CA2598510C - Q3 sparc deletion mutant and uses thereof - Google Patents

Info

Publication number

CA2598510C

CA2598510C CA2598510A CA2598510A CA2598510C CA 2598510 C CA2598510 C CA 2598510C CA 2598510 A CA2598510 A CA 2598510A CA 2598510 A CA2598510 A CA 2598510A CA 2598510 C CA2598510 C CA 2598510C

Authority

CA

Canada

Prior art keywords

sparc

polypeptide

deletion mutant

nucleic acid

seq

Prior art date

2005-02-18

Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)

Expired - Fee Related

Links

• Espacenet
• Global Dossier
• CIPO
• Discuss

• 238000012217 deletion Methods 0.000 title abstract description 141
• 230000037430 deletion Effects 0.000 title abstract description 139
• 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 232
• 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 225
• 229920001184 polypeptide Polymers 0.000 claims abstract description 221
• 150000007523 nucleic acids Chemical class 0.000 claims abstract description 100
• 102000039446 nucleic acids Human genes 0.000 claims abstract description 79
• 108020004707 nucleic acids Proteins 0.000 claims abstract description 79
• 210000004027 cell Anatomy 0.000 claims description 98
• 239000000203 mixture Substances 0.000 claims description 52
• 230000014509 gene expression Effects 0.000 claims description 43
• 239000003814 drug Substances 0.000 claims description 28
• 239000013598 vector Substances 0.000 claims description 28
• 108091028043 Nucleic acid sequence Proteins 0.000 claims description 26
• 229940124597 therapeutic agent Drugs 0.000 claims description 18
• 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 14
• 239000003937 drug carrier Substances 0.000 claims description 12
• 229920001223 polyethylene glycol Polymers 0.000 claims description 11
• 239000002202 Polyethylene glycol Substances 0.000 claims description 10
• 229940079593 drug Drugs 0.000 claims description 9
• 238000004519 manufacturing process Methods 0.000 claims description 8
• 210000003527 eukaryotic cell Anatomy 0.000 claims description 7
• 239000003053 toxin Substances 0.000 claims description 5
• 231100000765 toxin Toxicity 0.000 claims description 5
• 230000001939 inductive effect Effects 0.000 claims description 4
• 230000001131 transforming effect Effects 0.000 claims description 4
• 210000001236 prokaryotic cell Anatomy 0.000 claims description 3
• 101710100111 SPARC Proteins 0.000 claims description 2
• 102100037599 SPARC Human genes 0.000 claims description 2
• 125000003275 alpha amino acid group Chemical group 0.000 claims 2
• 238000000034 method Methods 0.000 abstract description 115
• ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 abstract description 22
• 230000035772 mutation Effects 0.000 abstract description 14
• 101000881168 Homo sapiens SPARC Proteins 0.000 abstract description 6
• 102000045436 human SPARC Human genes 0.000 abstract description 6
• 150000001413 amino acids Chemical class 0.000 description 102
• 206010028980 Neoplasm Diseases 0.000 description 86
• 235000001014 amino acid Nutrition 0.000 description 76
• 108090000623 proteins and genes Proteins 0.000 description 74
• 229940024606 amino acid Drugs 0.000 description 68
• RCINICONZNJXQF-MZXODVADSA-N taxol Chemical compound O([C@@H]1[C@@]2(C[C@@H](C(C)=C(C2(C)C)[C@H](C([C@]2(C)[C@@H](O)C[C@H]3OC[C@]3([C@H]21)OC(C)=O)=O)OC(=O)C)OC(=O)[C@H](O)[C@@H](NC(=O)C=1C=CC=CC=1)C=1C=CC=CC=1)O)C(=O)C1=CC=CC=C1 RCINICONZNJXQF-MZXODVADSA-N 0.000 description 68
• 229960001592 paclitaxel Drugs 0.000 description 66
• 229930012538 Paclitaxel Natural products 0.000 description 63
• 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 58
• 102000004169 proteins and genes Human genes 0.000 description 58
• 201000010099 disease Diseases 0.000 description 57
• 235000018102 proteins Nutrition 0.000 description 48
• 108010088751 Albumins Proteins 0.000 description 45
• 102000009027 Albumins Human genes 0.000 description 45
• 125000003729 nucleotide group Chemical group 0.000 description 38
• 239000002773 nucleotide Substances 0.000 description 37
• 108020004414 DNA Proteins 0.000 description 35
• 210000001519 tissue Anatomy 0.000 description 34
• 239000000523 sample Substances 0.000 description 29
• 201000011510 cancer Diseases 0.000 description 25
• 230000027455 binding Effects 0.000 description 23
• 235000004554 glutamine Nutrition 0.000 description 23
• 239000012634 fragment Substances 0.000 description 20
• 238000003752 polymerase chain reaction Methods 0.000 description 20
• 230000032258 transport Effects 0.000 description 19
• ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 18
• 239000002585 base Substances 0.000 description 18
• -1 Ca 2+ Chemical class 0.000 description 17
• 241000124008 Mammalia Species 0.000 description 17
• 238000011282 treatment Methods 0.000 description 17
• 239000002246 antineoplastic agent Substances 0.000 description 16
• 210000002889 endothelial cell Anatomy 0.000 description 16
• 239000013612 plasmid Substances 0.000 description 16
• 108010012934 Albumin-Bound Paclitaxel Proteins 0.000 description 15
• 229940127089 cytotoxic agent Drugs 0.000 description 15
• 238000009472 formulation Methods 0.000 description 15
• 238000001415 gene therapy Methods 0.000 description 15
• 239000002299 complementary DNA Substances 0.000 description 14
• 238000009396 hybridization Methods 0.000 description 14
• 125000005647 linker group Chemical group 0.000 description 14
• 238000010186 staining Methods 0.000 description 14
• 238000002560 therapeutic procedure Methods 0.000 description 14
• 238000003556 assay Methods 0.000 description 13
• 239000012472 biological sample Substances 0.000 description 13
• 238000006243 chemical reaction Methods 0.000 description 13
• 239000003795 chemical substances by application Substances 0.000 description 13
• 230000004927 fusion Effects 0.000 description 13
• 230000002062 proliferating effect Effects 0.000 description 13
• 238000012163 sequencing technique Methods 0.000 description 13
• 230000001225 therapeutic effect Effects 0.000 description 13
• 108091032973 (ribonucleotides)n+m Proteins 0.000 description 12
• 108010043324 Amyloid Precursor Protein Secretases Proteins 0.000 description 12
• 102000002659 Amyloid Precursor Protein Secretases Human genes 0.000 description 12
• 238000001514 detection method Methods 0.000 description 12
• 239000008194 pharmaceutical composition Substances 0.000 description 12
• 230000004044 response Effects 0.000 description 12
• 230000014616 translation Effects 0.000 description 12
• 102000035195 Peptidases Human genes 0.000 description 11
• 108091005804 Peptidases Proteins 0.000 description 11
• 230000000295 complement effect Effects 0.000 description 11
• 235000018417 cysteine Nutrition 0.000 description 11
• 230000000694 effects Effects 0.000 description 11
• 238000001727 in vivo Methods 0.000 description 11
• 239000000243 solution Substances 0.000 description 11
• 208000026310 Breast neoplasm Diseases 0.000 description 10
• ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 10
• 101000773038 Human herpesvirus 7 (strain RK) U21 glycoprotein Proteins 0.000 description 10
• XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 10
• 108091034117 Oligonucleotide Proteins 0.000 description 10
• 239000004365 Protease Substances 0.000 description 10
• FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
• XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 10
• MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 9
• AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 9
• 241001465754 Metazoa Species 0.000 description 9
• MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 9
• AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 9
• 239000004473 Threonine Substances 0.000 description 9
• 230000008859 change Effects 0.000 description 9
• 235000004400 serine Nutrition 0.000 description 9
• 235000008521 threonine Nutrition 0.000 description 9
• 230000031998 transcytosis Effects 0.000 description 9
• 238000013519 translation Methods 0.000 description 9
• 201000001320 Atherosclerosis Diseases 0.000 description 8
• 206010006187 Breast cancer Diseases 0.000 description 8
• 235000019419 proteases Nutrition 0.000 description 8
• 230000015572 biosynthetic process Effects 0.000 description 7
• 238000003776 cleavage reaction Methods 0.000 description 7
• 239000003623 enhancer Substances 0.000 description 7
• 230000002601 intratumoral effect Effects 0.000 description 7
• 210000003734 kidney Anatomy 0.000 description 7
• 239000003446 ligand Substances 0.000 description 7
• 239000002502 liposome Substances 0.000 description 7
• 230000001404 mediated effect Effects 0.000 description 7
• 102000054765 polymorphisms of proteins Human genes 0.000 description 7
• 108091033319 polynucleotide Proteins 0.000 description 7
• 102000040430 polynucleotide Human genes 0.000 description 7
• 239000002157 polynucleotide Substances 0.000 description 7
• 230000007017 scission Effects 0.000 description 7
• 230000035945 sensitivity Effects 0.000 description 7
• 210000004881 tumor cell Anatomy 0.000 description 7
• 241000894006 Bacteria Species 0.000 description 6
• 108020004705 Codon Proteins 0.000 description 6
• 241000588724 Escherichia coli Species 0.000 description 6
• DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
• 101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 description 6
• COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 6
• KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 6
• 108700026244 Open Reading Frames Proteins 0.000 description 6
• 102100040247 Tumor necrosis factor Human genes 0.000 description 6
• KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 6
• 241000700605 Viruses Species 0.000 description 6
• 239000000427 antigen Substances 0.000 description 6
• 108091007433 antigens Proteins 0.000 description 6
• 102000036639 antigens Human genes 0.000 description 6
• 239000000969 carrier Substances 0.000 description 6
• 210000000349 chromosome Anatomy 0.000 description 6
• 150000001875 compounds Chemical class 0.000 description 6
• 230000021615 conjugation Effects 0.000 description 6
• 239000000032 diagnostic agent Substances 0.000 description 6
• 229940039227 diagnostic agent Drugs 0.000 description 6
• 108020001507 fusion proteins Proteins 0.000 description 6
• 102000037865 fusion proteins Human genes 0.000 description 6
• 238000003205 genotyping method Methods 0.000 description 6
• 230000001976 improved effect Effects 0.000 description 6
• 238000002347 injection Methods 0.000 description 6
• 239000007924 injection Substances 0.000 description 6
• 239000002105 nanoparticle Substances 0.000 description 6
• 230000002018 overexpression Effects 0.000 description 6
• 239000012071 phase Substances 0.000 description 6
• COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 6
• 102000005962 receptors Human genes 0.000 description 6
• 108020003175 receptors Proteins 0.000 description 6
• 208000037803 restenosis Diseases 0.000 description 6
• 239000004474 valine Substances 0.000 description 6
• 235000014393 valine Nutrition 0.000 description 6
• 241000710198 Foot-and-mouth disease virus Species 0.000 description 5
• WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 5
• DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 5
• CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 5
• KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 5
• 239000004472 Lysine Substances 0.000 description 5
• 241000699666 Mus <mouse, genus> Species 0.000 description 5
• 229940028652 abraxane Drugs 0.000 description 5
• 230000035508 accumulation Effects 0.000 description 5
• 238000009825 accumulation Methods 0.000 description 5
• 238000004458 analytical method Methods 0.000 description 5
• 235000003704 aspartic acid Nutrition 0.000 description 5
• OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 5
• 210000004204 blood vessel Anatomy 0.000 description 5
• 210000000481 breast Anatomy 0.000 description 5
• 230000001413 cellular effect Effects 0.000 description 5
• 230000001419 dependent effect Effects 0.000 description 5
• 230000008497 endothelial barrier function Effects 0.000 description 5
• 238000005516 engineering process Methods 0.000 description 5
• 235000013922 glutamic acid Nutrition 0.000 description 5
• 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 5
• 235000014304 histidine Nutrition 0.000 description 5
• 206010020718 hyperplasia Diseases 0.000 description 5
• 238000000338 in vitro Methods 0.000 description 5
• 239000007788 liquid Substances 0.000 description 5
• 108020004999 messenger RNA Proteins 0.000 description 5
• 238000010369 molecular cloning Methods 0.000 description 5
• 238000002703 mutagenesis Methods 0.000 description 5
• 231100000350 mutagenesis Toxicity 0.000 description 5
• 238000002360 preparation method Methods 0.000 description 5
• 230000035755 proliferation Effects 0.000 description 5
• 230000002285 radioactive effect Effects 0.000 description 5
• 150000003839 salts Chemical class 0.000 description 5
• 230000001235 sensitizing effect Effects 0.000 description 5
• 239000011780 sodium chloride Substances 0.000 description 5
• 239000007787 solid Substances 0.000 description 5
• 238000013518 transcription Methods 0.000 description 5
• 230000035897 transcription Effects 0.000 description 5
• 238000001890 transfection Methods 0.000 description 5
• 230000002792 vascular Effects 0.000 description 5
• 239000004475 Arginine Substances 0.000 description 4
• DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 4
• AOJJSUZBOXZQNB-TZSSRYMLSA-N Doxorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 AOJJSUZBOXZQNB-TZSSRYMLSA-N 0.000 description 4
• 241000196324 Embryophyta Species 0.000 description 4
• LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
• 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 4
• 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 4
• 108010043121 Green Fluorescent Proteins Proteins 0.000 description 4
• 102000004144 Green Fluorescent Proteins Human genes 0.000 description 4
• ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 4
• WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 4
• HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 4
• ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 4
• 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 4
• 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 4
• 108010039491 Ricin Proteins 0.000 description 4
• 102000002933 Thioredoxin Human genes 0.000 description 4
• 239000013543 active substance Substances 0.000 description 4
• 238000007792 addition Methods 0.000 description 4
• ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 4
• 235000009582 asparagine Nutrition 0.000 description 4
• 229960001230 asparagine Drugs 0.000 description 4
• 210000000988 bone and bone Anatomy 0.000 description 4
• 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 4
• 239000002872 contrast media Substances 0.000 description 4
• 206010012601 diabetes mellitus Diseases 0.000 description 4
• 239000012636 effector Substances 0.000 description 4
• 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 4
• 210000002744 extracellular matrix Anatomy 0.000 description 4
• 230000006870 function Effects 0.000 description 4
• 239000004220 glutamic acid Substances 0.000 description 4
• 239000005090 green fluorescent protein Substances 0.000 description 4
• 230000012010 growth Effects 0.000 description 4
• HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 4
• 230000005764 inhibitory process Effects 0.000 description 4
• 238000003780 insertion Methods 0.000 description 4
• 230000037431 insertion Effects 0.000 description 4
• 210000004185 liver Anatomy 0.000 description 4
• 210000004072 lung Anatomy 0.000 description 4
• 230000007246 mechanism Effects 0.000 description 4
• 239000012528 membrane Substances 0.000 description 4
• 210000004088 microvessel Anatomy 0.000 description 4
• 210000001672 ovary Anatomy 0.000 description 4
• 210000001938 protoplast Anatomy 0.000 description 4
• 238000002864 sequence alignment Methods 0.000 description 4
• 239000001509 sodium citrate Substances 0.000 description 4
• 206010041823 squamous cell carcinoma Diseases 0.000 description 4
• 238000006467 substitution reaction Methods 0.000 description 4
• 238000003786 synthesis reaction Methods 0.000 description 4
• 230000008685 targeting Effects 0.000 description 4
• 108060008226 thioredoxin Proteins 0.000 description 4
• 229940094937 thioredoxin Drugs 0.000 description 4
• 108700012359 toxins Proteins 0.000 description 4
• 230000009466 transformation Effects 0.000 description 4
• 210000003932 urinary bladder Anatomy 0.000 description 4
• 230000003612 virological effect Effects 0.000 description 4
• 108010077480 Albumin Receptors Proteins 0.000 description 3
• 102000053602 DNA Human genes 0.000 description 3
• 229920002307 Dextran Polymers 0.000 description 3
• 241000233866 Fungi Species 0.000 description 3
• 241000287828 Gallus gallus Species 0.000 description 3
• PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
• 239000004471 Glycine Substances 0.000 description 3
• 241000282412 Homo Species 0.000 description 3
• 102000008394 Immunoglobulin Fragments Human genes 0.000 description 3
• 108010021625 Immunoglobulin Fragments Proteins 0.000 description 3
• 206010061218 Inflammation Diseases 0.000 description 3
• QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
• AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 3
• ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
• KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 3
• FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 3
• QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical group C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 3
• OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical group OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 3
• ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
• 108010006519 Molecular Chaperones Proteins 0.000 description 3
• 206010029113 Neovascularisation Diseases 0.000 description 3
• 101710163270 Nuclease Proteins 0.000 description 3
• 208000008589 Obesity Diseases 0.000 description 3
• 241000283973 Oryctolagus cuniculus Species 0.000 description 3
• 238000012408 PCR amplification Methods 0.000 description 3
• DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 3
• 102000006010 Protein Disulfide-Isomerase Human genes 0.000 description 3
• 108020004511 Recombinant DNA Proteins 0.000 description 3
• 206010038923 Retinopathy Diseases 0.000 description 3
• 108090000829 Ribosome Inactivating Proteins Proteins 0.000 description 3
• DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 3
• 108091081024 Start codon Proteins 0.000 description 3
• 108010000499 Thromboplastin Proteins 0.000 description 3
• 102000002262 Thromboplastin Human genes 0.000 description 3
• 108060008539 Transglutaminase Proteins 0.000 description 3
• QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Chemical group C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 3
• 208000007097 Urinary Bladder Neoplasms Diseases 0.000 description 3
• 230000002159 abnormal effect Effects 0.000 description 3
• 235000004279 alanine Nutrition 0.000 description 3
• 125000003277 amino group Chemical group 0.000 description 3
• 238000009175 antibody therapy Methods 0.000 description 3
• 238000013459 approach Methods 0.000 description 3
• 125000001797 benzyl group Chemical group [H]C1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])* 0.000 description 3
• 210000004369 blood Anatomy 0.000 description 3
• 239000008280 blood Substances 0.000 description 3
• 201000008275 breast carcinoma Diseases 0.000 description 3
• 239000011575 calcium Substances 0.000 description 3
• 210000000170 cell membrane Anatomy 0.000 description 3
• 230000004663 cell proliferation Effects 0.000 description 3
• 238000002512 chemotherapy Methods 0.000 description 3
• 230000008045 co-localization Effects 0.000 description 3
• 230000001276 controlling effect Effects 0.000 description 3
• 230000006378 damage Effects 0.000 description 3
• 229960002086 dextran Drugs 0.000 description 3
• 239000006185 dispersion Substances 0.000 description 3
• 238000004520 electroporation Methods 0.000 description 3
• 230000003511 endothelial effect Effects 0.000 description 3
• 108010048367 enhanced green fluorescent protein Proteins 0.000 description 3
• 102000035175 foldases Human genes 0.000 description 3
• 108091005749 foldases Proteins 0.000 description 3
• 125000002485 formyl group Chemical group [H]C(*)=O 0.000 description 3
• 210000001035 gastrointestinal tract Anatomy 0.000 description 3
• 238000001502 gel electrophoresis Methods 0.000 description 3
• 150000002309 glutamines Chemical group 0.000 description 3
• 210000003128 head Anatomy 0.000 description 3
• 230000004054 inflammatory process Effects 0.000 description 3
• 230000003993 interaction Effects 0.000 description 3
• 238000002955 isolation Methods 0.000 description 3
• AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 3
• 229960000310 isoleucine Drugs 0.000 description 3
• 230000003902 lesion Effects 0.000 description 3
• 239000006166 lysate Substances 0.000 description 3
• 210000004962 mammalian cell Anatomy 0.000 description 3
• 239000011159 matrix material Substances 0.000 description 3
• 229930182817 methionine Natural products 0.000 description 3
• 238000000520 microinjection Methods 0.000 description 3
• 230000004048 modification Effects 0.000 description 3
• 238000012986 modification Methods 0.000 description 3
• 210000000214 mouth Anatomy 0.000 description 3
• 230000009871 nonspecific binding Effects 0.000 description 3
• 235000020824 obesity Nutrition 0.000 description 3
• 230000036961 partial effect Effects 0.000 description 3
• 210000002381 plasma Anatomy 0.000 description 3
• 239000011148 porous material Substances 0.000 description 3
• 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 3
• 238000004393 prognosis Methods 0.000 description 3
• 210000002307 prostate Anatomy 0.000 description 3
• 108020003519 protein disulfide isomerase Proteins 0.000 description 3
• 238000001959 radiotherapy Methods 0.000 description 3
• 239000011541 reaction mixture Substances 0.000 description 3
• 238000007634 remodeling Methods 0.000 description 3
• 108091008146 restriction endonucleases Proteins 0.000 description 3
• 238000007894 restriction fragment length polymorphism technique Methods 0.000 description 3
• 150000003384 small molecules Chemical class 0.000 description 3
• NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 3
• FVAUCKIRQBBSSJ-UHFFFAOYSA-M sodium iodide Chemical compound [Na+].[I-] FVAUCKIRQBBSSJ-UHFFFAOYSA-M 0.000 description 3
• 210000004872 soft tissue Anatomy 0.000 description 3
• 241000894007 species Species 0.000 description 3
• 230000009870 specific binding Effects 0.000 description 3
• 230000004936 stimulating effect Effects 0.000 description 3
• 239000000725 suspension Substances 0.000 description 3
• 102000003601 transglutaminase Human genes 0.000 description 3
• 230000007723 transport mechanism Effects 0.000 description 3
• OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Chemical group OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 3
• 239000013603 viral vector Substances 0.000 description 3
• 238000005406 washing Methods 0.000 description 3
• 238000001262 western blot Methods 0.000 description 3
• 241000251468 Actinopterygii Species 0.000 description 2
• IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
• 241000972773 Aulopiformes Species 0.000 description 2
• 206010004446 Benign prostatic hyperplasia Diseases 0.000 description 2
• 241000283690 Bos taurus Species 0.000 description 2
• 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
• 206010055113 Breast cancer metastatic Diseases 0.000 description 2
• OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 2
• 241000283707 Capra Species 0.000 description 2
• 201000009030 Carcinoma Diseases 0.000 description 2
• 102000003727 Caveolin 1 Human genes 0.000 description 2
• 108090000026 Caveolin 1 Proteins 0.000 description 2
• 241000700199 Cavia porcellus Species 0.000 description 2
• 108091026890 Coding region Proteins 0.000 description 2
• 241000699800 Cricetinae Species 0.000 description 2
• 238000007399 DNA isolation Methods 0.000 description 2
• 102000004190 Enzymes Human genes 0.000 description 2
• 108090000790 Enzymes Proteins 0.000 description 2
• GHASVSINZRGABV-UHFFFAOYSA-N Fluorouracil Chemical compound FC1=CNC(=O)NC1=O GHASVSINZRGABV-UHFFFAOYSA-N 0.000 description 2
• 206010051920 Glomerulonephropathy Diseases 0.000 description 2
• 108010070675 Glutathione transferase Proteins 0.000 description 2
• 102000005720 Glutathione transferase Human genes 0.000 description 2
• 108010091358 Hypoxanthine Phosphoribosyltransferase Proteins 0.000 description 2
• 239000002616 MRI contrast agent Substances 0.000 description 2
• 102000005431 Molecular Chaperones Human genes 0.000 description 2
• 241000699670 Mus sp. Species 0.000 description 2
• 241000272144 Naja atra Species 0.000 description 2
• 238000000636 Northern blotting Methods 0.000 description 2
• 108010077077 Osteonectin Proteins 0.000 description 2
• 102000009890 Osteonectin Human genes 0.000 description 2
• 206010033128 Ovarian cancer Diseases 0.000 description 2
• 206010061535 Ovarian neoplasm Diseases 0.000 description 2
• 241001494479 Pecora Species 0.000 description 2
• 108091093037 Peptide nucleic acid Proteins 0.000 description 2
• 229920002873 Polyethylenimine Polymers 0.000 description 2
• ATUOYWHBWRKTHZ-UHFFFAOYSA-N Propane Chemical compound CCC ATUOYWHBWRKTHZ-UHFFFAOYSA-N 0.000 description 2
• 208000004403 Prostatic Hyperplasia Diseases 0.000 description 2
• 108010076504 Protein Sorting Signals Proteins 0.000 description 2
• 108020005067 RNA Splice Sites Proteins 0.000 description 2
• 241000700159 Rattus Species 0.000 description 2
• 206010070834 Sensitisation Diseases 0.000 description 2
• 108700005078 Synthetic Genes Proteins 0.000 description 2
• 108091005735 TGF-beta receptors Proteins 0.000 description 2
• 102000016715 Transforming Growth Factor beta Receptors Human genes 0.000 description 2
• XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
• 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 description 2
• 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 2
• 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 2
• 208000024248 Vascular System injury Diseases 0.000 description 2
• 208000012339 Vascular injury Diseases 0.000 description 2
• 230000002378 acidificating effect Effects 0.000 description 2
• RJURFGZVJUQBHK-UHFFFAOYSA-N actinomycin D Natural products CC1OC(=O)C(C(C)C)N(C)C(=O)CN(C)C(=O)C2CCCN2C(=O)C(C(C)C)NC(=O)C1NC(=O)C1=C(N)C(=O)C(C)=C2OC(C(C)=CC=C3C(=O)NC4C(=O)NC(C(N5CCCC5C(=O)N(C)CC(=O)N(C)C(C(C)C)C(=O)OC4C)=O)C(C)C)=C3N=C21 RJURFGZVJUQBHK-UHFFFAOYSA-N 0.000 description 2
• 230000009471 action Effects 0.000 description 2
• 239000004480 active ingredient Substances 0.000 description 2
• 239000000443 aerosol Substances 0.000 description 2
• 238000001042 affinity chromatography Methods 0.000 description 2
• 125000001931 aliphatic group Chemical group 0.000 description 2
• 150000001408 amides Chemical class 0.000 description 2
• 230000033115 angiogenesis Effects 0.000 description 2
• 238000000137 annealing Methods 0.000 description 2
• 239000007864 aqueous solution Substances 0.000 description 2
• 125000003118 aryl group Chemical group 0.000 description 2
• 230000003143 atherosclerotic effect Effects 0.000 description 2
• 108010027375 bacterioferritin Proteins 0.000 description 2
• 230000004071 biological effect Effects 0.000 description 2
• 229960000074 biopharmaceutical Drugs 0.000 description 2
• 238000001574 biopsy Methods 0.000 description 2
• 229940098773 bovine serum albumin Drugs 0.000 description 2
• 210000004556 brain Anatomy 0.000 description 2
• 239000000872 buffer Substances 0.000 description 2
• 229960005069 calcium Drugs 0.000 description 2
• 229910052791 calcium Inorganic materials 0.000 description 2
• 239000001506 calcium phosphate Substances 0.000 description 2
• 229960001714 calcium phosphate Drugs 0.000 description 2
• 229910000389 calcium phosphate Inorganic materials 0.000 description 2
• 235000011010 calcium phosphates Nutrition 0.000 description 2
• 210000003679 cervix uteri Anatomy 0.000 description 2
• 230000003196 chaotropic effect Effects 0.000 description 2
• 230000000973 chemotherapeutic effect Effects 0.000 description 2
• 238000010367 cloning Methods 0.000 description 2
• 230000024203 complement activation Effects 0.000 description 2
• 230000008878 coupling Effects 0.000 description 2
• 238000010168 coupling process Methods 0.000 description 2
• 238000005859 coupling reaction Methods 0.000 description 2
• 238000004132 cross linking Methods 0.000 description 2
• 210000004748 cultured cell Anatomy 0.000 description 2
• 210000000805 cytoplasm Anatomy 0.000 description 2
• 229940124447 delivery agent Drugs 0.000 description 2
• 229960000633 dextran sulfate Drugs 0.000 description 2
• 210000002249 digestive system Anatomy 0.000 description 2
• 239000000975 dye Substances 0.000 description 2
• 239000002961 echo contrast media Substances 0.000 description 2
• 230000002708 enhancing effect Effects 0.000 description 2
• 229940088598 enzyme Drugs 0.000 description 2
• 210000002919 epithelial cell Anatomy 0.000 description 2
• 235000019688 fish Nutrition 0.000 description 2
• 238000002866 fluorescence resonance energy transfer Methods 0.000 description 2
• 239000007850 fluorescent dye Substances 0.000 description 2
• 229960002949 fluorouracil Drugs 0.000 description 2
• 239000000499 gel Substances 0.000 description 2
• 239000003102 growth factor Substances 0.000 description 2
• 201000010536 head and neck cancer Diseases 0.000 description 2
• 208000014829 head and neck neoplasm Diseases 0.000 description 2
• 238000004128 high performance liquid chromatography Methods 0.000 description 2
• 210000005260 human cell Anatomy 0.000 description 2
• 230000002390 hyperplastic effect Effects 0.000 description 2
• 230000028993 immune response Effects 0.000 description 2
• 210000000987 immune system Anatomy 0.000 description 2
• 238000003018 immunoassay Methods 0.000 description 2
• 230000005847 immunogenicity Effects 0.000 description 2
• 210000003000 inclusion body Anatomy 0.000 description 2
• 238000010348 incorporation Methods 0.000 description 2
• 230000003834 intracellular effect Effects 0.000 description 2
• 238000007912 intraperitoneal administration Methods 0.000 description 2
• 238000001990 intravenous administration Methods 0.000 description 2
• 238000006317 isomerization reaction Methods 0.000 description 2
• 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 2
• 230000000670 limiting effect Effects 0.000 description 2
• 239000003550 marker Substances 0.000 description 2
• 238000004949 mass spectrometry Methods 0.000 description 2
• 210000003584 mesangial cell Anatomy 0.000 description 2
• 230000002503 metabolic effect Effects 0.000 description 2
• 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 2
• 238000002493 microarray Methods 0.000 description 2
• 244000005700 microbiome Species 0.000 description 2
• 125000004123 n-propyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])* 0.000 description 2
• 230000003472 neutralizing effect Effects 0.000 description 2
• 230000009972 noncorrosive effect Effects 0.000 description 2
• 210000004940 nucleus Anatomy 0.000 description 2
• 210000000056 organ Anatomy 0.000 description 2
• 230000002611 ovarian Effects 0.000 description 2
• 238000007911 parenteral administration Methods 0.000 description 2
• 230000008506 pathogenesis Effects 0.000 description 2
• 230000037361 pathway Effects 0.000 description 2
• 230000006320 pegylation Effects 0.000 description 2
• 238000002823 phage display Methods 0.000 description 2
• 239000000546 pharmaceutical excipient Substances 0.000 description 2
• 230000001766 physiological effect Effects 0.000 description 2
• 239000008389 polyethoxylated castor oil Substances 0.000 description 2
• 239000005020 polyethylene terephthalate Substances 0.000 description 2
• 239000001267 polyvinylpyrrolidone Substances 0.000 description 2
• 229920000036 polyvinylpyrrolidone Polymers 0.000 description 2
• 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 2
• 230000004481 post-translational protein modification Effects 0.000 description 2
• 239000000843 powder Substances 0.000 description 2
• 239000003755 preservative agent Substances 0.000 description 2
• 230000008569 process Effects 0.000 description 2
• 108020001580 protein domains Proteins 0.000 description 2
• 238000001243 protein synthesis Methods 0.000 description 2
• 230000017854 proteolysis Effects 0.000 description 2
• 238000010791 quenching Methods 0.000 description 2
• 230000007115 recruitment Effects 0.000 description 2
• 230000009467 reduction Effects 0.000 description 2
• 230000001105 regulatory effect Effects 0.000 description 2
• 210000002345 respiratory system Anatomy 0.000 description 2
• 230000001177 retroviral effect Effects 0.000 description 2
• 238000003757 reverse transcription PCR Methods 0.000 description 2
• 230000002441 reversible effect Effects 0.000 description 2
• 229960004641 rituximab Drugs 0.000 description 2
• 235000019515 salmon Nutrition 0.000 description 2
• 102000014452 scavenger receptors Human genes 0.000 description 2
• 108010078070 scavenger receptors Proteins 0.000 description 2
• 230000028327 secretion Effects 0.000 description 2
• 230000008313 sensitization Effects 0.000 description 2
• 239000002356 single layer Substances 0.000 description 2
• 238000002741 site-directed mutagenesis Methods 0.000 description 2
• 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
• 239000001488 sodium phosphate Substances 0.000 description 2
• 229910000162 sodium phosphate Inorganic materials 0.000 description 2
• 239000002904 solvent Substances 0.000 description 2
• 230000007480 spreading Effects 0.000 description 2
• 238000003892 spreading Methods 0.000 description 2
• 238000003860 storage Methods 0.000 description 2
• 239000000126 substance Substances 0.000 description 2
• 235000000346 sugar Nutrition 0.000 description 2
• 208000024891 symptom Diseases 0.000 description 2
• 230000002194 synthesizing effect Effects 0.000 description 2
• 230000010474 transient expression Effects 0.000 description 2
• 230000005945 translocation Effects 0.000 description 2
• 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 2
• GETQZCLCWQTVFV-UHFFFAOYSA-N trimethylamine Chemical compound CN(C)C GETQZCLCWQTVFV-UHFFFAOYSA-N 0.000 description 2
• RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 2
• 230000004614 tumor growth Effects 0.000 description 2
• 241000701161 unidentified adenovirus Species 0.000 description 2
• 230000002485 urinary effect Effects 0.000 description 2
• 210000004509 vascular smooth muscle cell Anatomy 0.000 description 2
• 210000003462 vein Anatomy 0.000 description 2
• XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
• BMKDZUISNHGIBY-ZETCQYMHSA-N (+)-dexrazoxane Chemical compound C([C@H](C)N1CC(=O)NC(=O)C1)N1CC(=O)NC(=O)C1 BMKDZUISNHGIBY-ZETCQYMHSA-N 0.000 description 1
• WRLUODMOTSXWIP-BYPYZUCNSA-N (2s)-5-(diaminomethylideneamino)-2-nitramidopentanoic acid Chemical compound NC(=N)NCCC[C@@H](C(O)=O)N[N+]([O-])=O WRLUODMOTSXWIP-BYPYZUCNSA-N 0.000 description 1
• FPVKHBSQESCIEP-UHFFFAOYSA-N (8S)-3-(2-deoxy-beta-D-erythro-pentofuranosyl)-3,6,7,8-tetrahydroimidazo[4,5-d][1,3]diazepin-8-ol Natural products C1C(O)C(CO)OC1N1C(NC=NCC2O)=C2N=C1 FPVKHBSQESCIEP-UHFFFAOYSA-N 0.000 description 1
• FDKXTQMXEQVLRF-ZHACJKMWSA-N (E)-dacarbazine Chemical compound CN(C)\N=N\c1[nH]cnc1C(N)=O FDKXTQMXEQVLRF-ZHACJKMWSA-N 0.000 description 1
• UUUHXMGGBIUAPW-UHFFFAOYSA-N 1-[1-[2-[[5-amino-2-[[1-[5-(diaminomethylideneamino)-2-[[1-[3-(1h-indol-3-yl)-2-[(5-oxopyrrolidine-2-carbonyl)amino]propanoyl]pyrrolidine-2-carbonyl]amino]pentanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-methylpentanoyl]pyrrolidine-2-carbon Chemical compound C1CCC(C(=O)N2C(CCC2)C(O)=O)N1C(=O)C(C(C)CC)NC(=O)C(CCC(N)=O)NC(=O)C1CCCN1C(=O)C(CCCN=C(N)N)NC(=O)C1CCCN1C(=O)C(CC=1C2=CC=CC=C2NC=1)NC(=O)C1CCC(=O)N1 UUUHXMGGBIUAPW-UHFFFAOYSA-N 0.000 description 1
• VSNHCAURESNICA-NJFSPNSNSA-N 1-oxidanylurea Chemical compound N[14C](=O)NO VSNHCAURESNICA-NJFSPNSNSA-N 0.000 description 1
• QZDDFQLIQRYMBV-UHFFFAOYSA-N 2-[3-nitro-2-(2-nitrophenyl)-4-oxochromen-8-yl]acetic acid Chemical compound OC(=O)CC1=CC=CC(C(C=2[N+]([O-])=O)=O)=C1OC=2C1=CC=CC=C1[N+]([O-])=O QZDDFQLIQRYMBV-UHFFFAOYSA-N 0.000 description 1
• ZRUVPQAHQFHMQG-UHFFFAOYSA-N 2-[[amino(hydrazinyl)methylidene]amino]butanoic acid Chemical compound CCC(C(O)=O)N=C(N)NN ZRUVPQAHQFHMQG-UHFFFAOYSA-N 0.000 description 1
• OZDAOHVKBFBBMZ-UHFFFAOYSA-N 2-aminopentanedioic acid;hydrate Chemical compound O.OC(=O)C(N)CCC(O)=O OZDAOHVKBFBBMZ-UHFFFAOYSA-N 0.000 description 1
• WYWHKKSPHMUBEB-UHFFFAOYSA-N 6-Mercaptoguanine Natural products N1C(N)=NC(=S)C2=C1N=CN2 WYWHKKSPHMUBEB-UHFFFAOYSA-N 0.000 description 1
• YSFGBPCBPNVLOK-UHFFFAOYSA-N 6-hydroxy-2-methylhex-2-enamide Chemical compound NC(=O)C(C)=CCCCO YSFGBPCBPNVLOK-UHFFFAOYSA-N 0.000 description 1
• STQGQHZAVUOBTE-UHFFFAOYSA-N 7-Cyan-hept-2t-en-4,6-diinsaeure Natural products C1=2C(O)=C3C(=O)C=4C(OC)=CC=CC=4C(=O)C3=C(O)C=2CC(O)(C(C)=O)CC1OC1CC(N)C(O)C(C)O1 STQGQHZAVUOBTE-UHFFFAOYSA-N 0.000 description 1
• 108010066676 Abrin Proteins 0.000 description 1
• 208000024893 Acute lymphoblastic leukemia Diseases 0.000 description 1
• 208000014697 Acute lymphocytic leukaemia Diseases 0.000 description 1
• 208000031261 Acute myeloid leukaemia Diseases 0.000 description 1
• ORILYTVJVMAKLC-UHFFFAOYSA-N Adamantane Natural products C1C(C2)CC3CC1CC2C3 ORILYTVJVMAKLC-UHFFFAOYSA-N 0.000 description 1
• 108700028369 Alleles Proteins 0.000 description 1
• 102100022749 Aminopeptidase N Human genes 0.000 description 1
• QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
• 108091093088 Amplicon Proteins 0.000 description 1
• 108010074415 Angiogenic Proteins Proteins 0.000 description 1
• 102000008076 Angiogenic Proteins Human genes 0.000 description 1
• 108020000948 Antisense Oligonucleotides Proteins 0.000 description 1
• 108020005544 Antisense RNA Proteins 0.000 description 1
• 208000002109 Argyria Diseases 0.000 description 1
• 102000015790 Asparaginase Human genes 0.000 description 1
• 108010024976 Asparaginase Proteins 0.000 description 1
• 241000228254 Aspergillus restrictus Species 0.000 description 1
• 101000669426 Aspergillus restrictus Ribonuclease mitogillin Proteins 0.000 description 1
• 241000271566 Aves Species 0.000 description 1
• 208000010839 B-cell chronic lymphocytic leukemia Diseases 0.000 description 1
• 208000032791 BCR-ABL1 positive chronic myelogenous leukemia Diseases 0.000 description 1
• 206010005003 Bladder cancer Diseases 0.000 description 1
• 108010006654 Bleomycin Proteins 0.000 description 1
• 241000255789 Bombyx mori Species 0.000 description 1
• 102100028728 Bone morphogenetic protein 1 Human genes 0.000 description 1
• 108090000654 Bone morphogenetic protein 1 Proteins 0.000 description 1
• 238000009010 Bradford assay Methods 0.000 description 1
• COVZYZSDYWQREU-UHFFFAOYSA-N Busulfan Chemical compound CS(=O)(=O)OCCCCOS(C)(=O)=O COVZYZSDYWQREU-UHFFFAOYSA-N 0.000 description 1
• 108010049990 CD13 Antigens Proteins 0.000 description 1
• 102100032912 CD44 antigen Human genes 0.000 description 1
• 208000004434 Calcinosis Diseases 0.000 description 1
• BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 1
• 102000005701 Calcium-Binding Proteins Human genes 0.000 description 1
• 108010045403 Calcium-Binding Proteins Proteins 0.000 description 1
• KLWPJMFMVPTNCC-UHFFFAOYSA-N Camptothecin Natural products CCC1(O)C(=O)OCC2=C1C=C3C4Nc5ccccc5C=C4CN3C2=O KLWPJMFMVPTNCC-UHFFFAOYSA-N 0.000 description 1
• GAGWJHPBXLXJQN-UORFTKCHSA-N Capecitabine Chemical compound C1=C(F)C(NC(=O)OCCCCC)=NC(=O)N1[C@H]1[C@H](O)[C@H](O)[C@@H](C)O1 GAGWJHPBXLXJQN-UORFTKCHSA-N 0.000 description 1
• GAGWJHPBXLXJQN-UHFFFAOYSA-N Capecitabine Natural products C1=C(F)C(NC(=O)OCCCCC)=NC(=O)N1C1C(O)C(O)C(C)O1 GAGWJHPBXLXJQN-UHFFFAOYSA-N 0.000 description 1
• DLGOEMSEDOSKAD-UHFFFAOYSA-N Carmustine Chemical compound ClCCNC(=O)N(N=O)CCCl DLGOEMSEDOSKAD-UHFFFAOYSA-N 0.000 description 1
• 102000014914 Carrier Proteins Human genes 0.000 description 1
• 108010078791 Carrier Proteins Proteins 0.000 description 1
• 108090000994 Catalytic RNA Proteins 0.000 description 1
• 102000053642 Catalytic RNA Human genes 0.000 description 1
• 229940123587 Cell cycle inhibitor Drugs 0.000 description 1
• 231100000023 Cell-mediated cytotoxicity Toxicity 0.000 description 1
• 206010057250 Cell-mediated cytotoxicity Diseases 0.000 description 1
• JWBOIMRXGHLCPP-UHFFFAOYSA-N Chloditan Chemical compound C=1C=CC=C(Cl)C=1C(C(Cl)Cl)C1=CC=C(Cl)C=C1 JWBOIMRXGHLCPP-UHFFFAOYSA-N 0.000 description 1
• 108010035563 Chloramphenicol O-acetyltransferase Proteins 0.000 description 1
• 208000010833 Chronic myeloid leukaemia Diseases 0.000 description 1
• 108091062157 Cis-regulatory element Proteins 0.000 description 1
• 108010035532 Collagen Proteins 0.000 description 1
• 102000008186 Collagen Human genes 0.000 description 1
• 102000012422 Collagen Type I Human genes 0.000 description 1
• 108010022452 Collagen Type I Proteins 0.000 description 1
• 108020004635 Complementary DNA Proteins 0.000 description 1
• 108091035707 Consensus sequence Proteins 0.000 description 1
• 229920000858 Cyclodextrin Polymers 0.000 description 1
• CMSMOCZEIVJLDB-UHFFFAOYSA-N Cyclophosphamide Chemical compound ClCCN(CCCl)P1(=O)NCCCO1 CMSMOCZEIVJLDB-UHFFFAOYSA-N 0.000 description 1
• UHDGCWIWMRVCDJ-CCXZUQQUSA-N Cytarabine Chemical compound O=C1N=C(N)C=CN1[C@H]1[C@@H](O)[C@H](O)[C@@H](CO)O1 UHDGCWIWMRVCDJ-CCXZUQQUSA-N 0.000 description 1
• 101710112752 Cytotoxin Proteins 0.000 description 1
• FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
• 238000000018 DNA microarray Methods 0.000 description 1
• 230000009946 DNA mutation Effects 0.000 description 1
• 230000006820 DNA synthesis Effects 0.000 description 1
• 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
• 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
• 108010092160 Dactinomycin Proteins 0.000 description 1
• 108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 1
• 241000702421 Dependoparvovirus Species 0.000 description 1
• 239000004338 Dichlorodifluoromethane Substances 0.000 description 1
• 102000016622 Dipeptidyl Peptidase 4 Human genes 0.000 description 1
• 108010053187 Diphtheria Toxin Proteins 0.000 description 1
• 102000016607 Diphtheria Toxin Human genes 0.000 description 1
• 101710106383 Disulfide bond formation protein B Proteins 0.000 description 1
• 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
• KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
• 238000002965 ELISA Methods 0.000 description 1
• 241000710188 Encephalomyocarditis virus Species 0.000 description 1
• 201000009273 Endometriosis Diseases 0.000 description 1
• 102100031780 Endonuclease Human genes 0.000 description 1
• 108010041308 Endothelial Growth Factors Proteins 0.000 description 1
• 108091029865 Exogenous DNA Proteins 0.000 description 1
• 229920001917 Ficoll Polymers 0.000 description 1
• 108090000652 Flap endonucleases Proteins 0.000 description 1
• 102000004150 Flap endonucleases Human genes 0.000 description 1
• 208000000666 Fowlpox Diseases 0.000 description 1
• 108010093031 Galactosidases Proteins 0.000 description 1
• 102000002464 Galactosidases Human genes 0.000 description 1
• 108700004714 Gelonium multiflorum GEL Proteins 0.000 description 1
• 101000930822 Giardia intestinalis Dipeptidyl-peptidase 4 Proteins 0.000 description 1
• 208000032612 Glial tumor Diseases 0.000 description 1
• 206010018338 Glioma Diseases 0.000 description 1
• 208000022461 Glomerular disease Diseases 0.000 description 1
• WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
• 102000003886 Glycoproteins Human genes 0.000 description 1
• 108090000288 Glycoproteins Proteins 0.000 description 1
• 108060005986 Granzyme Proteins 0.000 description 1
• 102000001398 Granzyme Human genes 0.000 description 1
• 102000009465 Growth Factor Receptors Human genes 0.000 description 1
• 108010009202 Growth Factor Receptors Proteins 0.000 description 1
• 102100023737 GrpE protein homolog 1, mitochondrial Human genes 0.000 description 1
• 241000175212 Herpesvirales Species 0.000 description 1
• 241000238631 Hexapoda Species 0.000 description 1
• 208000017604 Hodgkin disease Diseases 0.000 description 1
• 208000010747 Hodgkins lymphoma Diseases 0.000 description 1
• 101000868273 Homo sapiens CD44 antigen Proteins 0.000 description 1
• 101000829489 Homo sapiens GrpE protein homolog 1, mitochondrial Proteins 0.000 description 1
• 101000608935 Homo sapiens Leukosialin Proteins 0.000 description 1
• 101100478240 Homo sapiens SPARC gene Proteins 0.000 description 1
• 101000851376 Homo sapiens Tumor necrosis factor receptor superfamily member 8 Proteins 0.000 description 1
• 108091006905 Human Serum Albumin Proteins 0.000 description 1
• 102000008100 Human Serum Albumin Human genes 0.000 description 1
• 206010020880 Hypertrophy Diseases 0.000 description 1
• 102100029098 Hypoxanthine-guanine phosphoribosyltransferase Human genes 0.000 description 1
• HEFNNWSXXWATRW-UHFFFAOYSA-N Ibuprofen Chemical compound CC(C)CC1=CC=C(C(C)C(O)=O)C=C1 HEFNNWSXXWATRW-UHFFFAOYSA-N 0.000 description 1
• XDXDZDZNSLXDNA-TZNDIEGXSA-N Idarubicin Chemical compound C1[C@H](N)[C@H](O)[C@H](C)O[C@H]1O[C@@H]1C2=C(O)C(C(=O)C3=CC=CC=C3C3=O)=C3C(O)=C2C[C@@](O)(C(C)=O)C1 XDXDZDZNSLXDNA-TZNDIEGXSA-N 0.000 description 1
• XDXDZDZNSLXDNA-UHFFFAOYSA-N Idarubicin Natural products C1C(N)C(O)C(C)OC1OC1C2=C(O)C(C(=O)C3=CC=CC=C3C3=O)=C3C(O)=C2CC(O)(C(C)=O)C1 XDXDZDZNSLXDNA-UHFFFAOYSA-N 0.000 description 1
• DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
• 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
• 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
• 229930010555 Inosine Natural products 0.000 description 1
• UGQMRVRMYYASKQ-KQYNXXCUSA-N Inosine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C2=NC=NC(O)=C2N=C1 UGQMRVRMYYASKQ-KQYNXXCUSA-N 0.000 description 1
• 102000010781 Interleukin-6 Receptors Human genes 0.000 description 1
• 108010038501 Interleukin-6 Receptors Proteins 0.000 description 1
• 108010063738 Interleukins Proteins 0.000 description 1
• 102000015696 Interleukins Human genes 0.000 description 1
• 108091092195 Intron Proteins 0.000 description 1
• 102000004195 Isomerases Human genes 0.000 description 1
• 108090000769 Isomerases Proteins 0.000 description 1
• AHLPHDHHMVZTML-BYPYZUCNSA-N L-Ornithine Chemical compound NCCC[C@H](N)C(O)=O AHLPHDHHMVZTML-BYPYZUCNSA-N 0.000 description 1
• 108010092694 L-Selectin Proteins 0.000 description 1
• ZGUNAGUHMKGQNY-ZETCQYMHSA-N L-alpha-phenylglycine zwitterion Chemical group OC(=O)[C@@H](N)C1=CC=CC=C1 ZGUNAGUHMKGQNY-ZETCQYMHSA-N 0.000 description 1
• FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 1
• 102100033467 L-selectin Human genes 0.000 description 1
• 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 1
• 241000254158 Lampyridae Species 0.000 description 1
• 206010023825 Laryngeal cancer Diseases 0.000 description 1
• 101710180643 Leishmanolysin Proteins 0.000 description 1
• 241001071864 Lethrinus laticaudis Species 0.000 description 1
• 102100039564 Leukosialin Human genes 0.000 description 1
• 102000003960 Ligases Human genes 0.000 description 1
• 108090000364 Ligases Proteins 0.000 description 1
• GQYIWUVLTXOXAJ-UHFFFAOYSA-N Lomustine Chemical compound ClCCN(N=O)C(=O)NC1CCCCC1 GQYIWUVLTXOXAJ-UHFFFAOYSA-N 0.000 description 1
• 108060001084 Luciferase Proteins 0.000 description 1
• 239000005089 Luciferase Substances 0.000 description 1
• 208000031422 Lymphocytic Chronic B-Cell Leukemia Diseases 0.000 description 1
• 206010025323 Lymphomas Diseases 0.000 description 1
• 108010000684 Matrix Metalloproteinases Proteins 0.000 description 1
• 102000002274 Matrix Metalloproteinases Human genes 0.000 description 1
• 206010066453 Mesangioproliferative glomerulonephritis Diseases 0.000 description 1
• 206010027452 Metastases to bone Diseases 0.000 description 1
• 206010027454 Metastases to breast Diseases 0.000 description 1
• 229930192392 Mitomycin Natural products 0.000 description 1
• 208000034578 Multiple myelomas Diseases 0.000 description 1
• 241001529936 Murinae Species 0.000 description 1
• 208000033761 Myelogenous Chronic BCR-ABL Positive Leukemia Diseases 0.000 description 1
• 208000033776 Myeloid Acute Leukemia Diseases 0.000 description 1
• NWIBSHFKIJFRCO-WUDYKRTCSA-N Mytomycin Chemical compound C1N2C(C(C(C)=C(N)C3=O)=O)=C3[C@@H](COC(N)=O)[C@@]2(OC)[C@@H]2[C@H]1N2 NWIBSHFKIJFRCO-WUDYKRTCSA-N 0.000 description 1
• ZDZOTLJHXYCWBA-VCVYQWHSSA-N N-debenzoyl-N-(tert-butoxycarbonyl)-10-deacetyltaxol Chemical compound O([C@H]1[C@H]2[C@@](C([C@H](O)C3=C(C)[C@@H](OC(=O)[C@H](O)[C@@H](NC(=O)OC(C)(C)C)C=4C=CC=CC=4)C[C@]1(O)C3(C)C)=O)(C)[C@@H](O)C[C@H]1OC[C@]12OC(=O)C)C(=O)C1=CC=CC=C1 ZDZOTLJHXYCWBA-VCVYQWHSSA-N 0.000 description 1
• 108090000970 Nardilysin Proteins 0.000 description 1
• 102100021850 Nardilysin Human genes 0.000 description 1
• 229930193140 Neomycin Natural products 0.000 description 1
• 206010029260 Neuroblastoma Diseases 0.000 description 1
• 108090000812 Neurolysin Proteins 0.000 description 1
• 208000015914 Non-Hodgkin lymphomas Diseases 0.000 description 1
• 241001195348 Nusa Species 0.000 description 1
• 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
• AHLPHDHHMVZTML-UHFFFAOYSA-N Orn-delta-NH2 Natural products NCCCC(N)C(O)=O AHLPHDHHMVZTML-UHFFFAOYSA-N 0.000 description 1
• UTJLXEIPEHZYQJ-UHFFFAOYSA-N Ornithine Natural products OC(=O)C(C)CCCN UTJLXEIPEHZYQJ-UHFFFAOYSA-N 0.000 description 1
• 239000002033 PVDF binder Substances 0.000 description 1
• 208000000821 Parathyroid Neoplasms Diseases 0.000 description 1
• 235000019483 Peanut oil Nutrition 0.000 description 1
• 108010077524 Peptide Elongation Factor 1 Proteins 0.000 description 1
• 102000004270 Peptidyl-Dipeptidase A Human genes 0.000 description 1
• 108090000882 Peptidyl-Dipeptidase A Proteins 0.000 description 1
• 108010002747 Pfu DNA polymerase Proteins 0.000 description 1
• 108010010677 Phosphodiesterase I Proteins 0.000 description 1
• 231100000742 Plant toxin Toxicity 0.000 description 1
• 206010035226 Plasma cell myeloma Diseases 0.000 description 1
• 108010022233 Plasminogen Activator Inhibitor 1 Proteins 0.000 description 1
• 102100039418 Plasminogen activator inhibitor 1 Human genes 0.000 description 1
• 108010076039 Polyproteins Proteins 0.000 description 1
• ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
• 208000006664 Precursor Cell Lymphoblastic Leukemia-Lymphoma Diseases 0.000 description 1
• 101710116318 Probable disulfide formation protein Proteins 0.000 description 1
• 108010050808 Procollagen Proteins 0.000 description 1
• ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
• 108700033844 Pseudomonas aeruginosa toxA Proteins 0.000 description 1
• 102100033192 Puromycin-sensitive aminopeptidase Human genes 0.000 description 1
• 108090001002 Pyroglutamyl-peptidase II Proteins 0.000 description 1
• 102000004892 Pyroglutamyl-peptidase II Human genes 0.000 description 1
• 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
• 238000003559 RNA-seq method Methods 0.000 description 1
• 108091030071 RNAI Proteins 0.000 description 1
• 208000017442 Retinal disease Diseases 0.000 description 1
• 241000283984 Rodentia Species 0.000 description 1
• 108700015859 SPARC family Proteins 0.000 description 1
• 101150036757 SPARC gene Proteins 0.000 description 1
• 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
• 240000003946 Saponaria officinalis Species 0.000 description 1
• 108010084592 Saporins Proteins 0.000 description 1
• 206010039491 Sarcoma Diseases 0.000 description 1
• 238000012300 Sequence Analysis Methods 0.000 description 1
• 208000021712 Soft tissue sarcoma Diseases 0.000 description 1
• 238000002105 Southern blotting Methods 0.000 description 1
• 229930006000 Sucrose Natural products 0.000 description 1
• CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
• 229940123237 Taxane Drugs 0.000 description 1
• 102100031293 Thimet oligopeptidase Human genes 0.000 description 1
• FOCVUCIESVLUNU-UHFFFAOYSA-N Thiotepa Chemical compound C1CN1P(N1CC1)(=S)N1CC1 FOCVUCIESVLUNU-UHFFFAOYSA-N 0.000 description 1
• 108090000190 Thrombin Proteins 0.000 description 1
• 108010046722 Thrombospondin 1 Proteins 0.000 description 1
• 102100036034 Thrombospondin-1 Human genes 0.000 description 1
• 102000003978 Tissue Plasminogen Activator Human genes 0.000 description 1
• 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 1
• 102100037116 Transcription elongation factor 1 homolog Human genes 0.000 description 1
• 102000006747 Transforming Growth Factor alpha Human genes 0.000 description 1
• 108010009583 Transforming Growth Factors Proteins 0.000 description 1
• 102000009618 Transforming Growth Factors Human genes 0.000 description 1
• 101800004564 Transforming growth factor alpha Proteins 0.000 description 1
• 102100031988 Tumor necrosis factor ligand superfamily member 6 Human genes 0.000 description 1
• 108050002568 Tumor necrosis factor ligand superfamily member 6 Proteins 0.000 description 1
• 102100036857 Tumor necrosis factor receptor superfamily member 8 Human genes 0.000 description 1
• 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
• 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
• JXLYSJRDGCGARV-WWYNWVTFSA-N Vinblastine Natural products O=C(O[C@H]1[C@](O)(C(=O)OC)[C@@H]2N(C)c3c(cc(c(OC)c3)[C@]3(C(=O)OC)c4[nH]c5c(c4CCN4C[C@](O)(CC)C[C@H](C3)C4)cccc5)[C@@]32[C@H]2[C@@]1(CC)C=CCN2CC3)C JXLYSJRDGCGARV-WWYNWVTFSA-N 0.000 description 1
• 108700005077 Viral Genes Proteins 0.000 description 1
• 108010031318 Vitronectin Proteins 0.000 description 1
• 102100035140 Vitronectin Human genes 0.000 description 1
• JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
• 238000002835 absorbance Methods 0.000 description 1
• 239000002253 acid Substances 0.000 description 1
• RJURFGZVJUQBHK-IIXSONLDSA-N actinomycin D Chemical compound C[C@H]1OC(=O)[C@H](C(C)C)N(C)C(=O)CN(C)C(=O)[C@@H]2CCCN2C(=O)[C@@H](C(C)C)NC(=O)[C@H]1NC(=O)C1=C(N)C(=O)C(C)=C2OC(C(C)=CC=C3C(=O)N[C@@H]4C(=O)N[C@@H](C(N5CCC[C@H]5C(=O)N(C)CC(=O)N(C)[C@@H](C(C)C)C(=O)O[C@@H]4C)=O)C(C)C)=C3N=C21 RJURFGZVJUQBHK-IIXSONLDSA-N 0.000 description 1
• 229940009456 adriamycin Drugs 0.000 description 1
• 229940050528 albumin Drugs 0.000 description 1
• 125000000217 alkyl group Chemical group 0.000 description 1
• 239000002776 alpha toxin Substances 0.000 description 1
• 150000001412 amines Chemical class 0.000 description 1
• 230000003321 amplification Effects 0.000 description 1
• 239000003708 ampul Substances 0.000 description 1
• 210000002255 anal canal Anatomy 0.000 description 1
• 108010074902 angiotensin converting enzyme secretase Proteins 0.000 description 1
• 238000010171 animal model Methods 0.000 description 1
• 239000003242 anti bacterial agent Substances 0.000 description 1
• 230000000692 anti-sense effect Effects 0.000 description 1
• 230000000259 anti-tumor effect Effects 0.000 description 1
• 230000002137 anti-vascular effect Effects 0.000 description 1
• 229940088710 antibiotic agent Drugs 0.000 description 1
• 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 1
• 210000000628 antibody-producing cell Anatomy 0.000 description 1
• 239000003963 antioxidant agent Substances 0.000 description 1
• 235000006708 antioxidants Nutrition 0.000 description 1
• 239000000074 antisense oligonucleotide Substances 0.000 description 1
• 238000012230 antisense oligonucleotides Methods 0.000 description 1
• 210000000436 anus Anatomy 0.000 description 1
• 230000006907 apoptotic process Effects 0.000 description 1
• 239000008346 aqueous phase Substances 0.000 description 1
• 206010003246 arthritis Diseases 0.000 description 1
• 239000002473 artificial blood Substances 0.000 description 1
• 210000004507 artificial chromosome Anatomy 0.000 description 1
• 229960003272 asparaginase Drugs 0.000 description 1
• DCXYFEDJOCDNAF-UHFFFAOYSA-M asparaginate Chemical compound [O-]C(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-M 0.000 description 1
• 229940120638 avastin Drugs 0.000 description 1
• VSRXQHXAPYXROS-UHFFFAOYSA-N azanide;cyclobutane-1,1-dicarboxylic acid;platinum(2+) Chemical compound [NH2-].[NH2-].[Pt+2].OC(=O)C1(C(O)=O)CCC1 VSRXQHXAPYXROS-UHFFFAOYSA-N 0.000 description 1
• 230000001580 bacterial effect Effects 0.000 description 1
• 239000011324 bead Substances 0.000 description 1
• 230000008901 benefit Effects 0.000 description 1
• 108091008324 binding proteins Proteins 0.000 description 1
• 230000008827 biological function Effects 0.000 description 1
• 239000012620 biological material Substances 0.000 description 1
• 229960001561 bleomycin Drugs 0.000 description 1
• OYVAGSVQBOHSSS-UAPAGMARSA-O bleomycin A2 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC=C(N=1)C=1SC=C(N=1)C(=O)NCCC[S+](C)C)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C OYVAGSVQBOHSSS-UAPAGMARSA-O 0.000 description 1
• 210000001124 body fluid Anatomy 0.000 description 1
• 210000001185 bone marrow Anatomy 0.000 description 1
• 230000018678 bone mineralization Effects 0.000 description 1
• 210000000133 brain stem Anatomy 0.000 description 1
• 210000000621 bronchi Anatomy 0.000 description 1
• 229960002092 busulfan Drugs 0.000 description 1
• 210000004900 c-terminal fragment Anatomy 0.000 description 1
• 210000004899 c-terminal region Anatomy 0.000 description 1
• 229910001424 calcium ion Inorganic materials 0.000 description 1
• 229940127093 camptothecin Drugs 0.000 description 1
• VSJKWCGYPAHWDS-FQEVSTJZSA-N camptothecin Chemical compound C1=CC=C2C=C(CN3C4=CC5=C(C3=O)COC(=O)[C@]5(O)CC)C4=NC2=C1 VSJKWCGYPAHWDS-FQEVSTJZSA-N 0.000 description 1
• 230000009702 cancer cell proliferation Effects 0.000 description 1
• 208000035269 cancer or benign tumor Diseases 0.000 description 1
• 229960004117 capecitabine Drugs 0.000 description 1
• 239000004202 carbamide Substances 0.000 description 1
• 229960004562 carboplatin Drugs 0.000 description 1
• 229960005243 carmustine Drugs 0.000 description 1
• 230000015556 catabolic process Effects 0.000 description 1
• 230000003197 catalytic effect Effects 0.000 description 1
• 125000002091 cationic group Chemical group 0.000 description 1
• 150000001768 cations Chemical class 0.000 description 1
• 210000004323 caveolae Anatomy 0.000 description 1
• 230000006369 cell cycle progression Effects 0.000 description 1
• 238000010822 cell death assay Methods 0.000 description 1
• 230000032823 cell division Effects 0.000 description 1
• 230000003915 cell function Effects 0.000 description 1
• 239000013592 cell lysate Substances 0.000 description 1
• 239000013553 cell monolayer Substances 0.000 description 1
• 230000005890 cell-mediated cytotoxicity Effects 0.000 description 1
• 230000030570 cellular localization Effects 0.000 description 1
• 210000003169 central nervous system Anatomy 0.000 description 1
• 210000001175 cerebrospinal fluid Anatomy 0.000 description 1
• 239000003153 chemical reaction reagent Substances 0.000 description 1
• 230000035605 chemotaxis Effects 0.000 description 1
• 229940044683 chemotherapy drug Drugs 0.000 description 1
• 229960004630 chlorambucil Drugs 0.000 description 1
• JCKYGMPEJWAADB-UHFFFAOYSA-N chlorambucil Chemical compound OC(=O)CCCC1=CC=C(N(CCCl)CCCl)C=C1 JCKYGMPEJWAADB-UHFFFAOYSA-N 0.000 description 1
• 238000004587 chromatography analysis Methods 0.000 description 1
• 238000011097 chromatography purification Methods 0.000 description 1
• 208000032852 chronic lymphocytic leukemia Diseases 0.000 description 1
• DQLATGHUWYMOKM-UHFFFAOYSA-L cisplatin Chemical compound N[Pt](N)(Cl)Cl DQLATGHUWYMOKM-UHFFFAOYSA-L 0.000 description 1
• 229960004316 cisplatin Drugs 0.000 description 1
• 230000004186 co-expression Effects 0.000 description 1
• 229920001436 collagen Polymers 0.000 description 1
• 210000001072 colon Anatomy 0.000 description 1
• 238000007398 colorimetric assay Methods 0.000 description 1
• 238000009096 combination chemotherapy Methods 0.000 description 1
• 150000004814 combretastatins Chemical class 0.000 description 1
• 239000003184 complementary RNA Substances 0.000 description 1
• 210000002808 connective tissue Anatomy 0.000 description 1
• 208000029078 coronary artery disease Diseases 0.000 description 1
• 239000006071 cream Substances 0.000 description 1
• 238000002447 crystallographic data Methods 0.000 description 1
• 238000009109 curative therapy Methods 0.000 description 1
• WZHCOOQXZCIUNC-UHFFFAOYSA-N cyclandelate Chemical compound C1C(C)(C)CC(C)CC1OC(=O)C(O)C1=CC=CC=C1 WZHCOOQXZCIUNC-UHFFFAOYSA-N 0.000 description 1
• 125000000113 cyclohexyl group Chemical group [H]C1([H])C([H])([H])C([H])([H])C([H])(*)C([H])([H])C1([H])[H] 0.000 description 1
• 125000004210 cyclohexylmethyl group Chemical group [H]C([H])(*)C1([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
• 229960004397 cyclophosphamide Drugs 0.000 description 1
• 150000001945 cysteines Chemical class 0.000 description 1
• 229960000684 cytarabine Drugs 0.000 description 1
• 230000009089 cytolysis Effects 0.000 description 1
• 231100000599 cytotoxic agent Toxicity 0.000 description 1
• 231100000135 cytotoxicity Toxicity 0.000 description 1
• 239000002619 cytotoxin Substances 0.000 description 1
• 229960003901 dacarbazine Drugs 0.000 description 1
• 229960000640 dactinomycin Drugs 0.000 description 1
• STQGQHZAVUOBTE-VGBVRHCVSA-N daunorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(C)=O)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 STQGQHZAVUOBTE-VGBVRHCVSA-N 0.000 description 1
• 229960000975 daunorubicin Drugs 0.000 description 1
• 230000007423 decrease Effects 0.000 description 1
• 230000003247 decreasing effect Effects 0.000 description 1
• 238000006731 degradation reaction Methods 0.000 description 1
• 239000003599 detergent Substances 0.000 description 1
• 238000011161 development Methods 0.000 description 1
• 230000018109 developmental process Effects 0.000 description 1
• 229960000605 dexrazoxane Drugs 0.000 description 1
• PXBRQCKWGAHEHS-UHFFFAOYSA-N dichlorodifluoromethane Chemical compound FC(F)(Cl)Cl PXBRQCKWGAHEHS-UHFFFAOYSA-N 0.000 description 1
• 235000019404 dichlorodifluoromethane Nutrition 0.000 description 1
• 239000005546 dideoxynucleotide Substances 0.000 description 1
• 230000029087 digestion Effects 0.000 description 1
• 239000003085 diluting agent Substances 0.000 description 1
• 208000035475 disorder Diseases 0.000 description 1
• 230000009429 distress Effects 0.000 description 1
• 238000009826 distribution Methods 0.000 description 1
• 150000002019 disulfides Chemical class 0.000 description 1
• VSJKWCGYPAHWDS-UHFFFAOYSA-N dl-camptothecin Natural products C1=CC=C2C=C(CN3C4=CC5=C(C3=O)COC(=O)C5(O)CC)C4=NC2=C1 VSJKWCGYPAHWDS-UHFFFAOYSA-N 0.000 description 1
• 229960003668 docetaxel Drugs 0.000 description 1
• 229960004679 doxorubicin Drugs 0.000 description 1
• 238000012377 drug delivery Methods 0.000 description 1
• 230000001804 emulsifying effect Effects 0.000 description 1
• 238000005538 encapsulation Methods 0.000 description 1
• 210000000750 endocrine system Anatomy 0.000 description 1
• 230000012202 endocytosis Effects 0.000 description 1
• 201000006828 endometrial hyperplasia Diseases 0.000 description 1
• 210000001163 endosome Anatomy 0.000 description 1
• 108091007231 endothelial receptors Proteins 0.000 description 1
• 108010005324 enkephalin degrading enzyme Proteins 0.000 description 1
• 231100000655 enterotoxin Toxicity 0.000 description 1
• 230000007515 enzymatic degradation Effects 0.000 description 1
• 238000001976 enzyme digestion Methods 0.000 description 1
• 229940116977 epidermal growth factor Drugs 0.000 description 1
• 229930013356 epothilone Natural products 0.000 description 1
• HESCAJZNRMSMJG-KKQRBIROSA-N epothilone A Chemical class C/C([C@@H]1C[C@@H]2O[C@@H]2CCC[C@@H]([C@@H]([C@@H](C)C(=O)C(C)(C)[C@@H](O)CC(=O)O1)O)C)=C\C1=CSC(C)=N1 HESCAJZNRMSMJG-KKQRBIROSA-N 0.000 description 1
• 210000003238 esophagus Anatomy 0.000 description 1
• 150000002148 esters Chemical class 0.000 description 1
• 229960005420 etoposide Drugs 0.000 description 1
• VJJPUSNTGOMMGY-MRVIYFEKSA-N etoposide Chemical compound COC1=C(O)C(OC)=CC([C@@H]2C3=CC=4OCOC=4C=C3[C@@H](O[C@H]3[C@@H]([C@@H](O)[C@@H]4O[C@H](C)OC[C@H]4O3)O)[C@@H]3[C@@H]2C(OC3)=O)=C1 VJJPUSNTGOMMGY-MRVIYFEKSA-N 0.000 description 1
• 238000002474 experimental method Methods 0.000 description 1
• 239000013604 expression vector Substances 0.000 description 1
• 210000004996 female reproductive system Anatomy 0.000 description 1
• 238000000684 flow cytometry Methods 0.000 description 1
• ODKNJVUHOIMIIZ-RRKCRQDMSA-N floxuridine Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C(F)=C1 ODKNJVUHOIMIIZ-RRKCRQDMSA-N 0.000 description 1
• 229960000961 floxuridine Drugs 0.000 description 1
• 229960000390 fludarabine Drugs 0.000 description 1
• GIUYCYHIANZCFB-FJFJXFQQSA-N fludarabine phosphate Chemical compound C1=NC=2C(N)=NC(F)=NC=2N1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@@H]1O GIUYCYHIANZCFB-FJFJXFQQSA-N 0.000 description 1
• 239000012530 fluid Substances 0.000 description 1
• 239000006260 foam Substances 0.000 description 1
• 210000001650 focal adhesion Anatomy 0.000 description 1
• 108020005243 folate receptor Proteins 0.000 description 1
• 102000006815 folate receptor Human genes 0.000 description 1
• 235000019256 formaldehyde Nutrition 0.000 description 1
• 238000013467 fragmentation Methods 0.000 description 1
• 238000006062 fragmentation reaction Methods 0.000 description 1
• 239000012458 free base Substances 0.000 description 1
• 230000002538 fungal effect Effects 0.000 description 1
• 210000000232 gallbladder Anatomy 0.000 description 1
• SDUQYLNIPVEERB-QPPQHZFASA-N gemcitabine Chemical compound O=C1N=C(N)C=CN1[C@H]1C(F)(F)[C@H](O)[C@@H](CO)O1 SDUQYLNIPVEERB-QPPQHZFASA-N 0.000 description 1
• 229960005277 gemcitabine Drugs 0.000 description 1
• 230000009368 gene silencing by RNA Effects 0.000 description 1
• 230000002068 genetic effect Effects 0.000 description 1
• 238000010353 genetic engineering Methods 0.000 description 1
• 229940045109 genistein Drugs 0.000 description 1
• TZBJGXHYKVUXJN-UHFFFAOYSA-N genistein Natural products C1=CC(O)=CC=C1C1=COC2=CC(O)=CC(O)=C2C1=O TZBJGXHYKVUXJN-UHFFFAOYSA-N 0.000 description 1
• 235000006539 genistein Nutrition 0.000 description 1
• ZCOLJUOHXJRHDI-CMWLGVBASA-N genistein 7-O-beta-D-glucoside Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=CC(O)=C2C(=O)C(C=3C=CC(O)=CC=3)=COC2=C1 ZCOLJUOHXJRHDI-CMWLGVBASA-N 0.000 description 1
• 239000011521 glass Substances 0.000 description 1
• 231100000852 glomerular disease Toxicity 0.000 description 1
• 206010061989 glomerulosclerosis Diseases 0.000 description 1
• 239000008103 glucose Substances 0.000 description 1
• 230000013595 glycosylation Effects 0.000 description 1
• 238000006206 glycosylation reaction Methods 0.000 description 1
• PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
• 229910052737 gold Inorganic materials 0.000 description 1
• 239000010931 gold Substances 0.000 description 1
• 239000008187 granular material Substances 0.000 description 1
• 239000001963 growth medium Substances 0.000 description 1
• 150000002357 guanidines Chemical class 0.000 description 1
• 210000000777 hematopoietic system Anatomy 0.000 description 1
• 238000013537 high throughput screening Methods 0.000 description 1
• 150000002411 histidines Chemical class 0.000 description 1
• 150000007857 hydrazones Chemical class 0.000 description 1
• 235000011167 hydrochloric acid Nutrition 0.000 description 1
• 150000004679 hydroxides Chemical class 0.000 description 1
• 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
• 208000020673 hypertrichosis-acromegaloid facial appearance syndrome Diseases 0.000 description 1
• 229960001680 ibuprofen Drugs 0.000 description 1
• 229960000908 idarubicin Drugs 0.000 description 1
• HOMGKSMUEGBAAB-UHFFFAOYSA-N ifosfamide Chemical compound ClCCNP1(=O)OCCCN1CCCl HOMGKSMUEGBAAB-UHFFFAOYSA-N 0.000 description 1
• 229960001101 ifosfamide Drugs 0.000 description 1
• 239000012216 imaging agent Substances 0.000 description 1
• 238000003384 imaging method Methods 0.000 description 1
• 210000002865 immune cell Anatomy 0.000 description 1
• 230000001900 immune effect Effects 0.000 description 1
• 238000002649 immunization Methods 0.000 description 1
• 230000003053 immunization Effects 0.000 description 1
• 238000003364 immunohistochemistry Methods 0.000 description 1
• 239000002955 immunomodulating agent Substances 0.000 description 1
• 229940121354 immunomodulator Drugs 0.000 description 1
• 238000012744 immunostaining Methods 0.000 description 1
• 238000009169 immunotherapy Methods 0.000 description 1
• 239000002596 immunotoxin Substances 0.000 description 1
• 238000007901 in situ hybridization Methods 0.000 description 1
• 238000010874 in vitro model Methods 0.000 description 1
• 238000011065 in-situ storage Methods 0.000 description 1
• 238000011534 incubation Methods 0.000 description 1
• 239000000411 inducer Substances 0.000 description 1
• 230000006698 induction Effects 0.000 description 1
• 208000027866 inflammatory disease Diseases 0.000 description 1
• 230000002757 inflammatory effect Effects 0.000 description 1
• 239000003112 inhibitor Substances 0.000 description 1
• 230000002401 inhibitory effect Effects 0.000 description 1
• 238000011081 inoculation Methods 0.000 description 1
• 150000007529 inorganic bases Chemical class 0.000 description 1
• 229960003786 inosine Drugs 0.000 description 1
• 239000000543 intermediate Substances 0.000 description 1
• 238000001361 intraarterial administration Methods 0.000 description 1
• 239000007928 intraperitoneal injection Substances 0.000 description 1
• 238000010253 intravenous injection Methods 0.000 description 1
• 208000030776 invasive breast carcinoma Diseases 0.000 description 1
• 206010073095 invasive ductal breast carcinoma Diseases 0.000 description 1
• 238000005342 ion exchange Methods 0.000 description 1
• 229960004768 irinotecan Drugs 0.000 description 1
• UWKQSNNFCGGAFS-XIFFEERXSA-N irinotecan Chemical compound C1=C2C(CC)=C3CN(C(C4=C([C@@](C(=O)OC4)(O)CC)C=4)=O)C=4C3=NC2=CC=C1OC(=O)N(CC1)CCC1N1CCCCC1 UWKQSNNFCGGAFS-XIFFEERXSA-N 0.000 description 1
• 125000000959 isobutyl group Chemical group [H]C([H])([H])C([H])(C([H])([H])[H])C([H])([H])* 0.000 description 1
• JJWLVOIRVHMVIS-UHFFFAOYSA-N isopropylamine Chemical compound CC(C)N JJWLVOIRVHMVIS-UHFFFAOYSA-N 0.000 description 1
• 210000001503 joint Anatomy 0.000 description 1
• 210000000244 kidney pelvis Anatomy 0.000 description 1
• 239000008101 lactose Substances 0.000 description 1
• 206010023841 laryngeal neoplasm Diseases 0.000 description 1
• 210000000867 larynx Anatomy 0.000 description 1
• 208000032839 leukemia Diseases 0.000 description 1
• 230000021633 leukocyte mediated immunity Effects 0.000 description 1
• 150000002632 lipids Chemical class 0.000 description 1
• 239000006193 liquid solution Substances 0.000 description 1
• 239000006194 liquid suspension Substances 0.000 description 1
• 229960002247 lomustine Drugs 0.000 description 1
• 210000004924 lung microvascular endothelial cell Anatomy 0.000 description 1
• 229920001427 mPEG Polymers 0.000 description 1
• 108010026228 mRNA guanylyltransferase Proteins 0.000 description 1
• 229920002521 macromolecule Polymers 0.000 description 1
• 210000002540 macrophage Anatomy 0.000 description 1
• 210000004995 male reproductive system Anatomy 0.000 description 1
• 208000026045 malignant tumor of parathyroid gland Diseases 0.000 description 1
• 238000007726 management method Methods 0.000 description 1
• 238000001840 matrix-assisted laser desorption--ionisation time-of-flight mass spectrometry Methods 0.000 description 1
• HAWPXGHAZFHHAD-UHFFFAOYSA-N mechlorethamine Chemical compound ClCCN(C)CCCl HAWPXGHAZFHHAD-UHFFFAOYSA-N 0.000 description 1
• 229960004961 mechlorethamine Drugs 0.000 description 1
• 239000002609 medium Substances 0.000 description 1
• 201000001441 melanoma Diseases 0.000 description 1
• 206010027191 meningioma Diseases 0.000 description 1
• GLVAUDGFNGKCSF-UHFFFAOYSA-N mercaptopurine Chemical compound S=C1NC=NC2=C1NC=N2 GLVAUDGFNGKCSF-UHFFFAOYSA-N 0.000 description 1
• 229960001428 mercaptopurine Drugs 0.000 description 1
• 229960000485 methotrexate Drugs 0.000 description 1
• 125000004092 methylthiomethyl group Chemical group [H]C([H])([H])SC([H])([H])* 0.000 description 1
• 239000000693 micelle Substances 0.000 description 1
• 239000004005 microsphere Substances 0.000 description 1
• 150000007522 mineralic acids Chemical class 0.000 description 1
• CFCUWKMKBJTWLW-BKHRDMLASA-N mithramycin Chemical compound O([C@@H]1C[C@@H](O[C@H](C)[C@H]1O)OC=1C=C2C=C3C[C@H]([C@@H](C(=O)C3=C(O)C2=C(O)C=1C)O[C@@H]1O[C@H](C)[C@@H](O)[C@H](O[C@@H]2O[C@H](C)[C@H](O)[C@H](O[C@@H]3O[C@H](C)[C@@H](O)[C@@](C)(O)C3)C2)C1)[C@H](OC)C(=O)[C@@H](O)[C@@H](C)O)[C@H]1C[C@@H](O)[C@H](O)[C@@H](C)O1 CFCUWKMKBJTWLW-BKHRDMLASA-N 0.000 description 1
• 229960004857 mitomycin Drugs 0.000 description 1
• 230000011278 mitosis Effects 0.000 description 1
• 229960000350 mitotane Drugs 0.000 description 1
• 229960001156 mitoxantrone Drugs 0.000 description 1
• KKZJGLLVHKMTCM-UHFFFAOYSA-N mitoxantrone Chemical compound O=C1C2=C(O)C=CC(O)=C2C(=O)C2=C1C(NCCNCCO)=CC=C2NCCNCCO KKZJGLLVHKMTCM-UHFFFAOYSA-N 0.000 description 1
• 238000002156 mixing Methods 0.000 description 1
• 231100000219 mutagenic Toxicity 0.000 description 1
• 230000003505 mutagenic effect Effects 0.000 description 1
• 210000000066 myeloid cell Anatomy 0.000 description 1
• 210000004898 n-terminal fragment Anatomy 0.000 description 1
• 239000006225 natural substrate Substances 0.000 description 1
• 239000006199 nebulizer Substances 0.000 description 1
• 230000014399 negative regulation of angiogenesis Effects 0.000 description 1
• 229960004927 neomycin Drugs 0.000 description 1
• 230000001613 neoplastic effect Effects 0.000 description 1
• 230000007935 neutral effect Effects 0.000 description 1
• 229910052757 nitrogen Inorganic materials 0.000 description 1
• 208000002154 non-small cell lung carcinoma Diseases 0.000 description 1
• 238000003199 nucleic acid amplification method Methods 0.000 description 1
• 239000003921 oil Substances 0.000 description 1
• 235000019198 oils Nutrition 0.000 description 1
• 239000002751 oligonucleotide probe Substances 0.000 description 1
• 238000005457 optimization Methods 0.000 description 1
• 150000007524 organic acids Chemical class 0.000 description 1
• 235000005985 organic acids Nutrition 0.000 description 1
• 150000007530 organic bases Chemical class 0.000 description 1
• 229960003104 ornithine Drugs 0.000 description 1
• 230000003204 osmotic effect Effects 0.000 description 1
• 238000007500 overflow downdraw method Methods 0.000 description 1
• 230000003647 oxidation Effects 0.000 description 1
• 238000007254 oxidation reaction Methods 0.000 description 1
• 229940046231 pamidronate Drugs 0.000 description 1
• WRUUGTRCQOWXEG-UHFFFAOYSA-N pamidronate Chemical compound NCCC(O)(P(O)(O)=O)P(O)(O)=O WRUUGTRCQOWXEG-UHFFFAOYSA-N 0.000 description 1
• 210000000496 pancreas Anatomy 0.000 description 1
• 239000002245 particle Substances 0.000 description 1
• 239000006072 paste Substances 0.000 description 1
• 239000000312 peanut oil Substances 0.000 description 1
• 210000003899 penis Anatomy 0.000 description 1
• XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
• 229960002340 pentostatin Drugs 0.000 description 1
• FPVKHBSQESCIEP-JQCXWYLXSA-N pentostatin Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(N=CNC[C@H]2O)=C2N=C1 FPVKHBSQESCIEP-JQCXWYLXSA-N 0.000 description 1
• 238000012510 peptide mapping method Methods 0.000 description 1
• 210000003800 pharynx Anatomy 0.000 description 1
• 150000002989 phenols Chemical class 0.000 description 1
• 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 1
• 150000008300 phosphoramidites Chemical class 0.000 description 1
• 235000011007 phosphoric acid Nutrition 0.000 description 1
• 150000003016 phosphoric acids Chemical class 0.000 description 1
• 239000003123 plant toxin Substances 0.000 description 1
• 230000007505 plaque formation Effects 0.000 description 1
• 229940012957 plasmin Drugs 0.000 description 1
• 229960003171 plicamycin Drugs 0.000 description 1
• 231100000614 poison Toxicity 0.000 description 1
• 230000007096 poisonous effect Effects 0.000 description 1
• 230000008488 polyadenylation Effects 0.000 description 1
• 229920000768 polyamine Polymers 0.000 description 1
• 229920005862 polyol Polymers 0.000 description 1
• 150000003077 polyols Chemical class 0.000 description 1
• 229920002981 polyvinylidene fluoride Polymers 0.000 description 1
• 230000008092 positive effect Effects 0.000 description 1
• 239000011591 potassium Substances 0.000 description 1
• 229910052700 potassium Inorganic materials 0.000 description 1
• 230000003389 potentiating effect Effects 0.000 description 1
• 238000001556 precipitation Methods 0.000 description 1
• 230000002335 preservative effect Effects 0.000 description 1
• 230000002265 prevention Effects 0.000 description 1
• 238000009117 preventive therapy Methods 0.000 description 1
• 150000003141 primary amines Chemical class 0.000 description 1
• MFDFERRIHVXMIY-UHFFFAOYSA-N procaine Chemical compound CCN(CC)CCOC(=O)C1=CC=C(N)C=C1 MFDFERRIHVXMIY-UHFFFAOYSA-N 0.000 description 1
• 229960004919 procaine Drugs 0.000 description 1
• CPTBDICYNRMXFX-UHFFFAOYSA-N procarbazine Chemical compound CNNCC1=CC=C(C(=O)NC(C)C)C=C1 CPTBDICYNRMXFX-UHFFFAOYSA-N 0.000 description 1
• 229960000624 procarbazine Drugs 0.000 description 1
• 238000012545 processing Methods 0.000 description 1
• 230000000750 progressive effect Effects 0.000 description 1
• 230000002035 prolonged effect Effects 0.000 description 1
• 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
• 230000001915 proofreading effect Effects 0.000 description 1
• 239000001294 propane Substances 0.000 description 1
• 239000003380 propellant Substances 0.000 description 1
• 235000019833 protease Nutrition 0.000 description 1
• 238000002731 protein assay Methods 0.000 description 1
• 235000004252 protein component Nutrition 0.000 description 1
• 238000002331 protein detection Methods 0.000 description 1
• 239000012474 protein marker Substances 0.000 description 1
• 238000001742 protein purification Methods 0.000 description 1
• 229940124272 protein stabilizer Drugs 0.000 description 1
• 238000011002 quantification Methods 0.000 description 1
• 230000000171 quenching effect Effects 0.000 description 1
• 238000009790 rate-determining step (RDS) Methods 0.000 description 1
• 210000000664 rectum Anatomy 0.000 description 1
• 230000002829 reductive effect Effects 0.000 description 1
• 229940116176 remicade Drugs 0.000 description 1
• 210000004994 reproductive system Anatomy 0.000 description 1
• 238000011160 research Methods 0.000 description 1
• 230000008458 response to injury Effects 0.000 description 1
• 230000000717 retained effect Effects 0.000 description 1
• 210000003705 ribosome Anatomy 0.000 description 1
• 108091092562 ribozyme Proteins 0.000 description 1
• ATEBXHFBFRCZMA-VXTBVIBXSA-N rifabutin Chemical compound O([C@](C1=O)(C)O/C=C/[C@@H]([C@H]([C@@H](OC(C)=O)[C@H](C)[C@H](O)[C@H](C)[C@@H](O)[C@@H](C)\C=C\C=C(C)/C(=O)NC(=C2N3)C(=O)C=4C(O)=C5C)C)OC)C5=C1C=4C2=NC13CCN(CC(C)C)CC1 ATEBXHFBFRCZMA-VXTBVIBXSA-N 0.000 description 1
• 229960000885 rifabutin Drugs 0.000 description 1
• 238000007480 sanger sequencing Methods 0.000 description 1
• 238000012216 screening Methods 0.000 description 1
• 238000011451 sequencing strategy Methods 0.000 description 1
• 210000002966 serum Anatomy 0.000 description 1
• 239000008159 sesame oil Substances 0.000 description 1
• 235000011803 sesame oil Nutrition 0.000 description 1
• 230000019491 signal transduction Effects 0.000 description 1
• QFJCIRLUMZQUOT-HPLJOQBZSA-N sirolimus Chemical compound C1C[C@@H](O)[C@H](OC)C[C@@H]1C[C@@H](C)[C@H]1OC(=O)[C@@H]2CCCCN2C(=O)C(=O)[C@](O)(O2)[C@H](C)CC[C@H]2C[C@H](OC)/C(C)=C/C=C/C=C/[C@@H](C)C[C@@H](C)C(=O)[C@H](OC)[C@H](O)/C(C)=C/[C@@H](C)C(=O)C1 QFJCIRLUMZQUOT-HPLJOQBZSA-N 0.000 description 1
• 238000005549 size reduction Methods 0.000 description 1
• 238000004513 sizing Methods 0.000 description 1
• 210000003491 skin Anatomy 0.000 description 1
• 210000000813 small intestine Anatomy 0.000 description 1
• 239000011734 sodium Substances 0.000 description 1
• 229910052708 sodium Inorganic materials 0.000 description 1
• FQENQNTWSFEDLI-UHFFFAOYSA-J sodium diphosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])([O-])=O FQENQNTWSFEDLI-UHFFFAOYSA-J 0.000 description 1
• 235000009518 sodium iodide Nutrition 0.000 description 1
• 239000012064 sodium phosphate buffer Substances 0.000 description 1
• 229940048086 sodium pyrophosphate Drugs 0.000 description 1
• RWVGQQGBQSJDQV-UHFFFAOYSA-M sodium;3-[[4-[(e)-[4-(4-ethoxyanilino)phenyl]-[4-[ethyl-[(3-sulfonatophenyl)methyl]azaniumylidene]-2-methylcyclohexa-2,5-dien-1-ylidene]methyl]-n-ethyl-3-methylanilino]methyl]benzenesulfonate Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C(=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C)C=2C(=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C)C=C1 RWVGQQGBQSJDQV-UHFFFAOYSA-M 0.000 description 1
• 238000000638 solvent extraction Methods 0.000 description 1
• 238000000527 sonication Methods 0.000 description 1
• 239000000600 sorbitol Substances 0.000 description 1
• 239000007921 spray Substances 0.000 description 1
• 239000003381 stabilizer Substances 0.000 description 1
• 150000003431 steroids Chemical class 0.000 description 1
• 210000002784 stomach Anatomy 0.000 description 1
• 229960001052 streptozocin Drugs 0.000 description 1
• ZSJLQEPLLKMAKR-GKHCUFPYSA-N streptozocin Chemical compound O=NN(C)C(=O)N[C@H]1[C@@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O ZSJLQEPLLKMAKR-GKHCUFPYSA-N 0.000 description 1
• 210000002536 stromal cell Anatomy 0.000 description 1
• 238000010254 subcutaneous injection Methods 0.000 description 1
• 239000007929 subcutaneous injection Substances 0.000 description 1
• 239000000758 substrate Substances 0.000 description 1
• 239000005720 sucrose Substances 0.000 description 1
• 150000008163 sugars Chemical class 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
• 239000000375 suspending agent Substances 0.000 description 1
• 230000008961 swelling Effects 0.000 description 1
• 239000003826 tablet Substances 0.000 description 1
• 229960001278 teniposide Drugs 0.000 description 1
• NRUKOCRGYNPUPR-QBPJDGROSA-N teniposide Chemical compound COC1=C(O)C(OC)=CC([C@@H]2C3=CC=4OCOC=4C=C3[C@@H](O[C@H]3[C@@H]([C@@H](O)[C@@H]4O[C@@H](OC[C@H]4O3)C=3SC=CC=3)O)[C@@H]3[C@@H]2C(OC3)=O)=C1 NRUKOCRGYNPUPR-QBPJDGROSA-N 0.000 description 1
• 210000001550 testis Anatomy 0.000 description 1
• 235000019818 tetrasodium diphosphate Nutrition 0.000 description 1
• 239000001577 tetrasodium phosphonato phosphate Substances 0.000 description 1
• 239000002562 thickening agent Substances 0.000 description 1
• 108010073106 thimet oligopeptidase Proteins 0.000 description 1
• 150000003573 thiols Chemical class 0.000 description 1
• 229960001196 thiotepa Drugs 0.000 description 1
• 229960004072 thrombin Drugs 0.000 description 1
• 210000001685 thyroid gland Anatomy 0.000 description 1
• 229960003087 tioguanine Drugs 0.000 description 1
• MNRILEROXIRVNJ-UHFFFAOYSA-N tioguanine Chemical compound N1C(N)=NC(=S)C2=NC=N[C]21 MNRILEROXIRVNJ-UHFFFAOYSA-N 0.000 description 1
• 229960000187 tissue plasminogen activator Drugs 0.000 description 1
• 230000007838 tissue remodeling Effects 0.000 description 1
• 238000010361 transduction Methods 0.000 description 1
• 230000026683 transduction Effects 0.000 description 1
• 238000003151 transfection method Methods 0.000 description 1
• 238000006276 transfer reaction Methods 0.000 description 1
• 238000011426 transformation method Methods 0.000 description 1
• 230000001052 transient effect Effects 0.000 description 1
• 150000005691 triesters Chemical class 0.000 description 1
• HRXKRNGNAMMEHJ-UHFFFAOYSA-K trisodium citrate Chemical compound [Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O HRXKRNGNAMMEHJ-UHFFFAOYSA-K 0.000 description 1
• 229940038773 trisodium citrate Drugs 0.000 description 1
• 230000036326 tumor accumulation Effects 0.000 description 1
• 230000001173 tumoral effect Effects 0.000 description 1
• 210000004026 tunica intima Anatomy 0.000 description 1
• 229940121358 tyrosine kinase inhibitor Drugs 0.000 description 1
• 239000005483 tyrosine kinase inhibitor Substances 0.000 description 1
• 210000003606 umbilical vein Anatomy 0.000 description 1
• 241001529453 unidentified herpesvirus Species 0.000 description 1
• 241001430294 unidentified retrovirus Species 0.000 description 1
• 238000011144 upstream manufacturing Methods 0.000 description 1
• 210000000626 ureter Anatomy 0.000 description 1
• 201000005112 urinary bladder cancer Diseases 0.000 description 1
• 210000002700 urine Anatomy 0.000 description 1
• 210000001215 vagina Anatomy 0.000 description 1
• 229960003048 vinblastine Drugs 0.000 description 1
• JXLYSJRDGCGARV-XQKSVPLYSA-N vincaleukoblastine Chemical compound C([C@@H](C[C@]1(C(=O)OC)C=2C(=CC3=C([C@]45[C@H]([C@@]([C@H](OC(C)=O)[C@]6(CC)C=CCN([C@H]56)CC4)(O)C(=O)OC)N3C)C=2)OC)C[C@@](C2)(O)CC)N2CCC2=C1NC1=CC=CC=C21 JXLYSJRDGCGARV-XQKSVPLYSA-N 0.000 description 1
• 229960004528 vincristine Drugs 0.000 description 1
• OGWKCGZFUXNPDA-XQKSVPLYSA-N vincristine Chemical compound C([N@]1C[C@@H](C[C@]2(C(=O)OC)C=3C(=CC4=C([C@]56[C@H]([C@@]([C@H](OC(C)=O)[C@]7(CC)C=CCN([C@H]67)CC5)(O)C(=O)OC)N4C=O)C=3)OC)C[C@@](C1)(O)CC)CC1=C2NC2=CC=CC=C12 OGWKCGZFUXNPDA-XQKSVPLYSA-N 0.000 description 1
• OGWKCGZFUXNPDA-UHFFFAOYSA-N vincristine Natural products C1C(CC)(O)CC(CC2(C(=O)OC)C=3C(=CC4=C(C56C(C(C(OC(C)=O)C7(CC)C=CCN(C67)CC5)(O)C(=O)OC)N4C=O)C=3)OC)CN1CCC1=C2NC2=CC=CC=C12 OGWKCGZFUXNPDA-UHFFFAOYSA-N 0.000 description 1
• 229960002066 vinorelbine Drugs 0.000 description 1
• GBABOYUKABKIAF-GHYRFKGUSA-N vinorelbine Chemical compound C1N(CC=2C3=CC=CC=C3NC=22)CC(CC)=C[C@H]1C[C@]2(C(=O)OC)C1=CC([C@]23[C@H]([C@]([C@H](OC(C)=O)[C@]4(CC)C=CCN([C@H]34)CC2)(O)C(=O)OC)N2C)=C2C=C1OC GBABOYUKABKIAF-GHYRFKGUSA-N 0.000 description 1
• 238000012800 visualization Methods 0.000 description 1
• 210000003905 vulva Anatomy 0.000 description 1
• 230000029663 wound healing Effects 0.000 description 1