and erythropoietin |
AU2007307736C1 (en) | 2006-10-10 | 2014-04-10 | Acorda Therapeutics, Inc. | Compositions and methods of using chondroitinase ABCI mutants |
EP2583550A1 (de) | 2007-03-13 | 2013-04-24 | National Jewish Health | Verfahren zur Erzeugung von Antikörpern |
US8986702B2 (en) | 2008-05-16 | 2015-03-24 | Taiga Biotechnologies, Inc. | Antibodies and processes for preparing the same |
SG193145A1 (en) | 2008-07-21 | 2013-09-30 | Taiga Biotechnologies Inc | Differentiated anucleated cells and method for preparing the same |
EP2318435B1 (de) | 2008-08-28 | 2015-12-23 | Taiga Biotechnologies, Inc. | Myc-modulatoren, verfahren zu ihrer verwendung und verfahren zur identifikation von mitteln zur myc-modulierung |
EP3252068A3 (de) | 2009-10-12 | 2018-03-14 | Larry J. Smith | Verfahren und zusammensetzungen zur modulation der genexpression unter verwendung in-vivo- oder in-vitro-verabreichten arzneistoffen auf oligonukleotidbasis |
WO2012038950A1 (en) | 2010-09-20 | 2012-03-29 | Ramot At Tel-Aviv University Ltd. | Activatable toxin complexes comprising a cleavable inhibitory peptide |
EP3453762B1 (de) | 2012-05-02 | 2021-04-21 | Sirna Therapeutics, Inc. | Sina-zusammensetzungen |
CA3133302A1 (en) | 2012-07-20 | 2014-01-23 | Taiga Biotechnologies, Inc. | Enhanced reconstitution and autoreconstitution of the hematopoietic compartment comprising a myc polypeptide |
US10272115B2 (en) | 2013-03-11 | 2019-04-30 | Taiga Biotechnologies, Inc. | Production and use of red blood cells |
US9365825B2 (en) | 2013-03-11 | 2016-06-14 | Taiga Biotechnologies, Inc. | Expansion of adult stem cells in vitro |
WO2014194259A1 (en) * | 2013-05-30 | 2014-12-04 | Arizona Board Of Regents, A Body Corporate Of The State Of Arizona, Acting For And On Behalf Of Arizona State University | Methods and compositions for treating brain diseases |
AU2017367730A1 (en) | 2016-12-02 | 2019-06-06 | Taiga Biotechnologies, Inc. | Nanoparticle formulations |
CA3067851C (en) | 2017-06-22 | 2023-01-31 | Catalyst Biosciences, Inc. | Modified membrane type serine protease 1 (mtsp-1) polypeptides and methods of use |
US10149898B2 (en) | 2017-08-03 | 2018-12-11 | Taiga Biotechnologies, Inc. | Methods and compositions for the treatment of melanoma |
US11613744B2 (en) | 2018-12-28 | 2023-03-28 | Vertex Pharmaceuticals Incorporated | Modified urokinase-type plasminogen activator polypeptides and methods of use |
MX2021007843A (es) | 2018-12-28 | 2021-08-11 | Vertex Pharma | Polipeptidos de activador de plasminogeno, tipo urocinasa, modificados y metodos de uso. |
Family Cites Families (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5672683A (en) * | 1989-09-07 | 1997-09-30 | Alkermes, Inc. | Transferrin neuropharmaceutical agent fusion protein |
US5674980A (en) * | 1989-12-21 | 1997-10-07 | Biogen Inc | Fusion protein comprising tat-derived transport moiety |
US5328984A (en) * | 1991-03-04 | 1994-07-12 | The United States As Represented By The Department Of Health & Human Services | Recombinant chimeric proteins deliverable across cellular membranes into cytosol of target cells |
NZ501110A (en) * | 1997-05-15 | 2001-10-26 | Elan Corp Plc | Random peptides that bind to gastro-intestinal tract (GIT) transport receptors and related drug delivery methods |
CA2314267A1 (en) * | 1997-12-10 | 1999-06-17 | Washington University | Anti-pathogen system and methods of use thereof |
-
2000
- 2000-02-28 WO PCT/US2000/005097 patent/WO2000062067A1/en not_active Application Discontinuation
- 2000-02-28 EP EP00962058A patent/EP1157275A4/de not_active Withdrawn
- 2000-02-28 JP JP2000611079A patent/JP2003514765A/ja active Pending
- 2000-02-28 CA CA002364690A patent/CA2364690A1/en not_active Abandoned
- 2000-02-28 AU AU74970/00A patent/AU7497000A/en not_active Abandoned
Cited By (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2007527856A (ja) * | 2003-06-30 | 2007-10-04 | ユニベルシテ ド ローザンヌ | 癌細胞を選択的に死滅させるRasGAP由来ペプチド |
JP2007099707A (ja) * | 2005-10-05 | 2007-04-19 | Toagosei Co Ltd | 神経分化抑制ペプチド及びその利用 |
US7893031B2 (en) | 2005-10-05 | 2011-02-22 | Toagosei Co., Ltd. | Neuronal differentiation inhibitor peptide and use thereof |
JP4677319B2 (ja) * | 2005-10-05 | 2011-04-27 | 東亞合成株式会社 | 神経分化抑制ペプチド及びその利用 |
JP2009532045A (ja) * | 2006-04-07 | 2009-09-10 | ゲオルク−アウグスト−ウニヴェルジテート・ゲッティンゲン・シュティフトゥング・エッフェントリヒェン・レッヒツ | タンパク質置換治療のための合成mecp2配列 |
JP2010226992A (ja) * | 2009-03-26 | 2010-10-14 | Nihon Univ | レチノイン酸受容体αを含む融合タンパク質 |
JP5817038B2 (ja) * | 2009-06-22 | 2015-11-18 | 洋孝 松尾 | 尿酸トランスポーター、並びに、尿酸輸送関連疾患素因及び炎症関連疾患素因の評価方法及び評価キット、検査体及び薬 |
JP2015231993A (ja) * | 2009-06-22 | 2015-12-24 | 洋孝 松尾 | 尿酸トランスポーター、並びに、尿酸輸送関連疾患素因及び炎症関連疾患素因の評価方法及び評価キット、検査体及び薬 |
Also Published As
Publication number | Publication date |
---|---|
WO2000062067A1 (en) | 2000-10-19 |
EP1157275A1 (de) | 2001-11-28 |
WO2000062067A9 (en) | 2002-07-11 |
AU7497000A (en) | 2000-11-14 |
EP1157275A4 (de) | 2003-01-15 |
CA2364690A1 (en) | 2000-10-19 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP2003514765A (ja) | 新規形質導入分子およびその使用方法 | |
US6221355B1 (en) | Anti-pathogen system and methods of use thereof | |
JP2002531113A (ja) | 蛋白質の形質導入システムおよびその使用法 | |
BRPI0620806A2 (pt) | peptìdeos úteis como peptìdeos de penetração de célula | |
US7718610B2 (en) | Retrocyclins: antiviral and antimicrobial peptides | |
CA2996975C (en) | Methods for treatment of diseases | |
US9738878B2 (en) | HIV-1 integrase derived peptides and compositions | |
JP7276895B2 (ja) | 遺伝子発現抑制剤 | |
RU2741123C1 (ru) | Липопептид для эффективного ингибирования вич, его производное, фармацевтическая композиция и их применение | |
KR20220139079A (ko) | 세포 투과성 펩타이드 변이체 및 이의 용도 | |
JP2022549057A (ja) | 分子の細胞内送達のための複合体 | |
JP2012518417A (ja) | Pa−cardを用いて癌を予防及び/又は治療するための組成物及び方法 | |
US20050059122A1 (en) | Targeted carrier fusions for delivery of chemotherapeutic agents | |
US11186614B2 (en) | Anti-HIV peptides | |
JP4927546B2 (ja) | ヘプタペプチドパターン及び細胞透過ドメインを含む相互作用ポリペプチド | |
CA2407570A1 (en) | Compositions and methods for delivery of a molecule into a cell | |
US20030219451A1 (en) | Stable helical C peptides and uses therefor | |
WO2018141089A1 (zh) | 广谱抑制hiv的脂肽、其衍生物、其药物组合物及其用途 | |
US20040043949A1 (en) | Therapeutic system targeting pathogen proteases and uses thereof | |
ITRM20090650A1 (it) | Peptidi e loro derivati che inibiscono il rilascio extracellulare dellaproteina tat di hiv-1 e la replicazione di hiv-1 | |
US20160310567A1 (en) | Compositions for inhibiting viral replication and methods of use and production thereof | |
Carr | Anatomy of the coiled coil and its role in the conformational change of influenza hemagglutinin | |
JP2005008645A (ja) | ウィルス感染・増殖抑制剤 |