JP7596069B2 - 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 - Google Patents
付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 Download PDFInfo
- Publication number
- JP7596069B2 JP7596069B2 JP2019550715A JP2019550715A JP7596069B2 JP 7596069 B2 JP7596069 B2 JP 7596069B2 JP 2019550715 A JP2019550715 A JP 2019550715A JP 2019550715 A JP2019550715 A JP 2019550715A JP 7596069 B2 JP7596069 B2 JP 7596069B2
- Authority
- JP
- Japan
- Prior art keywords
- box
- high mobility
- mobility group
- modified high
- antibody
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 238000000034 method Methods 0.000 title claims description 174
- 239000000203 mixture Substances 0.000 title claims description 93
- 230000001580 bacterial effect Effects 0.000 title description 23
- 206010061218 Inflammation Diseases 0.000 title description 7
- 230000004054 inflammatory process Effects 0.000 title description 7
- 101001025337 Homo sapiens High mobility group protein B1 Proteins 0.000 claims description 172
- 102100037907 High mobility group protein B1 Human genes 0.000 claims description 170
- 238000006467 substitution reaction Methods 0.000 claims description 139
- 102220491845 Cilia- and flagella-associated protein HOATZ_C23S_mutation Human genes 0.000 claims description 118
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 115
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 102
- 229920001184 polypeptide Polymers 0.000 claims description 97
- 102220491822 High mobility group protein B1_C106S_mutation Human genes 0.000 claims description 94
- 230000027455 binding Effects 0.000 claims description 75
- 108020004414 DNA Proteins 0.000 claims description 73
- 230000000813 microbial effect Effects 0.000 claims description 47
- 208000015181 infectious disease Diseases 0.000 claims description 45
- 238000000338 in vitro Methods 0.000 claims description 41
- 238000001727 in vivo Methods 0.000 claims description 38
- 241000371430 Burkholderia cenocepacia Species 0.000 claims description 30
- 239000003242 anti bacterial agent Substances 0.000 claims description 29
- 230000002401 inhibitory effect Effects 0.000 claims description 26
- 241000588724 Escherichia coli Species 0.000 claims description 24
- 241000588914 Enterobacter Species 0.000 claims description 16
- 241000194031 Enterococcus faecium Species 0.000 claims description 16
- 230000003115 biocidal effect Effects 0.000 claims description 16
- 241000606749 Aggregatibacter actinomycetemcomitans Species 0.000 claims description 15
- 241000589517 Pseudomonas aeruginosa Species 0.000 claims description 15
- 241000191967 Staphylococcus aureus Species 0.000 claims description 15
- 241000588626 Acinetobacter baumannii Species 0.000 claims description 14
- 241000606768 Haemophilus influenzae Species 0.000 claims description 14
- 241000588747 Klebsiella pneumoniae Species 0.000 claims description 14
- 229940047650 haemophilus influenzae Drugs 0.000 claims description 14
- 208000035143 Bacterial infection Diseases 0.000 claims description 12
- 208000022362 bacterial infectious disease Diseases 0.000 claims description 12
- 102000053602 DNA Human genes 0.000 claims description 9
- 230000015572 biosynthetic process Effects 0.000 claims description 8
- 239000011248 coating agent Substances 0.000 claims description 8
- 238000000576 coating method Methods 0.000 claims description 8
- 244000005700 microbiome Species 0.000 claims description 8
- 102220491808 Cilia- and flagella-associated protein HOATZ_C45S_mutation Human genes 0.000 claims 9
- 108090000623 proteins and genes Proteins 0.000 description 101
- 102000004169 proteins and genes Human genes 0.000 description 87
- 235000018102 proteins Nutrition 0.000 description 80
- 239000000427 antigen Substances 0.000 description 66
- 108091007433 antigens Proteins 0.000 description 64
- 102000036639 antigens Human genes 0.000 description 64
- 210000004027 cell Anatomy 0.000 description 60
- 102000040430 polynucleotide Human genes 0.000 description 56
- 108091033319 polynucleotide Proteins 0.000 description 56
- 239000002157 polynucleotide Substances 0.000 description 56
- 235000001014 amino acid Nutrition 0.000 description 43
- 102100022128 High mobility group protein B2 Human genes 0.000 description 34
- 101001045791 Homo sapiens High mobility group protein B2 Proteins 0.000 description 34
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 34
- 239000013598 vector Substances 0.000 description 32
- 229940024606 amino acid Drugs 0.000 description 31
- 150000001413 amino acids Chemical class 0.000 description 31
- 102100022130 High mobility group protein B3 Human genes 0.000 description 29
- 101001045794 Homo sapiens High mobility group protein B3 Proteins 0.000 description 29
- 125000003275 alpha amino acid group Chemical group 0.000 description 28
- 150000007523 nucleic acids Chemical class 0.000 description 28
- 102100022124 High mobility group protein B4 Human genes 0.000 description 27
- 101001045782 Homo sapiens High mobility group protein B4 Proteins 0.000 description 27
- 108060003951 Immunoglobulin Proteins 0.000 description 27
- 230000000694 effects Effects 0.000 description 27
- 239000012634 fragment Substances 0.000 description 27
- 102000018358 immunoglobulin Human genes 0.000 description 27
- 239000003795 chemical substances by application Substances 0.000 description 26
- 238000011282 treatment Methods 0.000 description 26
- 102000039446 nucleic acids Human genes 0.000 description 24
- 108020004707 nucleic acids Proteins 0.000 description 24
- -1 Nucleic Acid Acids Chemical class 0.000 description 23
- 235000018417 cysteine Nutrition 0.000 description 23
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 22
- 241001465754 Metazoa Species 0.000 description 21
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 21
- 241000894006 Bacteria Species 0.000 description 20
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 20
- 230000028993 immune response Effects 0.000 description 20
- 241000894007 species Species 0.000 description 20
- 230000006870 function Effects 0.000 description 19
- 210000004602 germ cell Anatomy 0.000 description 18
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 18
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 17
- 229940088710 antibiotic agent Drugs 0.000 description 17
- 230000001225 therapeutic effect Effects 0.000 description 17
- 239000002671 adjuvant Substances 0.000 description 16
- 239000004599 antimicrobial Substances 0.000 description 15
- 210000000440 neutrophil Anatomy 0.000 description 15
- 239000000126 substance Substances 0.000 description 15
- 201000010099 disease Diseases 0.000 description 14
- 241000699666 Mus <mouse, genus> Species 0.000 description 13
- 125000000539 amino acid group Chemical group 0.000 description 13
- 150000001875 compounds Chemical class 0.000 description 13
- 239000003814 drug Substances 0.000 description 13
- 230000002163 immunogen Effects 0.000 description 13
- 238000004519 manufacturing process Methods 0.000 description 13
- 102000004190 Enzymes Human genes 0.000 description 12
- 108090000790 Enzymes Proteins 0.000 description 12
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 12
- 241000282412 Homo Species 0.000 description 12
- 229940088598 enzyme Drugs 0.000 description 12
- 230000004048 modification Effects 0.000 description 12
- 238000012986 modification Methods 0.000 description 12
- 230000004044 response Effects 0.000 description 12
- 239000002202 Polyethylene glycol Substances 0.000 description 11
- 239000000969 carrier Substances 0.000 description 11
- 238000005516 engineering process Methods 0.000 description 11
- 210000004408 hybridoma Anatomy 0.000 description 11
- 239000000463 material Substances 0.000 description 11
- 229920001223 polyethylene glycol Polymers 0.000 description 11
- 230000008569 process Effects 0.000 description 11
- 210000001519 tissue Anatomy 0.000 description 11
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 10
- 241000196324 Embryophyta Species 0.000 description 10
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 10
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 10
- 206010033078 Otitis media Diseases 0.000 description 10
- 210000000959 ear middle Anatomy 0.000 description 10
- 230000037230 mobility Effects 0.000 description 10
- 125000003729 nucleotide group Chemical group 0.000 description 10
- 102000016911 Deoxyribonucleases Human genes 0.000 description 9
- 108010053770 Deoxyribonucleases Proteins 0.000 description 9
- 238000010171 animal model Methods 0.000 description 9
- 230000036039 immunity Effects 0.000 description 9
- 230000028709 inflammatory response Effects 0.000 description 9
- 210000004072 lung Anatomy 0.000 description 9
- 230000002829 reductive effect Effects 0.000 description 9
- 230000001177 retroviral effect Effects 0.000 description 9
- 238000012360 testing method Methods 0.000 description 9
- 230000009261 transgenic effect Effects 0.000 description 9
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 8
- 241000699670 Mus sp. Species 0.000 description 8
- 230000003214 anti-biofilm Effects 0.000 description 8
- 238000003556 assay Methods 0.000 description 8
- 239000000872 buffer Substances 0.000 description 8
- 208000035475 disorder Diseases 0.000 description 8
- 239000003937 drug carrier Substances 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- 230000009467 reduction Effects 0.000 description 8
- 230000000699 topical effect Effects 0.000 description 8
- 108010015268 Integration Host Factors Proteins 0.000 description 7
- 230000000890 antigenic effect Effects 0.000 description 7
- 239000003638 chemical reducing agent Substances 0.000 description 7
- 239000003085 diluting agent Substances 0.000 description 7
- 239000003623 enhancer Substances 0.000 description 7
- 239000007850 fluorescent dye Substances 0.000 description 7
- 230000014509 gene expression Effects 0.000 description 7
- 230000013595 glycosylation Effects 0.000 description 7
- 238000006206 glycosylation reaction Methods 0.000 description 7
- 238000009396 hybridization Methods 0.000 description 7
- 230000001965 increasing effect Effects 0.000 description 7
- 238000001990 intravenous administration Methods 0.000 description 7
- 239000003446 ligand Substances 0.000 description 7
- 230000000670 limiting effect Effects 0.000 description 7
- 230000001404 mediated effect Effects 0.000 description 7
- DYKFCLLONBREIL-KVUCHLLUSA-N minocycline Chemical compound C([C@H]1C2)C3=C(N(C)C)C=CC(O)=C3C(=O)C1=C(O)[C@@]1(O)[C@@H]2[C@H](N(C)C)C(O)=C(C(N)=O)C1=O DYKFCLLONBREIL-KVUCHLLUSA-N 0.000 description 7
- 229960004023 minocycline Drugs 0.000 description 7
- 239000002773 nucleotide Substances 0.000 description 7
- 238000004806 packaging method and process Methods 0.000 description 7
- 238000002360 preparation method Methods 0.000 description 7
- 230000002285 radioactive effect Effects 0.000 description 7
- 238000002560 therapeutic procedure Methods 0.000 description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 6
- 101710117290 Aldo-keto reductase family 1 member C4 Proteins 0.000 description 6
- 238000011740 C57BL/6 mouse Methods 0.000 description 6
- 108091035707 Consensus sequence Proteins 0.000 description 6
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 6
- 239000004471 Glycine Substances 0.000 description 6
- 241000124008 Mammalia Species 0.000 description 6
- 239000004793 Polystyrene Substances 0.000 description 6
- 241000700159 Rattus Species 0.000 description 6
- 230000000295 complement effect Effects 0.000 description 6
- 229940079593 drug Drugs 0.000 description 6
- 238000009472 formulation Methods 0.000 description 6
- 230000005847 immunogenicity Effects 0.000 description 6
- 239000013612 plasmid Substances 0.000 description 6
- 229920002223 polystyrene Polymers 0.000 description 6
- 230000009870 specific binding Effects 0.000 description 6
- 229940124597 therapeutic agent Drugs 0.000 description 6
- 238000013518 transcription Methods 0.000 description 6
- 230000035897 transcription Effects 0.000 description 6
- 238000012546 transfer Methods 0.000 description 6
- 238000012384 transportation and delivery Methods 0.000 description 6
- 229920002307 Dextran Polymers 0.000 description 5
- 241000713813 Gibbon ape leukemia virus Species 0.000 description 5
- 241000713869 Moloney murine leukemia virus Species 0.000 description 5
- 206010028980 Neoplasm Diseases 0.000 description 5
- 241000283973 Oryctolagus cuniculus Species 0.000 description 5
- 241000700605 Viruses Species 0.000 description 5
- 238000013459 approach Methods 0.000 description 5
- 210000003719 b-lymphocyte Anatomy 0.000 description 5
- 229960002685 biotin Drugs 0.000 description 5
- 235000020958 biotin Nutrition 0.000 description 5
- 239000011616 biotin Substances 0.000 description 5
- 238000004113 cell culture Methods 0.000 description 5
- 229920002678 cellulose Polymers 0.000 description 5
- 235000010980 cellulose Nutrition 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 230000001684 chronic effect Effects 0.000 description 5
- 239000002299 complementary DNA Substances 0.000 description 5
- 238000001218 confocal laser scanning microscopy Methods 0.000 description 5
- 230000004927 fusion Effects 0.000 description 5
- 230000036541 health Effects 0.000 description 5
- 244000052637 human pathogen Species 0.000 description 5
- 239000007943 implant Substances 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- 230000001939 inductive effect Effects 0.000 description 5
- 230000002757 inflammatory effect Effects 0.000 description 5
- 239000007924 injection Substances 0.000 description 5
- 238000002347 injection Methods 0.000 description 5
- 230000035772 mutation Effects 0.000 description 5
- 210000003200 peritoneal cavity Anatomy 0.000 description 5
- 239000008194 pharmaceutical composition Substances 0.000 description 5
- 230000004481 post-translational protein modification Effects 0.000 description 5
- 238000000746 purification Methods 0.000 description 5
- 238000010188 recombinant method Methods 0.000 description 5
- 239000000523 sample Substances 0.000 description 5
- 239000000725 suspension Substances 0.000 description 5
- 239000002028 Biomass Substances 0.000 description 4
- 108090000994 Catalytic RNA Proteins 0.000 description 4
- 102000053642 Catalytic RNA Human genes 0.000 description 4
- 241000700114 Chinchillidae Species 0.000 description 4
- 201000003883 Cystic fibrosis Diseases 0.000 description 4
- 230000004568 DNA-binding Effects 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
- 101001046686 Homo sapiens Integrin alpha-M Proteins 0.000 description 4
- 102100034353 Integrase Human genes 0.000 description 4
- 102100022338 Integrin alpha-M Human genes 0.000 description 4
- 101001065556 Mus musculus Lymphocyte antigen 6G Proteins 0.000 description 4
- 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 4
- 108091028043 Nucleic acid sequence Proteins 0.000 description 4
- 239000004677 Nylon Substances 0.000 description 4
- 108091034117 Oligonucleotide Proteins 0.000 description 4
- 206010035664 Pneumonia Diseases 0.000 description 4
- 239000004698 Polyethylene Substances 0.000 description 4
- 239000004743 Polypropylene Substances 0.000 description 4
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 102000040945 Transcription factor Human genes 0.000 description 4
- 108091023040 Transcription factor Proteins 0.000 description 4
- 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 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000000845 anti-microbial effect Effects 0.000 description 4
- 239000011324 bead Substances 0.000 description 4
- 230000032770 biofilm formation Effects 0.000 description 4
- 230000037396 body weight Effects 0.000 description 4
- 201000011510 cancer Diseases 0.000 description 4
- 230000001413 cellular effect Effects 0.000 description 4
- 230000004700 cellular uptake Effects 0.000 description 4
- 239000002738 chelating agent Substances 0.000 description 4
- 230000001419 dependent effect Effects 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 230000018109 developmental process Effects 0.000 description 4
- 108010078428 env Gene Products Proteins 0.000 description 4
- 210000003527 eukaryotic cell Anatomy 0.000 description 4
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 4
- 239000000499 gel Substances 0.000 description 4
- 230000002068 genetic effect Effects 0.000 description 4
- 239000011521 glass Substances 0.000 description 4
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 4
- 238000004128 high performance liquid chromatography Methods 0.000 description 4
- 102000053637 human HMGB1 Human genes 0.000 description 4
- 210000000987 immune system Anatomy 0.000 description 4
- 238000011081 inoculation Methods 0.000 description 4
- 210000004698 lymphocyte Anatomy 0.000 description 4
- 229920002521 macromolecule Polymers 0.000 description 4
- 210000004962 mammalian cell Anatomy 0.000 description 4
- 210000004379 membrane Anatomy 0.000 description 4
- 239000012528 membrane Substances 0.000 description 4
- 108020004999 messenger RNA Proteins 0.000 description 4
- 230000005012 migration Effects 0.000 description 4
- 238000013508 migration Methods 0.000 description 4
- 238000002703 mutagenesis Methods 0.000 description 4
- 231100000350 mutagenesis Toxicity 0.000 description 4
- 210000004940 nucleus Anatomy 0.000 description 4
- 229920001778 nylon Polymers 0.000 description 4
- 238000011275 oncology therapy Methods 0.000 description 4
- 230000003647 oxidation Effects 0.000 description 4
- 238000007254 oxidation reaction Methods 0.000 description 4
- 230000006320 pegylation Effects 0.000 description 4
- 230000026731 phosphorylation Effects 0.000 description 4
- 238000006366 phosphorylation reaction Methods 0.000 description 4
- 229920002401 polyacrylamide Polymers 0.000 description 4
- 229920000573 polyethylene Polymers 0.000 description 4
- 229920001155 polypropylene Polymers 0.000 description 4
- 210000001236 prokaryotic cell Anatomy 0.000 description 4
- 230000000069 prophylactic effect Effects 0.000 description 4
- 108091092562 ribozyme Proteins 0.000 description 4
- 210000003491 skin Anatomy 0.000 description 4
- 235000002639 sodium chloride Nutrition 0.000 description 4
- 239000007787 solid Substances 0.000 description 4
- 239000003053 toxin Substances 0.000 description 4
- 231100000765 toxin Toxicity 0.000 description 4
- 108700012359 toxins Proteins 0.000 description 4
- 238000011830 transgenic mouse model Methods 0.000 description 4
- 238000013519 translation Methods 0.000 description 4
- 230000003612 virological effect Effects 0.000 description 4
- FDKXTQMXEQVLRF-ZHACJKMWSA-N (E)-dacarbazine Chemical compound CN(C)\N=N\c1[nH]cnc1C(N)=O FDKXTQMXEQVLRF-ZHACJKMWSA-N 0.000 description 3
- 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 3
- 102000013142 Amylases Human genes 0.000 description 3
- 108010065511 Amylases Proteins 0.000 description 3
- 241000282693 Cercopithecidae Species 0.000 description 3
- 241000700112 Chinchilla Species 0.000 description 3
- 102000052510 DNA-Binding Proteins Human genes 0.000 description 3
- 108010092160 Dactinomycin Proteins 0.000 description 3
- 241000233866 Fungi Species 0.000 description 3
- 241000238631 Hexapoda Species 0.000 description 3
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 3
- 241000725303 Human immunodeficiency virus Species 0.000 description 3
- 241000699660 Mus musculus Species 0.000 description 3
- 244000061176 Nicotiana tabacum Species 0.000 description 3
- 235000002637 Nicotiana tabacum Nutrition 0.000 description 3
- 241000288906 Primates Species 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 108010039491 Ricin Proteins 0.000 description 3
- 108010092262 T-Cell Antigen Receptors Proteins 0.000 description 3
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 3
- 230000021736 acetylation Effects 0.000 description 3
- 238000006640 acetylation reaction Methods 0.000 description 3
- 230000002378 acidificating effect Effects 0.000 description 3
- 238000005917 acylation reaction Methods 0.000 description 3
- 238000007792 addition Methods 0.000 description 3
- 235000019418 amylase Nutrition 0.000 description 3
- 210000000628 antibody-producing cell Anatomy 0.000 description 3
- 230000004071 biological effect Effects 0.000 description 3
- 230000033228 biological regulation Effects 0.000 description 3
- 230000005540 biological transmission Effects 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 150000001720 carbohydrates Chemical class 0.000 description 3
- 239000001913 cellulose Substances 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 230000001268 conjugating effect Effects 0.000 description 3
- 230000021615 conjugation Effects 0.000 description 3
- 230000001086 cytosolic effect Effects 0.000 description 3
- 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 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- 239000004053 dental implant Substances 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 235000014113 dietary fatty acids Nutrition 0.000 description 3
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 3
- 238000012377 drug delivery Methods 0.000 description 3
- 108700004025 env Genes Proteins 0.000 description 3
- 150000002148 esters Chemical class 0.000 description 3
- 229930195729 fatty acid Natural products 0.000 description 3
- 239000000194 fatty acid Substances 0.000 description 3
- 150000004665 fatty acids Chemical class 0.000 description 3
- 210000002865 immune cell Anatomy 0.000 description 3
- 230000003053 immunization Effects 0.000 description 3
- 230000016784 immunoglobulin production Effects 0.000 description 3
- 229940072221 immunoglobulins Drugs 0.000 description 3
- 230000008595 infiltration Effects 0.000 description 3
- 238000001764 infiltration Methods 0.000 description 3
- 210000004969 inflammatory cell Anatomy 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- SZVJSHCCFOBDDC-UHFFFAOYSA-N iron(II,III) oxide Inorganic materials O=[Fe]O[Fe]O[Fe]=O SZVJSHCCFOBDDC-UHFFFAOYSA-N 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 230000002147 killing effect Effects 0.000 description 3
- 238000002372 labelling Methods 0.000 description 3
- 229910021645 metal ion Inorganic materials 0.000 description 3
- 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 3
- 229960004857 mitomycin Drugs 0.000 description 3
- 239000012188 paraffin wax Substances 0.000 description 3
- 238000007911 parenteral administration Methods 0.000 description 3
- 230000036961 partial effect Effects 0.000 description 3
- 239000000546 pharmaceutical excipient Substances 0.000 description 3
- 239000002953 phosphate buffered saline Substances 0.000 description 3
- 229960003171 plicamycin Drugs 0.000 description 3
- 239000003755 preservative agent Substances 0.000 description 3
- 238000003259 recombinant expression Methods 0.000 description 3
- 230000006798 recombination Effects 0.000 description 3
- 230000000306 recurrent effect Effects 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 238000003860 storage Methods 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 230000002195 synergetic effect Effects 0.000 description 3
- 230000009885 systemic effect Effects 0.000 description 3
- 208000019206 urinary tract infection Diseases 0.000 description 3
- IAKHMKGGTNLKSZ-INIZCTEOSA-N (S)-colchicine Chemical compound C1([C@@H](NC(C)=O)CC2)=CC(=O)C(OC)=CC=C1C1=C2C=C(OC)C(OC)=C1OC IAKHMKGGTNLKSZ-INIZCTEOSA-N 0.000 description 2
- KIUMMUBSPKGMOY-UHFFFAOYSA-N 3,3'-Dithiobis(6-nitrobenzoic acid) Chemical compound C1=C([N+]([O-])=O)C(C(=O)O)=CC(SSC=2C=C(C(=CC=2)[N+]([O-])=O)C(O)=O)=C1 KIUMMUBSPKGMOY-UHFFFAOYSA-N 0.000 description 2
- VPFUWHKTPYPNGT-UHFFFAOYSA-N 3-(3,4-dihydroxyphenyl)-1-(5-hydroxy-2,2-dimethylchromen-6-yl)propan-1-one Chemical compound OC1=C2C=CC(C)(C)OC2=CC=C1C(=O)CCC1=CC=C(O)C(O)=C1 VPFUWHKTPYPNGT-UHFFFAOYSA-N 0.000 description 2
- VXPSQDAMFATNNG-UHFFFAOYSA-N 3-[2-(2,5-dioxopyrrol-3-yl)phenyl]pyrrole-2,5-dione Chemical compound O=C1NC(=O)C(C=2C(=CC=CC=2)C=2C(NC(=O)C=2)=O)=C1 VXPSQDAMFATNNG-UHFFFAOYSA-N 0.000 description 2
- 230000005730 ADP ribosylation Effects 0.000 description 2
- 108010000239 Aequorin Proteins 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- 244000105975 Antidesma platyphyllum Species 0.000 description 2
- 108091023037 Aptamer Proteins 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- 108090001008 Avidin Proteins 0.000 description 2
- 102000004506 Blood Proteins Human genes 0.000 description 2
- 108010017384 Blood Proteins Proteins 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 241000282465 Canis Species 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 241000700198 Cavia Species 0.000 description 2
- 108010049048 Cholera Toxin Proteins 0.000 description 2
- 102000009016 Cholera Toxin Human genes 0.000 description 2
- 108010077544 Chromatin Proteins 0.000 description 2
- 101710094648 Coat protein Proteins 0.000 description 2
- 208000003322 Coinfection Diseases 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 2
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 2
- 108700020911 DNA-Binding Proteins Proteins 0.000 description 2
- 101710141836 DNA-binding protein HU homolog Proteins 0.000 description 2
- 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 2
- 241000283073 Equus caballus Species 0.000 description 2
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 2
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 2
- 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 2
- 108010024636 Glutathione Proteins 0.000 description 2
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 2
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 2
- 108010033040 Histones Proteins 0.000 description 2
- 108090000144 Human Proteins Proteins 0.000 description 2
- 102000003839 Human Proteins Human genes 0.000 description 2
- 102000008100 Human Serum Albumin Human genes 0.000 description 2
- 108091006905 Human Serum Albumin Proteins 0.000 description 2
- GQYIWUVLTXOXAJ-UHFFFAOYSA-N Lomustine Chemical compound ClCCN(N=O)C(=O)NC1CCCCC1 GQYIWUVLTXOXAJ-UHFFFAOYSA-N 0.000 description 2
- 108060001084 Luciferase Proteins 0.000 description 2
- 239000005089 Luciferase Substances 0.000 description 2
- 102000004857 Lymphoid enhancer-binding factor 1 Human genes 0.000 description 2
- 108090001093 Lymphoid enhancer-binding factor 1 Proteins 0.000 description 2
- 229930195725 Mannitol Natural products 0.000 description 2
- 229930192392 Mitomycin Natural products 0.000 description 2
- 101710174628 Modulating protein YmoA Proteins 0.000 description 2
- 241000713862 Moloney murine sarcoma virus Species 0.000 description 2
- 241001529936 Murinae Species 0.000 description 2
- 241001494479 Pecora Species 0.000 description 2
- 206010035226 Plasma cell myeloma Diseases 0.000 description 2
- 108010029485 Protein Isoforms Proteins 0.000 description 2
- 102000001708 Protein Isoforms Human genes 0.000 description 2
- RADKZDMFGJYCBB-UHFFFAOYSA-N Pyridoxal Chemical compound CC1=NC=C(CO)C(C=O)=C1O RADKZDMFGJYCBB-UHFFFAOYSA-N 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 108010083644 Ribonucleases Proteins 0.000 description 2
- 102000006382 Ribonucleases Human genes 0.000 description 2
- 241000283984 Rodentia Species 0.000 description 2
- 241000714474 Rous sarcoma virus Species 0.000 description 2
- 206010040047 Sepsis Diseases 0.000 description 2
- 102100022978 Sex-determining region Y protein Human genes 0.000 description 2
- 101710188553 Sex-determining region Y protein Proteins 0.000 description 2
- 241000713880 Spleen focus-forming virus Species 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 2
- 102000008685 T Cell Transcription Factor 1 Human genes 0.000 description 2
- 108010088184 T Cell Transcription Factor 1 Proteins 0.000 description 2
- 108020004566 Transfer RNA Proteins 0.000 description 2
- VGQOVCHZGQWAOI-UHFFFAOYSA-N UNPD55612 Natural products N1C(O)C2CC(C=CC(N)=O)=CN2C(=O)C2=CC=C(C)C(O)=C12 VGQOVCHZGQWAOI-UHFFFAOYSA-N 0.000 description 2
- 241000711975 Vesicular stomatitis virus Species 0.000 description 2
- 240000008042 Zea mays Species 0.000 description 2
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 2
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 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 2
- 230000001154 acute effect Effects 0.000 description 2
- 230000010933 acylation Effects 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 238000005804 alkylation reaction Methods 0.000 description 2
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 2
- 125000003277 amino group Chemical group 0.000 description 2
- 229940025131 amylases Drugs 0.000 description 2
- VGQOVCHZGQWAOI-HYUHUPJXSA-N anthramycin Chemical compound N1[C@@H](O)[C@@H]2CC(\C=C\C(N)=O)=CN2C(=O)C2=CC=C(C)C(O)=C12 VGQOVCHZGQWAOI-HYUHUPJXSA-N 0.000 description 2
- 230000000692 anti-sense effect Effects 0.000 description 2
- 239000003963 antioxidant agent Substances 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 2
- 239000007975 buffered saline Substances 0.000 description 2
- 239000002775 capsule Substances 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000007795 chemical reaction product Substances 0.000 description 2
- 210000003483 chromatin Anatomy 0.000 description 2
- 238000002648 combination therapy Methods 0.000 description 2
- 235000005822 corn Nutrition 0.000 description 2
- 230000007797 corrosion Effects 0.000 description 2
- 238000005260 corrosion Methods 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
- 239000003431 cross linking reagent Substances 0.000 description 2
- 150000001945 cysteines Chemical class 0.000 description 2
- 229940127089 cytotoxic agent Drugs 0.000 description 2
- 239000002254 cytotoxic agent Substances 0.000 description 2
- 231100000599 cytotoxic agent Toxicity 0.000 description 2
- 229960000640 dactinomycin Drugs 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 229960000975 daunorubicin Drugs 0.000 description 2
- 208000002925 dental caries Diseases 0.000 description 2
- CFCUWKMKBJTWLW-UHFFFAOYSA-N deoliosyl-3C-alpha-L-digitoxosyl-MTM Natural products CC=1C(O)=C2C(O)=C3C(=O)C(OC4OC(C)C(O)C(OC5OC(C)C(O)C(OC6OC(C)C(O)C(C)(O)C6)C5)C4)C(C(OC)C(=O)C(O)C(C)O)CC3=CC2=CC=1OC(OC(C)C1O)CC1OC1CC(O)C(O)C(C)O1 CFCUWKMKBJTWLW-UHFFFAOYSA-N 0.000 description 2
- 238000003745 diagnosis Methods 0.000 description 2
- 239000000032 diagnostic agent Substances 0.000 description 2
- 229940039227 diagnostic agent Drugs 0.000 description 2
- 229960004679 doxorubicin Drugs 0.000 description 2
- 239000000975 dye Substances 0.000 description 2
- 239000002158 endotoxin Substances 0.000 description 2
- 101150030339 env gene Proteins 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 210000002744 extracellular matrix Anatomy 0.000 description 2
- 108091006047 fluorescent proteins Proteins 0.000 description 2
- 102000034287 fluorescent proteins Human genes 0.000 description 2
- 125000000524 functional group Chemical group 0.000 description 2
- 230000002538 fungal effect Effects 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 239000007789 gas Substances 0.000 description 2
- 210000001035 gastrointestinal tract Anatomy 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 229960003180 glutathione Drugs 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 239000005090 green fluorescent protein Substances 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 235000009424 haa Nutrition 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 238000007918 intramuscular administration Methods 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- FZWBNHMXJMCXLU-BLAUPYHCSA-N isomaltotriose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@@H](OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C=O)O1 FZWBNHMXJMCXLU-BLAUPYHCSA-N 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 229920006008 lipopolysaccharide Polymers 0.000 description 2
- 210000001165 lymph node Anatomy 0.000 description 2
- 239000000594 mannitol Substances 0.000 description 2
- 235000010355 mannitol Nutrition 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- GLVAUDGFNGKCSF-UHFFFAOYSA-N mercaptopurine Chemical compound S=C1NC=NC2=C1NC=N2 GLVAUDGFNGKCSF-UHFFFAOYSA-N 0.000 description 2
- 230000011987 methylation Effects 0.000 description 2
- 238000007069 methylation reaction Methods 0.000 description 2
- 229960001156 mitoxantrone Drugs 0.000 description 2
- 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 2
- 108010010621 modeccin Proteins 0.000 description 2
- 238000001823 molecular biology technique Methods 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 229940035032 monophosphoryl lipid a Drugs 0.000 description 2
- 201000000050 myeloid neoplasm Diseases 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 238000007899 nucleic acid hybridization Methods 0.000 description 2
- 239000003921 oil Substances 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 244000052769 pathogen Species 0.000 description 2
- 239000000816 peptidomimetic Substances 0.000 description 2
- 201000001245 periodontitis Diseases 0.000 description 2
- 210000005259 peripheral blood Anatomy 0.000 description 2
- 239000011886 peripheral blood Substances 0.000 description 2
- 239000003208 petroleum Substances 0.000 description 2
- 239000000825 pharmaceutical preparation Substances 0.000 description 2
- 230000008488 polyadenylation Effects 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 229920001282 polysaccharide Polymers 0.000 description 2
- 239000005017 polysaccharide Substances 0.000 description 2
- 230000000770 proinflammatory effect Effects 0.000 description 2
- AQHHHDLHHXJYJD-UHFFFAOYSA-N propranolol Chemical compound C1=CC=C2C(OCC(O)CNC(C)C)=CC=CC2=C1 AQHHHDLHHXJYJD-UHFFFAOYSA-N 0.000 description 2
- 230000001681 protective effect Effects 0.000 description 2
- 230000006337 proteolytic cleavage Effects 0.000 description 2
- RXWNCPJZOCPEPQ-NVWDDTSBSA-N puromycin Chemical compound C1=CC(OC)=CC=C1C[C@H](N)C(=O)N[C@H]1[C@@H](O)[C@H](N2C3=NC=NC(=C3N=C2)N(C)C)O[C@@H]1CO RXWNCPJZOCPEPQ-NVWDDTSBSA-N 0.000 description 2
- BBEAQIROQSPTKN-UHFFFAOYSA-N pyrene Chemical compound C1=CC=C2C=CC3=CC=CC4=CC=C1C2=C43 BBEAQIROQSPTKN-UHFFFAOYSA-N 0.000 description 2
- 239000012857 radioactive material Substances 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 210000002345 respiratory system Anatomy 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000007790 solid phase Substances 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 208000024891 symptom Diseases 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 230000002194 synthesizing effect Effects 0.000 description 2
- ZFXYFBGIUFBOJW-UHFFFAOYSA-N theophylline Chemical compound O=C1N(C)C(=O)N(C)C2=C1NC=N2 ZFXYFBGIUFBOJW-UHFFFAOYSA-N 0.000 description 2
- CWERGRDVMFNCDR-UHFFFAOYSA-M thioglycolate(1-) Chemical compound [O-]C(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-M 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- WYWHKKSPHMUBEB-UHFFFAOYSA-N tioguanine Chemical compound N1C(N)=NC(=S)C2=C1N=CN2 WYWHKKSPHMUBEB-UHFFFAOYSA-N 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 241001515965 unidentified phage Species 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- 239000013603 viral vector Substances 0.000 description 2
- PCHJSUWPFVWCPO-NJFSPNSNSA-N (199au)gold Chemical compound [199Au] PCHJSUWPFVWCPO-NJFSPNSNSA-N 0.000 description 1
- FLCQLSRLQIPNLM-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 2-acetylsulfanylacetate Chemical compound CC(=O)SCC(=O)ON1C(=O)CCC1=O FLCQLSRLQIPNLM-UHFFFAOYSA-N 0.000 description 1
- JWDFQMWEFLOOED-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 3-(pyridin-2-yldisulfanyl)propanoate Chemical compound O=C1CCC(=O)N1OC(=O)CCSSC1=CC=CC=N1 JWDFQMWEFLOOED-UHFFFAOYSA-N 0.000 description 1
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- BEJKOYIMCGMNRB-GRHHLOCNSA-N (2s)-2-amino-3-(4-hydroxyphenyl)propanoic acid;(2s)-2-amino-3-phenylpropanoic acid Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1.OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 BEJKOYIMCGMNRB-GRHHLOCNSA-N 0.000 description 1
- YUXKOWPNKJSTPQ-AXWWPMSFSA-N (2s,3r)-2-amino-3-hydroxybutanoic acid;(2s)-2-amino-3-hydroxypropanoic acid Chemical compound OC[C@H](N)C(O)=O.C[C@@H](O)[C@H](N)C(O)=O YUXKOWPNKJSTPQ-AXWWPMSFSA-N 0.000 description 1
- QJVHTELASVOWBE-AGNWQMPPSA-N (2s,5r,6r)-6-[[(2r)-2-amino-2-(4-hydroxyphenyl)acetyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid;(2r,3z,5r)-3-(2-hydroxyethylidene)-7-oxo-4-oxa-1-azabicyclo[3.2.0]heptane-2-carboxylic acid Chemical compound OC(=O)[C@H]1C(=C/CO)/O[C@@H]2CC(=O)N21.C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=C(O)C=C1 QJVHTELASVOWBE-AGNWQMPPSA-N 0.000 description 1
- YYGNTYWPHWGJRM-UHFFFAOYSA-N (6E,10E,14E,18E)-2,6,10,15,19,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene Chemical compound CC(C)=CCCC(C)=CCCC(C)=CCCC=C(C)CCC=C(C)CCC=C(C)C YYGNTYWPHWGJRM-UHFFFAOYSA-N 0.000 description 1
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- VSNHCAURESNICA-NJFSPNSNSA-N 1-oxidanylurea Chemical compound N[14C](=O)NO VSNHCAURESNICA-NJFSPNSNSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- PNDPGZBMCMUPRI-HVTJNCQCSA-N 10043-66-0 Chemical compound [131I][131I] PNDPGZBMCMUPRI-HVTJNCQCSA-N 0.000 description 1
- WUAPFZMCVAUBPE-NJFSPNSNSA-N 188Re Chemical compound [188Re] WUAPFZMCVAUBPE-NJFSPNSNSA-N 0.000 description 1
- CHHHXKFHOYLYRE-UHFFFAOYSA-M 2,4-Hexadienoic acid, potassium salt (1:1), (2E,4E)- Chemical compound [K+].CC=CC=CC([O-])=O CHHHXKFHOYLYRE-UHFFFAOYSA-M 0.000 description 1
- UFBJCMHMOXMLKC-UHFFFAOYSA-N 2,4-dinitrophenol Chemical compound OC1=CC=C([N+]([O-])=O)C=C1[N+]([O-])=O UFBJCMHMOXMLKC-UHFFFAOYSA-N 0.000 description 1
- 150000003923 2,5-pyrrolediones Chemical class 0.000 description 1
- FBUTXZSKZCQABC-UHFFFAOYSA-N 2-amino-1-methyl-7h-purine-6-thione Chemical compound S=C1N(C)C(N)=NC2=C1NC=N2 FBUTXZSKZCQABC-UHFFFAOYSA-N 0.000 description 1
- GOLORTLGFDVFDW-UHFFFAOYSA-N 3-(1h-benzimidazol-2-yl)-7-(diethylamino)chromen-2-one Chemical compound C1=CC=C2NC(C3=CC4=CC=C(C=C4OC3=O)N(CC)CC)=NC2=C1 GOLORTLGFDVFDW-UHFFFAOYSA-N 0.000 description 1
- VIIIJFZJKFXOGG-UHFFFAOYSA-N 3-methylchromen-2-one Chemical compound C1=CC=C2OC(=O)C(C)=CC2=C1 VIIIJFZJKFXOGG-UHFFFAOYSA-N 0.000 description 1
- WZRJTRPJURQBRM-UHFFFAOYSA-N 4-amino-n-(5-methyl-1,2-oxazol-3-yl)benzenesulfonamide;5-[(3,4,5-trimethoxyphenyl)methyl]pyrimidine-2,4-diamine Chemical compound O1C(C)=CC(NS(=O)(=O)C=2C=CC(N)=CC=2)=N1.COC1=C(OC)C(OC)=CC(CC=2C(=NC(N)=NC=2)N)=C1 WZRJTRPJURQBRM-UHFFFAOYSA-N 0.000 description 1
- CJIJXIFQYOPWTF-UHFFFAOYSA-N 7-hydroxycoumarin Natural products O1C(=O)C=CC2=CC(O)=CC=C21 CJIJXIFQYOPWTF-UHFFFAOYSA-N 0.000 description 1
- 108010066676 Abrin Proteins 0.000 description 1
- 102000012440 Acetylcholinesterase Human genes 0.000 description 1
- 108010022752 Acetylcholinesterase Proteins 0.000 description 1
- 206010069754 Acquired gene mutation Diseases 0.000 description 1
- 241001164825 Adeno-associated virus - 8 Species 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 108010083359 Antigen Receptors Proteins 0.000 description 1
- 102000006306 Antigen Receptors Human genes 0.000 description 1
- 101100178203 Arabidopsis thaliana HMGB3 gene Proteins 0.000 description 1
- 241000203069 Archaea Species 0.000 description 1
- 102000015790 Asparaginase Human genes 0.000 description 1
- 108010024976 Asparaginase Proteins 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 101100017024 Aspergillus japonicus himD gene Proteins 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 108020003591 B-Form DNA Proteins 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 108010077805 Bacterial Proteins Proteins 0.000 description 1
- 235000018185 Betula X alpestris Nutrition 0.000 description 1
- 235000018212 Betula X uliginosa Nutrition 0.000 description 1
- 108010006654 Bleomycin Proteins 0.000 description 1
- 241000589969 Borreliella burgdorferi Species 0.000 description 1
- COVZYZSDYWQREU-UHFFFAOYSA-N Busulfan Chemical compound CS(=O)(=O)OCCCCOS(C)(=O)=O COVZYZSDYWQREU-UHFFFAOYSA-N 0.000 description 1
- 101100489922 Caenorhabditis elegans abf-2 gene Proteins 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 101710158575 Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase Proteins 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
- 108020004998 Chloroplast DNA Proteins 0.000 description 1
- 108020005133 Chloroplast RNA Proteins 0.000 description 1
- 206010008631 Cholera Diseases 0.000 description 1
- 208000006545 Chronic Obstructive Pulmonary Disease Diseases 0.000 description 1
- PTOAARAWEBMLNO-KVQBGUIXSA-N Cladribine Chemical compound C1=NC=2C(N)=NC(Cl)=NC=2N1[C@H]1C[C@H](O)[C@@H](CO)O1 PTOAARAWEBMLNO-KVQBGUIXSA-N 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 208000035473 Communicable disease Diseases 0.000 description 1
- 206010011224 Cough Diseases 0.000 description 1
- 241000938605 Crocodylia Species 0.000 description 1
- 239000004971 Cross linker Substances 0.000 description 1
- 108700032819 Croton tiglium crotin II Proteins 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
- 108090000695 Cytokines Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
- 230000033616 DNA repair Effects 0.000 description 1
- 230000004543 DNA replication Effects 0.000 description 1
- 101710096438 DNA-binding protein Proteins 0.000 description 1
- XPDXVDYUQZHFPV-UHFFFAOYSA-N Dansyl Chloride Chemical compound C1=CC=C2C(N(C)C)=CC=CC2=C1S(Cl)(=O)=O XPDXVDYUQZHFPV-UHFFFAOYSA-N 0.000 description 1
- WEAHRLBPCANXCN-UHFFFAOYSA-N Daunomycin Natural products CCC1(O)CC(OC2CC(N)C(O)C(C)O2)c3cc4C(=O)c5c(OC)cccc5C(=O)c4c(O)c3C1 WEAHRLBPCANXCN-UHFFFAOYSA-N 0.000 description 1
- 206010011968 Decreased immune responsiveness Diseases 0.000 description 1
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
- 241000702421 Dependoparvovirus Species 0.000 description 1
- 206010012735 Diarrhoea Diseases 0.000 description 1
- RWSOTUBLDIXVET-UHFFFAOYSA-N Dihydrogen sulfide Chemical compound S RWSOTUBLDIXVET-UHFFFAOYSA-N 0.000 description 1
- 108010053187 Diphtheria Toxin Proteins 0.000 description 1
- 102000016607 Diphtheria Toxin Human genes 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- MBYXEBXZARTUSS-QLWBXOBMSA-N Emetamine Natural products O(C)c1c(OC)cc2c(c(C[C@@H]3[C@H](CC)CN4[C@H](c5c(cc(OC)c(OC)c5)CC4)C3)ncc2)c1 MBYXEBXZARTUSS-QLWBXOBMSA-N 0.000 description 1
- 241000194032 Enterococcus faecalis Species 0.000 description 1
- 101710146739 Enterotoxin Proteins 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 241001446387 Escherichia coli UTI89 Species 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 206010053172 Fatal outcomes Diseases 0.000 description 1
- 102000009109 Fc receptors Human genes 0.000 description 1
- 108010087819 Fc receptors Proteins 0.000 description 1
- 108010008177 Fd immunoglobulins Proteins 0.000 description 1
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 1
- GHASVSINZRGABV-UHFFFAOYSA-N Fluorouracil Chemical compound FC1=CNC(=O)NC1=O GHASVSINZRGABV-UHFFFAOYSA-N 0.000 description 1
- 108091006027 G proteins Proteins 0.000 description 1
- 102000030782 GTP binding Human genes 0.000 description 1
- 108091000058 GTP-Binding Proteins 0.000 description 1
- 101710177291 Gag polyprotein Proteins 0.000 description 1
- GYHNNYVSQQEPJS-OIOBTWANSA-N Gallium-67 Chemical compound [67Ga] GYHNNYVSQQEPJS-OIOBTWANSA-N 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 108700004714 Gelonium multiflorum GEL Proteins 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 108010026389 Gramicidin Proteins 0.000 description 1
- 101150091750 HMG1 gene Proteins 0.000 description 1
- 102000000849 HMGB Proteins Human genes 0.000 description 1
- 108010001860 HMGB Proteins Proteins 0.000 description 1
- 108700010013 HMGB1 Proteins 0.000 description 1
- 101150021904 HMGB1 gene Proteins 0.000 description 1
- 241000590002 Helicobacter pylori Species 0.000 description 1
- 102000018802 High Mobility Group Proteins Human genes 0.000 description 1
- 108010052512 High Mobility Group Proteins Proteins 0.000 description 1
- 101710168537 High mobility group protein B1 Proteins 0.000 description 1
- 101000690301 Homo sapiens Aldo-keto reductase family 1 member C4 Proteins 0.000 description 1
- 101100178199 Homo sapiens HMGB2 gene Proteins 0.000 description 1
- 101100178206 Homo sapiens HMGB3 gene Proteins 0.000 description 1
- 101100178210 Homo sapiens HMGB4 gene Proteins 0.000 description 1
- 101000798109 Homo sapiens Melanotransferrin Proteins 0.000 description 1
- 101000967073 Homo sapiens Metal regulatory transcription factor 1 Proteins 0.000 description 1
- 101001030197 Homo sapiens Myelin transcription factor 1 Proteins 0.000 description 1
- 101001116548 Homo sapiens Protein CBFA2T1 Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 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
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 1
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 1
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 1
- 102000013463 Immunoglobulin Light Chains Human genes 0.000 description 1
- 108010065825 Immunoglobulin Light Chains Proteins 0.000 description 1
- 206010021531 Impetigo Diseases 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- XEEYBQQBJWHFJM-AKLPVKDBSA-N Iron-59 Chemical compound [59Fe] XEEYBQQBJWHFJM-AKLPVKDBSA-N 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-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
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 244000207740 Lemna minor Species 0.000 description 1
- 235000006439 Lemna minor Nutrition 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- NNJVILVZKWQKPM-UHFFFAOYSA-N Lidocaine Chemical compound CCN(CC)CC(=O)NC1=C(C)C=CC=C1C NNJVILVZKWQKPM-UHFFFAOYSA-N 0.000 description 1
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
- 208000004852 Lung Injury Diseases 0.000 description 1
- 208000016604 Lyme disease Diseases 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 101710125418 Major capsid protein Proteins 0.000 description 1
- 201000009906 Meningitis Diseases 0.000 description 1
- 102100040514 Metal regulatory transcription factor 1 Human genes 0.000 description 1
- VFKZTMPDYBFSTM-KVTDHHQDSA-N Mitobronitol Chemical compound BrC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CBr VFKZTMPDYBFSTM-KVTDHHQDSA-N 0.000 description 1
- 108020005196 Mitochondrial DNA Proteins 0.000 description 1
- ZOKXTWBITQBERF-AKLPVKDBSA-N Molybdenum Mo-99 Chemical compound [99Mo] ZOKXTWBITQBERF-AKLPVKDBSA-N 0.000 description 1
- 244000302512 Momordica charantia Species 0.000 description 1
- 235000009811 Momordica charantia Nutrition 0.000 description 1
- 241000714177 Murine leukemia virus Species 0.000 description 1
- 108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 1
- 241000588652 Neisseria gonorrhoeae Species 0.000 description 1
- 241000588650 Neisseria meningitidis Species 0.000 description 1
- 241000772415 Neovison vison Species 0.000 description 1
- 102000007999 Nuclear Proteins Human genes 0.000 description 1
- 108010089610 Nuclear Proteins Proteins 0.000 description 1
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 1
- 108091005461 Nucleic proteins Proteins 0.000 description 1
- 208000005141 Otitis Diseases 0.000 description 1
- 101710116435 Outer membrane protein Proteins 0.000 description 1
- 101710167675 Outer membrane protein P5 Proteins 0.000 description 1
- 240000007019 Oxalis corniculata Species 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 229930012538 Paclitaxel Natural products 0.000 description 1
- 241000282579 Pan Species 0.000 description 1
- 241000282520 Papio Species 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 208000006389 Peri-Implantitis Diseases 0.000 description 1
- 108010081690 Pertussis Toxin Proteins 0.000 description 1
- OAICVXFJPJFONN-OUBTZVSYSA-N Phosphorus-32 Chemical compound [32P] OAICVXFJPJFONN-OUBTZVSYSA-N 0.000 description 1
- OAICVXFJPJFONN-NJFSPNSNSA-N Phosphorus-33 Chemical compound [33P] OAICVXFJPJFONN-NJFSPNSNSA-N 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 240000007643 Phytolacca americana Species 0.000 description 1
- 235000009074 Phytolacca americana Nutrition 0.000 description 1
- 101100413173 Phytolacca americana PAP2 gene Proteins 0.000 description 1
- 241000605862 Porphyromonas gingivalis Species 0.000 description 1
- 235000001855 Portulaca oleracea Nutrition 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108010007568 Protamines Proteins 0.000 description 1
- 102000007327 Protamines Human genes 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
- 108010001267 Protein Subunits Proteins 0.000 description 1
- 102000002067 Protein Subunits Human genes 0.000 description 1
- 208000032536 Pseudomonas Infections Diseases 0.000 description 1
- 101000762949 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) Exotoxin A Proteins 0.000 description 1
- 102000017143 RNA Polymerase I Human genes 0.000 description 1
- 108010013845 RNA Polymerase I Proteins 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 108091030071 RNAI Proteins 0.000 description 1
- 101100409194 Rattus norvegicus Ppargc1b gene Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 108010073443 Ribi adjuvant Proteins 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- 238000011579 SCID mouse model Methods 0.000 description 1
- AUVVAXYIELKVAI-UHFFFAOYSA-N SJ000285215 Natural products N1CCC2=CC(OC)=C(OC)C=C2C1CC1CC2C3=CC(OC)=C(OC)C=C3CCN2CC1CC AUVVAXYIELKVAI-UHFFFAOYSA-N 0.000 description 1
- 102000017100 SOX Transcription Factors Human genes 0.000 description 1
- 108010013721 SOX Transcription Factors Proteins 0.000 description 1
- 101000997749 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Intrastrand cross-link recognition protein Proteins 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 241001138501 Salmonella enterica Species 0.000 description 1
- 108010084592 Saporins Proteins 0.000 description 1
- 102100038583 Secreted Ly-6/uPAR-related protein 1 Human genes 0.000 description 1
- BUGBHKTXTAQXES-AHCXROLUSA-N Selenium-75 Chemical compound [75Se] BUGBHKTXTAQXES-AHCXROLUSA-N 0.000 description 1
- 108010079723 Shiga Toxin Proteins 0.000 description 1
- 108010091769 Shiga Toxin 1 Proteins 0.000 description 1
- 108010090763 Shiga Toxin 2 Proteins 0.000 description 1
- 108010017898 Shiga Toxins Proteins 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 108010003723 Single-Domain Antibodies Proteins 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 108020004459 Small interfering RNA Proteins 0.000 description 1
- 244000061456 Solanum tuberosum Species 0.000 description 1
- 235000002595 Solanum tuberosum Nutrition 0.000 description 1
- 241000191963 Staphylococcus epidermidis Species 0.000 description 1
- PJANXHGTPQOBST-VAWYXSNFSA-N Stilbene Natural products C=1C=CC=CC=1/C=C/C1=CC=CC=C1 PJANXHGTPQOBST-VAWYXSNFSA-N 0.000 description 1
- 208000007107 Stomach Ulcer Diseases 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 241000193985 Streptococcus agalactiae Species 0.000 description 1
- 241000194019 Streptococcus mutans Species 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 230000006044 T cell activation Effects 0.000 description 1
- 208000000389 T-cell leukemia Diseases 0.000 description 1
- 208000028530 T-cell lymphoblastic leukemia/lymphoma Diseases 0.000 description 1
- 108010055044 Tetanus Toxin Proteins 0.000 description 1
- BHEOSNUKNHRBNM-UHFFFAOYSA-N Tetramethylsqualene Natural products CC(=C)C(C)CCC(=C)C(C)CCC(C)=CCCC=C(C)CCC(C)C(=C)CCC(C)C(C)=C BHEOSNUKNHRBNM-UHFFFAOYSA-N 0.000 description 1
- FOCVUCIESVLUNU-UHFFFAOYSA-N Thiotepa Chemical compound C1CN1P(N1CC1)(=S)N1CC1 FOCVUCIESVLUNU-UHFFFAOYSA-N 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 206010069363 Traumatic lung injury Diseases 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 101150017421 UBTF gene Proteins 0.000 description 1
- GBOGMAARMMDZGR-UHFFFAOYSA-N UNPD149280 Natural products N1C(=O)C23OC(=O)C=CC(O)CCCC(C)CC=CC3C(O)C(=C)C(C)C2C1CC1=CC=CC=C1 GBOGMAARMMDZGR-UHFFFAOYSA-N 0.000 description 1
- 102100038458 Ubinuclein-1 Human genes 0.000 description 1
- 101710094188 Ubinuclein-1 Proteins 0.000 description 1
- 206010046914 Vaginal infection Diseases 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 240000001866 Vernicia fordii Species 0.000 description 1
- 241000607626 Vibrio cholerae Species 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
- 206010048038 Wound infection Diseases 0.000 description 1
- VWQVUPCCIRVNHF-OUBTZVSYSA-N Yttrium-90 Chemical compound [90Y] VWQVUPCCIRVNHF-OUBTZVSYSA-N 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
- 206010000269 abscess Diseases 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- DPXJVFZANSGRMM-UHFFFAOYSA-N acetic acid;2,3,4,5,6-pentahydroxyhexanal;sodium Chemical compound [Na].CC(O)=O.OCC(O)C(O)C(O)C(O)C=O DPXJVFZANSGRMM-UHFFFAOYSA-N 0.000 description 1
- 229940022698 acetylcholinesterase Drugs 0.000 description 1
- 229940125666 actinium-225 Drugs 0.000 description 1
- QQINRWTZWGJFDB-YPZZEJLDSA-N actinium-225 Chemical compound [225Ac] QQINRWTZWGJFDB-YPZZEJLDSA-N 0.000 description 1
- 229930183665 actinomycin Natural products 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 210000005006 adaptive immune system Anatomy 0.000 description 1
- 230000001464 adherent effect Effects 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 208000037883 airway inflammation Diseases 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 229940100198 alkylating agent Drugs 0.000 description 1
- 239000002168 alkylating agent Substances 0.000 description 1
- 230000029936 alkylation Effects 0.000 description 1
- 108010001818 alpha-sarcin Proteins 0.000 description 1
- PNEYBMLMFCGWSK-UHFFFAOYSA-N aluminium oxide Inorganic materials [O-2].[O-2].[O-2].[Al+3].[Al+3] PNEYBMLMFCGWSK-UHFFFAOYSA-N 0.000 description 1
- CEGOLXSVJUTHNZ-UHFFFAOYSA-K aluminium tristearate Chemical compound [Al+3].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O CEGOLXSVJUTHNZ-UHFFFAOYSA-K 0.000 description 1
- 229940063655 aluminum stearate Drugs 0.000 description 1
- 230000009435 amidation Effects 0.000 description 1
- 238000007112 amidation reaction Methods 0.000 description 1
- 238000010640 amide synthesis reaction Methods 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 229960003022 amoxicillin Drugs 0.000 description 1
- LSQZJLSUYDQPKJ-NJBDSQKTSA-N amoxicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=C(O)C=C1 LSQZJLSUYDQPKJ-NJBDSQKTSA-N 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000000340 anti-metabolite Effects 0.000 description 1
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 1
- 229940100197 antimetabolite Drugs 0.000 description 1
- 239000002256 antimetabolite Substances 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 239000003125 aqueous solvent Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- RQNWIZPPADIBDY-NJFSPNSNSA-N arsenic-77 Chemical compound [77As] RQNWIZPPADIBDY-NJFSPNSNSA-N 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
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- RYXHOMYVWAEKHL-OUBTZVSYSA-N astatine-211 Chemical compound [211At] RYXHOMYVWAEKHL-OUBTZVSYSA-N 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000004900 autophagic degradation Effects 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
- 229960004099 azithromycin Drugs 0.000 description 1
- MQTOSJVFKKJCRP-BICOPXKESA-N azithromycin Chemical compound O([C@@H]1[C@@H](C)C(=O)O[C@@H]([C@@]([C@H](O)[C@@H](C)N(C)C[C@H](C)C[C@@](C)(O)[C@H](O[C@H]2[C@@H]([C@H](C[C@@H](C)O2)N(C)C)O)[C@H]1C)(C)O)CC)[C@H]1C[C@@](C)(OC)[C@@H](O)[C@H](C)O1 MQTOSJVFKKJCRP-BICOPXKESA-N 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 201000005008 bacterial sepsis Diseases 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 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 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 230000004993 binary fission Effects 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 230000029918 bioluminescence Effects 0.000 description 1
- 238000005415 bioluminescence Methods 0.000 description 1
- JCXGWMGPZLAOME-AKLPVKDBSA-N bismuth-212 Chemical compound [212Bi] JCXGWMGPZLAOME-AKLPVKDBSA-N 0.000 description 1
- JCXGWMGPZLAOME-RNFDNDRNSA-N bismuth-213 Chemical compound [213Bi] JCXGWMGPZLAOME-RNFDNDRNSA-N 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
- 230000000903 blocking effect Effects 0.000 description 1
- RSIHSRDYCUFFLA-DYKIIFRCSA-N boldenone Chemical compound O=C1C=C[C@]2(C)[C@H]3CC[C@](C)([C@H](CC4)O)[C@@H]4[C@@H]3CCC2=C1 RSIHSRDYCUFFLA-DYKIIFRCSA-N 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 235000012206 bottled water Nutrition 0.000 description 1
- 206010006451 bronchitis Diseases 0.000 description 1
- 229960002092 busulfan Drugs 0.000 description 1
- 150000001718 carbodiimides Chemical class 0.000 description 1
- 125000000837 carbohydrate group Chemical group 0.000 description 1
- 229960004562 carboplatin Drugs 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 229960005243 carmustine Drugs 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- RTXOFQZKPXMALH-GHXIOONMSA-N cefdinir Chemical compound S1C(N)=NC(C(=N\O)\C(=O)N[C@@H]2C(N3C(=C(C=C)CS[C@@H]32)C(O)=O)=O)=C1 RTXOFQZKPXMALH-GHXIOONMSA-N 0.000 description 1
- 229960003719 cefdinir Drugs 0.000 description 1
- 239000002458 cell surface marker Substances 0.000 description 1
- 230000005889 cellular cytotoxicity Effects 0.000 description 1
- 230000010094 cellular senescence Effects 0.000 description 1
- 210000003850 cellular structure Anatomy 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- NDAYQJDHGXTBJL-MWWSRJDJSA-N chembl557217 Chemical compound C1=CC=C2C(C[C@H](NC(=O)[C@@H](CC(C)C)NC(=O)[C@H](CC=3C4=CC=CC=C4NC=3)NC(=O)[C@@H](CC(C)C)NC(=O)[C@H](CC=3C4=CC=CC=C4NC=3)NC(=O)[C@@H](CC(C)C)NC(=O)[C@H](CC=3C4=CC=CC=C4NC=3)NC(=O)[C@@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](C(C)C)NC(=O)[C@H](C)NC(=O)[C@H](NC(=O)CNC(=O)[C@@H](NC=O)C(C)C)CC(C)C)C(=O)NCCO)=CNC2=C1 NDAYQJDHGXTBJL-MWWSRJDJSA-N 0.000 description 1
- 238000012412 chemical coupling Methods 0.000 description 1
- 230000035605 chemotaxis Effects 0.000 description 1
- 235000013330 chicken meat Nutrition 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
- 201000001883 cholelithiasis Diseases 0.000 description 1
- 108091006090 chromatin-associated proteins Proteins 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 208000013116 chronic cough 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
- 239000007979 citrate buffer Substances 0.000 description 1
- 229960002436 cladribine Drugs 0.000 description 1
- 229960001338 colchicine Drugs 0.000 description 1
- 239000008119 colloidal silica Substances 0.000 description 1
- 230000001010 compromised effect Effects 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 239000000599 controlled substance Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- RYGMFSIKBFXOCR-YPZZEJLDSA-N copper-62 Chemical compound [62Cu] RYGMFSIKBFXOCR-YPZZEJLDSA-N 0.000 description 1
- RYGMFSIKBFXOCR-IGMARMGPSA-N copper-64 Chemical compound [64Cu] RYGMFSIKBFXOCR-IGMARMGPSA-N 0.000 description 1
- RYGMFSIKBFXOCR-AKLPVKDBSA-N copper-67 Chemical compound [67Cu] RYGMFSIKBFXOCR-AKLPVKDBSA-N 0.000 description 1
- 239000007822 coupling agent Substances 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 229960004397 cyclophosphamide Drugs 0.000 description 1
- 150000001944 cysteine derivatives Chemical class 0.000 description 1
- 229960000684 cytarabine Drugs 0.000 description 1
- GBOGMAARMMDZGR-TYHYBEHESA-N cytochalasin B Chemical compound C([C@H]1[C@@H]2[C@@H](C([C@@H](O)[C@@H]3/C=C/C[C@H](C)CCC[C@@H](O)/C=C/C(=O)O[C@@]23C(=O)N1)=C)C)C1=CC=CC=C1 GBOGMAARMMDZGR-TYHYBEHESA-N 0.000 description 1
- GBOGMAARMMDZGR-JREHFAHYSA-N cytochalasin B Natural products C[C@H]1CCC[C@@H](O)C=CC(=O)O[C@@]23[C@H](C=CC1)[C@H](O)C(=C)[C@@H](C)[C@@H]2[C@H](Cc4ccccc4)NC3=O GBOGMAARMMDZGR-JREHFAHYSA-N 0.000 description 1
- 238000004163 cytometry Methods 0.000 description 1
- 210000004292 cytoskeleton Anatomy 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 229960003901 dacarbazine Drugs 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- RSIHSRDYCUFFLA-UHFFFAOYSA-N dehydrotestosterone Natural products O=C1C=CC2(C)C3CCC(C)(C(CC4)O)C4C3CCC2=C1 RSIHSRDYCUFFLA-UHFFFAOYSA-N 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 229910021641 deionized water Inorganic materials 0.000 description 1
- 210000004443 dendritic cell Anatomy 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000012631 diagnostic technique Methods 0.000 description 1
- 229930191339 dianthin Natural products 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- GXGAKHNRMVGRPK-UHFFFAOYSA-N dimagnesium;dioxido-bis[[oxido(oxo)silyl]oxy]silane Chemical compound [Mg+2].[Mg+2].[O-][Si](=O)O[Si]([O-])([O-])O[Si]([O-])=O GXGAKHNRMVGRPK-UHFFFAOYSA-N 0.000 description 1
- 206010013023 diphtheria Diseases 0.000 description 1
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 1
- 229910000396 dipotassium phosphate Inorganic materials 0.000 description 1
- 235000019797 dipotassium phosphate Nutrition 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- PRAKJMSDJKAYCZ-UHFFFAOYSA-N dodecahydrosqualene Natural products CC(C)CCCC(C)CCCC(C)CCCCC(C)CCCC(C)CCCC(C)C PRAKJMSDJKAYCZ-UHFFFAOYSA-N 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 239000003651 drinking water Substances 0.000 description 1
- KBQHZAAAGSGFKK-AKLPVKDBSA-N dysprosium-166 Chemical compound [166Dy] KBQHZAAAGSGFKK-AKLPVKDBSA-N 0.000 description 1
- 208000019258 ear infection Diseases 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- AUVVAXYIELKVAI-CKBKHPSWSA-N emetine Chemical compound N1CCC2=CC(OC)=C(OC)C=C2[C@H]1C[C@H]1C[C@H]2C3=CC(OC)=C(OC)C=C3CCN2C[C@@H]1CC AUVVAXYIELKVAI-CKBKHPSWSA-N 0.000 description 1
- 229960002694 emetine Drugs 0.000 description 1
- AUVVAXYIELKVAI-UWBTVBNJSA-N emetine Natural products N1CCC2=CC(OC)=C(OC)C=C2[C@H]1C[C@H]1C[C@H]2C3=CC(OC)=C(OC)C=C3CCN2C[C@H]1CC AUVVAXYIELKVAI-UWBTVBNJSA-N 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 206010014665 endocarditis Diseases 0.000 description 1
- 108010028531 enomycin Proteins 0.000 description 1
- 229940032049 enterococcus faecalis Drugs 0.000 description 1
- 239000000147 enterotoxin Substances 0.000 description 1
- 231100000655 enterotoxin Toxicity 0.000 description 1
- YQGOJNYOYNNSMM-UHFFFAOYSA-N eosin Chemical compound [Na+].OC(=O)C1=CC=CC=C1C1=C2C=C(Br)C(=O)C(Br)=C2OC2=C(Br)C(O)=C(Br)C=C21 YQGOJNYOYNNSMM-UHFFFAOYSA-N 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- UYAHIZSMUZPPFV-NJFSPNSNSA-N erbium-169 Chemical compound [169Er] UYAHIZSMUZPPFV-NJFSPNSNSA-N 0.000 description 1
- IINNWAYUJNWZRM-UHFFFAOYSA-L erythrosin B Chemical compound [Na+].[Na+].[O-]C(=O)C1=CC=CC=C1C1=C2C=C(I)C(=O)C(I)=C2OC2=C(I)C([O-])=C(I)C=C21 IINNWAYUJNWZRM-UHFFFAOYSA-L 0.000 description 1
- 229940011411 erythrosine Drugs 0.000 description 1
- 235000012732 erythrosine Nutrition 0.000 description 1
- 239000004174 erythrosine Substances 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- BEFDCLMNVWHSGT-UHFFFAOYSA-N ethenylcyclopentane Chemical compound C=CC1CCCC1 BEFDCLMNVWHSGT-UHFFFAOYSA-N 0.000 description 1
- 150000002170 ethers Chemical class 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 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
- 229960005420 etoposide Drugs 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000005713 exacerbation Effects 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 210000001723 extracellular space Anatomy 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 210000000416 exudates and transudate Anatomy 0.000 description 1
- 210000003754 fetus Anatomy 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 239000004931 filters and membranes Substances 0.000 description 1
- 238000000684 flow cytometry Methods 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
- GVEPBJHOBDJJJI-UHFFFAOYSA-N fluoranthrene Natural products C1=CC(C2=CC=CC=C22)=C3C2=CC=CC3=C1 GVEPBJHOBDJJJI-UHFFFAOYSA-N 0.000 description 1
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
- 238000000799 fluorescence microscopy Methods 0.000 description 1
- 229960002949 fluorouracil Drugs 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 125000002485 formyl group Chemical group [H]C(*)=O 0.000 description 1
- 125000002446 fucosyl group Chemical group C1([C@@H](O)[C@H](O)[C@H](O)[C@@H](O1)C)* 0.000 description 1
- 230000005021 gait Effects 0.000 description 1
- 229940006110 gallium-67 Drugs 0.000 description 1
- 208000001130 gallstones Diseases 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 229960005277 gemcitabine Drugs 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
- 230000009368 gene silencing by RNA Effects 0.000 description 1
- GJMUCSXZXBCQRZ-UHFFFAOYSA-N geraniin Natural products Oc1cc(cc(O)c1O)C(=O)OC2OC3COC(=O)c4cc(O)c(O)c(O)c4c5cc(C(=O)C67OC3C(O6)C2OC(=O)c8cc(O)c(O)c9OC%10(O)C(C(=CC(=O)C%10(O)O)C7=O)c89)c(O)c(O)c5O GJMUCSXZXBCQRZ-UHFFFAOYSA-N 0.000 description 1
- 229930194078 geranin Natural products 0.000 description 1
- 208000007565 gingivitis Diseases 0.000 description 1
- 239000003862 glucocorticoid Substances 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 125000005456 glyceride group Chemical group 0.000 description 1
- 229960002449 glycine Drugs 0.000 description 1
- 125000003827 glycol group Chemical group 0.000 description 1
- 239000010931 gold Substances 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- PCHJSUWPFVWCPO-OUBTZVSYSA-N gold-198 Chemical compound [198Au] PCHJSUWPFVWCPO-OUBTZVSYSA-N 0.000 description 1
- 125000005179 haloacetyl group Chemical group 0.000 description 1
- 210000003709 heart valve Anatomy 0.000 description 1
- 229940037467 helicobacter pylori Drugs 0.000 description 1
- 238000013537 high throughput screening Methods 0.000 description 1
- 101150019159 himA gene Proteins 0.000 description 1
- 238000011540 hip replacement Methods 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 102000054751 human RUNX1T1 Human genes 0.000 description 1
- 229910000037 hydrogen sulfide Inorganic materials 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 229960000908 idarubicin Drugs 0.000 description 1
- 101150117117 ihfB gene Proteins 0.000 description 1
- 210000001822 immobilized cell Anatomy 0.000 description 1
- 230000002519 immonomodulatory effect Effects 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 229940127121 immunoconjugate Drugs 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 239000002596 immunotoxin Substances 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 238000005462 in vivo assay Methods 0.000 description 1
- 229940055742 indium-111 Drugs 0.000 description 1
- APFVFJFRJDLVQX-AHCXROLUSA-N indium-111 Chemical compound [111In] APFVFJFRJDLVQX-AHCXROLUSA-N 0.000 description 1
- 208000022760 infectious otitis media Diseases 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 230000015788 innate immune response Effects 0.000 description 1
- 210000005007 innate immune system Anatomy 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000007913 intrathecal administration Methods 0.000 description 1
- XMBWDFGMSWQBCA-YPZZEJLDSA-N iodane Chemical compound [125IH] XMBWDFGMSWQBCA-YPZZEJLDSA-N 0.000 description 1
- 229940044173 iodine-125 Drugs 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- GKOZUEZYRPOHIO-NJFSPNSNSA-N iridium-194 Chemical compound [194Ir] GKOZUEZYRPOHIO-NJFSPNSNSA-N 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- ZBKFYXZXZJPWNQ-UHFFFAOYSA-N isothiocyanate group Chemical group [N-]=C=S ZBKFYXZXZJPWNQ-UHFFFAOYSA-N 0.000 description 1
- 238000013150 knee replacement Methods 0.000 description 1
- 150000002605 large molecules Chemical class 0.000 description 1
- WABPQHHGFIMREM-RNFDNDRNSA-N lead-211 Chemical compound [211Pb] WABPQHHGFIMREM-RNFDNDRNSA-N 0.000 description 1
- WABPQHHGFIMREM-BKFZFHPZSA-N lead-212 Chemical compound [212Pb] WABPQHHGFIMREM-BKFZFHPZSA-N 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 231100000518 lethal Toxicity 0.000 description 1
- 230000001665 lethal effect Effects 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 229960004194 lidocaine Drugs 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 229960002247 lomustine Drugs 0.000 description 1
- DLBFLQKQABVKGT-UHFFFAOYSA-L lucifer yellow dye Chemical compound [Li+].[Li+].[O-]S(=O)(=O)C1=CC(C(N(C(=O)NN)C2=O)=O)=C3C2=CC(S([O-])(=O)=O)=CC3=C1N DLBFLQKQABVKGT-UHFFFAOYSA-L 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 231100000515 lung injury Toxicity 0.000 description 1
- OHSVLFRHMCKCQY-AHCXROLUSA-N lutetium-171 Chemical compound [171Lu] OHSVLFRHMCKCQY-AHCXROLUSA-N 0.000 description 1
- 210000002751 lymph Anatomy 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 239000000391 magnesium silicate Substances 0.000 description 1
- 229940099273 magnesium trisilicate Drugs 0.000 description 1
- 229910000386 magnesium trisilicate Inorganic materials 0.000 description 1
- 235000019793 magnesium trisilicate Nutrition 0.000 description 1
- 229940107698 malachite green Drugs 0.000 description 1
- FDZZZRQASAIRJF-UHFFFAOYSA-M malachite green Chemical compound [Cl-].C1=CC(N(C)C)=CC=C1C(C=1C=CC=CC=1)=C1C=CC(=[N+](C)C)C=C1 FDZZZRQASAIRJF-UHFFFAOYSA-M 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 230000013011 mating Effects 0.000 description 1
- 229960004961 mechlorethamine Drugs 0.000 description 1
- HAWPXGHAZFHHAD-UHFFFAOYSA-N mechlorethamine Chemical compound ClCCN(C)CCCl HAWPXGHAZFHHAD-UHFFFAOYSA-N 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 229960001924 melphalan Drugs 0.000 description 1
- SGDBTWWWUNNDEQ-LBPRGKRZSA-N melphalan Chemical compound OC(=O)[C@@H](N)CC1=CC=C(N(CCCl)CCCl)C=C1 SGDBTWWWUNNDEQ-LBPRGKRZSA-N 0.000 description 1
- 210000005060 membrane bound organelle Anatomy 0.000 description 1
- 229960001428 mercaptopurine Drugs 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 229960000485 methotrexate Drugs 0.000 description 1
- 244000005706 microflora Species 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 229960005485 mitobronitol Drugs 0.000 description 1
- 210000003470 mitochondria Anatomy 0.000 description 1
- 108091064355 mitochondrial RNA Proteins 0.000 description 1
- 230000002438 mitochondrial effect Effects 0.000 description 1
- 229950009740 molybdenum mo-99 Drugs 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 210000000214 mouth Anatomy 0.000 description 1
- 210000004877 mucosa Anatomy 0.000 description 1
- ZTLGJPIZUOVDMT-UHFFFAOYSA-N n,n-dichlorotriazin-4-amine Chemical compound ClN(Cl)C1=CC=NN=N1 ZTLGJPIZUOVDMT-UHFFFAOYSA-N 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 231100000956 nontoxicity Toxicity 0.000 description 1
- 239000002853 nucleic acid probe Substances 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 238000002515 oligonucleotide synthesis Methods 0.000 description 1
- 239000007935 oral tablet Substances 0.000 description 1
- 230000005305 organ development Effects 0.000 description 1
- LSQZJLSUYDQPKJ-UHFFFAOYSA-N p-Hydroxyampicillin Natural products O=C1N2C(C(O)=O)C(C)(C)SC2C1NC(=O)C(N)C1=CC=C(O)C=C1 LSQZJLSUYDQPKJ-UHFFFAOYSA-N 0.000 description 1
- 229960001592 paclitaxel Drugs 0.000 description 1
- 210000002741 palatine tonsil Anatomy 0.000 description 1
- KDLHZDBZIXYQEI-AKLPVKDBSA-N palladium-109 Chemical compound [109Pd] KDLHZDBZIXYQEI-AKLPVKDBSA-N 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 230000037361 pathway Effects 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
- WCVRQHFDJLLWFE-UHFFFAOYSA-N pentane-1,2-diol Chemical compound CCCC(O)CO WCVRQHFDJLLWFE-UHFFFAOYSA-N 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 208000028169 periodontal disease Diseases 0.000 description 1
- 230000003239 periodontal effect Effects 0.000 description 1
- 239000003330 peritoneal dialysis fluid Substances 0.000 description 1
- 230000002688 persistence Effects 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 108010076042 phenomycin Proteins 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 235000021317 phosphate Nutrition 0.000 description 1
- 229940080469 phosphocellulose Drugs 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 229940097886 phosphorus 32 Drugs 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 230000036470 plasma concentration Effects 0.000 description 1
- 150000003057 platinum Chemical class 0.000 description 1
- BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Substances [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 description 1
- 108010089520 pol Gene Products Proteins 0.000 description 1
- 230000010287 polarization Effects 0.000 description 1
- 229920000058 polyacrylate Polymers 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 239000004800 polyvinyl chloride Substances 0.000 description 1
- 229920000915 polyvinyl chloride Polymers 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- 238000002600 positron emission tomography Methods 0.000 description 1
- 235000010241 potassium sorbate Nutrition 0.000 description 1
- 239000004302 potassium sorbate Substances 0.000 description 1
- 229940069338 potassium sorbate Drugs 0.000 description 1
- PUDIUYLPXJFUGB-OUBTZVSYSA-N praseodymium-142 Chemical compound [142Pr] PUDIUYLPXJFUGB-OUBTZVSYSA-N 0.000 description 1
- PUDIUYLPXJFUGB-NJFSPNSNSA-N praseodymium-143 Chemical compound [143Pr] PUDIUYLPXJFUGB-NJFSPNSNSA-N 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 230000007112 pro inflammatory response Effects 0.000 description 1
- 230000001023 pro-angiogenic effect Effects 0.000 description 1
- 229960004919 procaine Drugs 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
- 229960000624 procarbazine 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
- VQMWBBYLQSCNPO-RNFDNDRNSA-N promethium-149 Chemical compound [149Pm] VQMWBBYLQSCNPO-RNFDNDRNSA-N 0.000 description 1
- 229960003712 propranolol Drugs 0.000 description 1
- 229950008679 protamine sulfate Drugs 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 230000006916 protein interaction Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000004850 protein–protein interaction Effects 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 229950010131 puromycin Drugs 0.000 description 1
- 229960003581 pyridoxal Drugs 0.000 description 1
- 235000008164 pyridoxal Nutrition 0.000 description 1
- 239000011674 pyridoxal Substances 0.000 description 1
- 229960005562 radium-223 Drugs 0.000 description 1
- HCWPIIXVSYCSAN-OIOBTWANSA-N radium-223 Chemical compound [223Ra] HCWPIIXVSYCSAN-OIOBTWANSA-N 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 230000007115 recruitment Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000008439 repair process Effects 0.000 description 1
- 210000005000 reproductive tract Anatomy 0.000 description 1
- 230000008261 resistance mechanism Effects 0.000 description 1
- 230000004043 responsiveness Effects 0.000 description 1
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 1
- WUAPFZMCVAUBPE-IGMARMGPSA-N rhenium-186 Chemical compound [186Re] WUAPFZMCVAUBPE-IGMARMGPSA-N 0.000 description 1
- WUAPFZMCVAUBPE-AKLPVKDBSA-N rhenium-189 Chemical compound [189Re] WUAPFZMCVAUBPE-AKLPVKDBSA-N 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 108020004418 ribosomal RNA Proteins 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 238000002702 ribosome display Methods 0.000 description 1
- 235000002020 sage Nutrition 0.000 description 1
- KZUNJOHGWZRPMI-AKLPVKDBSA-N samarium-153 Chemical compound [153Sm] KZUNJOHGWZRPMI-AKLPVKDBSA-N 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- SIXSYDAISGFNSX-NJFSPNSNSA-N scandium-47 Chemical compound [47Sc] SIXSYDAISGFNSX-NJFSPNSNSA-N 0.000 description 1
- 238000007423 screening assay Methods 0.000 description 1
- 230000014639 sexual reproduction Effects 0.000 description 1
- BQCADISMDOOEFD-AKLPVKDBSA-N silver-111 Chemical compound [111Ag] BQCADISMDOOEFD-AKLPVKDBSA-N 0.000 description 1
- 201000009890 sinusitis Diseases 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 235000019812 sodium carboxymethyl cellulose Nutrition 0.000 description 1
- 229920001027 sodium carboxymethylcellulose Polymers 0.000 description 1
- 230000000392 somatic effect Effects 0.000 description 1
- 230000037439 somatic mutation Effects 0.000 description 1
- 235000010199 sorbic acid Nutrition 0.000 description 1
- 229940075582 sorbic acid Drugs 0.000 description 1
- 239000004334 sorbic acid Substances 0.000 description 1
- 238000004611 spectroscopical analysis Methods 0.000 description 1
- 229940031439 squalene Drugs 0.000 description 1
- TUHBEKDERLKLEC-UHFFFAOYSA-N squalene Natural products CC(=CCCC(=CCCC(=CCCC=C(/C)CCC=C(/C)CC=C(C)C)C)C)C TUHBEKDERLKLEC-UHFFFAOYSA-N 0.000 description 1
- 229910001220 stainless steel Inorganic materials 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000008174 sterile solution Substances 0.000 description 1
- PJANXHGTPQOBST-UHFFFAOYSA-N stilbene Chemical compound C=1C=CC=CC=1C=CC1=CC=CC=C1 PJANXHGTPQOBST-UHFFFAOYSA-N 0.000 description 1
- 235000021286 stilbenes Nutrition 0.000 description 1
- 230000004936 stimulating effect Effects 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
- CIOAGBVUUVVLOB-OUBTZVSYSA-N strontium-89 Chemical compound [89Sr] CIOAGBVUUVVLOB-OUBTZVSYSA-N 0.000 description 1
- 229940006509 strontium-89 Drugs 0.000 description 1
- 150000003461 sulfonyl halides Chemical class 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000008093 supporting effect Effects 0.000 description 1
- 239000000829 suppository Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 230000009182 swimming Effects 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 238000012385 systemic delivery Methods 0.000 description 1
- 229940037128 systemic glucocorticoids Drugs 0.000 description 1
- 239000003826 tablet Substances 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 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 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
- 229960001278 teniposide Drugs 0.000 description 1
- GZCRRIHWUXGPOV-NJFSPNSNSA-N terbium-161 Chemical compound [161Tb] GZCRRIHWUXGPOV-NJFSPNSNSA-N 0.000 description 1
- 229940118376 tetanus toxin Drugs 0.000 description 1
- 229960002372 tetracaine Drugs 0.000 description 1
- GKCBAIGFKIBETG-UHFFFAOYSA-N tetracaine Chemical compound CCCCNC1=CC=C(C(=O)OCCN(C)C)C=C1 GKCBAIGFKIBETG-UHFFFAOYSA-N 0.000 description 1
- WGTODYJZXSJIAG-UHFFFAOYSA-N tetramethylrhodamine chloride Chemical compound [Cl-].C=12C=CC(N(C)C)=CC2=[O+]C2=CC(N(C)C)=CC=C2C=1C1=CC=CC=C1C(O)=O WGTODYJZXSJIAG-UHFFFAOYSA-N 0.000 description 1
- MPLHNVLQVRSVEE-UHFFFAOYSA-N texas red Chemical compound [O-]S(=O)(=O)C1=CC(S(Cl)(=O)=O)=CC=C1C(C1=CC=2CCCN3CCCC(C=23)=C1O1)=C2C1=C(CCC1)C3=[N+]1CCCC3=C2 MPLHNVLQVRSVEE-UHFFFAOYSA-N 0.000 description 1
- 229960000278 theophylline Drugs 0.000 description 1
- 231100001274 therapeutic index Toxicity 0.000 description 1
- 230000004797 therapeutic response Effects 0.000 description 1
- 229960001196 thiotepa Drugs 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 229960003087 tioguanine Drugs 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 239000011573 trace mineral Substances 0.000 description 1
- 235000013619 trace mineral Nutrition 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000011269 treatment regimen Methods 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- ORHBXUUXSCNDEV-UHFFFAOYSA-N umbelliferone Chemical compound C1=CC(=O)OC2=CC(O)=CC=C21 ORHBXUUXSCNDEV-UHFFFAOYSA-N 0.000 description 1
- HFTAFOQKODTIJY-UHFFFAOYSA-N umbelliferone Natural products Cc1cc2C=CC(=O)Oc2cc1OCC=CC(C)(C)O HFTAFOQKODTIJY-UHFFFAOYSA-N 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 238000011870 unpaired t-test Methods 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 235000015112 vegetable and seed oil Nutrition 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 229940118696 vibrio cholerae Drugs 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
- 238000012800 visualization Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 229920003169 water-soluble polymer Polymers 0.000 description 1
- 239000001993 wax Substances 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 210000002268 wool Anatomy 0.000 description 1
- 150000003751 zinc Chemical class 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N37/00—Biocides, pest repellants or attractants, or plant growth regulators containing organic compounds containing a carbon atom having three bonds to hetero atoms with at the most two bonds to halogen, e.g. carboxylic acids
- A01N37/44—Biocides, pest repellants or attractants, or plant growth regulators containing organic compounds containing a carbon atom having three bonds to hetero atoms with at the most two bonds to halogen, e.g. carboxylic acids containing at least one carboxylic group or a thio analogue, or a derivative thereof, and a nitrogen atom attached to the same carbon skeleton by a single or double bond, this nitrogen atom not being a member of a derivative or of a thio analogue of a carboxylic group, e.g. amino-carboxylic acids
- A01N37/46—N-acyl derivatives
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N63/00—Biocides, pest repellants or attractants, or plant growth regulators containing microorganisms, viruses, microbial fungi, animals or substances produced by, or obtained from, microorganisms, viruses, microbial fungi or animals, e.g. enzymes or fermentates
- A01N63/50—Isolated enzymes; Isolated proteins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/19—Cytokines; Lymphokines; Interferons
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
- A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Gastroenterology & Hepatology (AREA)
- Epidemiology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Toxicology (AREA)
- Environmental Sciences (AREA)
- Agronomy & Crop Science (AREA)
- Biophysics (AREA)
- Pest Control & Pesticides (AREA)
- Plant Pathology (AREA)
- Dentistry (AREA)
- Oncology (AREA)
- Virology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Communicable Diseases (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Immunology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Agricultural Chemicals And Associated Chemicals (AREA)
Priority Applications (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2022194227A JP2023014389A (ja) | 2017-03-15 | 2022-12-05 | 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 |
| JP2025018512A JP2025065351A (ja) | 2017-03-15 | 2025-02-06 | 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 |
| JP2025119036A JP2025148518A (ja) | 2017-03-15 | 2025-07-15 | 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 |
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201762471834P | 2017-03-15 | 2017-03-15 | |
| US62/471,834 | 2017-03-15 | ||
| PCT/US2018/022508 WO2018170178A1 (en) | 2017-03-15 | 2018-03-14 | Composition and methods for disruption of bacterial biofilms without accompanying inflammation |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2022194227A Division JP2023014389A (ja) | 2017-03-15 | 2022-12-05 | 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2020513808A JP2020513808A (ja) | 2020-05-21 |
| JP2020513808A5 JP2020513808A5 (https=) | 2021-04-22 |
| JP7596069B2 true JP7596069B2 (ja) | 2024-12-09 |
Family
ID=62025942
Family Applications (4)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2019550715A Active JP7596069B2 (ja) | 2017-03-15 | 2018-03-14 | 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 |
| JP2022194227A Pending JP2023014389A (ja) | 2017-03-15 | 2022-12-05 | 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 |
| JP2025018512A Pending JP2025065351A (ja) | 2017-03-15 | 2025-02-06 | 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 |
| JP2025119036A Pending JP2025148518A (ja) | 2017-03-15 | 2025-07-15 | 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 |
Family Applications After (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2022194227A Pending JP2023014389A (ja) | 2017-03-15 | 2022-12-05 | 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 |
| JP2025018512A Pending JP2025065351A (ja) | 2017-03-15 | 2025-02-06 | 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 |
| JP2025119036A Pending JP2025148518A (ja) | 2017-03-15 | 2025-07-15 | 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US11746136B2 (https=) |
| EP (1) | EP3595445B1 (https=) |
| JP (4) | JP7596069B2 (https=) |
| AU (1) | AU2018236271B2 (https=) |
| CA (1) | CA3056088A1 (https=) |
| WO (1) | WO2018170178A1 (https=) |
Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US11274144B2 (en) | 2013-06-13 | 2022-03-15 | Research Institute At Nationwide Children's Hospital | Compositions and methods for the removal of biofilms |
| WO2017023863A1 (en) | 2015-07-31 | 2017-02-09 | Research Institute At Nationwide Children's Hospital | Peptides and antibodies for the removal of biofilms |
| JP7661008B2 (ja) | 2017-01-04 | 2025-04-14 | リサーチ インスティチュート アット ネイションワイド チルドレンズ ホスピタル | バイオフィルム関連障害の処置のための抗体断片 |
| US11564982B2 (en) | 2017-01-04 | 2023-01-31 | Research Institute At Nationwide Children's Hospital | DNABII vaccines and antibodies with enhanced activity |
| WO2018170178A1 (en) * | 2017-03-15 | 2018-09-20 | Research Institute At Nationwide Children's Hospital | Composition and methods for disruption of bacterial biofilms without accompanying inflammation |
| AU2019354829B2 (en) * | 2018-10-05 | 2025-04-17 | Research Institute At Nationwide Children's Hospital | Hmgb1 protein derivatives for the removal of biofilms |
| CA3183196A1 (en) * | 2020-07-07 | 2022-01-13 | Steven D. Goodman | Combination therapies for the treatment and prevention of biofilms |
| EP4615483A2 (en) * | 2022-11-11 | 2025-09-17 | Research Institute at Nationwide Children's Hospital | Compositions and methods for treating biofilms and neutrophil extracellular trap formation |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2013542185A (ja) | 2010-09-09 | 2013-11-21 | ユニバーシティー オブ サザン カリフォルニア | バイオフィルムを除去するための組成物および方法 |
| WO2014016417A1 (en) | 2012-07-26 | 2014-01-30 | Ospedale San Raffaele Srl | Hmgb1 variants and uses thereof |
Family Cites Families (78)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| DE3572982D1 (en) | 1984-03-06 | 1989-10-19 | Takeda Chemical Industries Ltd | Chemically modified lymphokine and production thereof |
| US4683195A (en) | 1986-01-30 | 1987-07-28 | Cetus Corporation | Process for amplifying, detecting, and/or-cloning nucleic acid sequences |
| DE229046T1 (de) | 1985-03-30 | 1987-12-17 | Marc Genf/Geneve Ballivet | Verfahren zum erhalten von dns, rns, peptiden, polypeptiden oder proteinen durch dns-rekombinant-verfahren. |
| US6492107B1 (en) | 1986-11-20 | 2002-12-10 | Stuart Kauffman | Process for obtaining DNA, RNA, peptides, polypeptides, or protein, by recombinant DNA technique |
| US5618920A (en) | 1985-11-01 | 1997-04-08 | Xoma Corporation | Modular assembly of antibody genes, antibodies prepared thereby and use |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US4704692A (en) | 1986-09-02 | 1987-11-03 | Ladner Robert C | Computer based system and method for determining and displaying possible chemical structures for converting double- or multiple-chain polypeptides to single-chain polypeptides |
| EP0832981A1 (en) | 1987-02-17 | 1998-04-01 | Pharming B.V. | DNA sequences to target proteins to the mammary gland for efficient secretion |
| US4873316A (en) | 1987-06-23 | 1989-10-10 | Biogen, Inc. | Isolation of exogenous recombinant proteins from the milk of transgenic mammals |
| US5677425A (en) | 1987-09-04 | 1997-10-14 | Celltech Therapeutics Limited | Recombinant antibody |
| GB8725529D0 (en) | 1987-10-30 | 1987-12-02 | Delta Biotechnology Ltd | Polypeptides |
| WO1990006952A1 (fr) | 1988-12-22 | 1990-06-28 | Kirin-Amgen, Inc. | Facteur de stimulation de colonies de granulocytes modifies chimiquement |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| DE3920358A1 (de) | 1989-06-22 | 1991-01-17 | Behringwerke Ag | Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung |
| SE509359C2 (sv) | 1989-08-01 | 1999-01-18 | Cemu Bioteknik Ab | Användning av stabiliserade protein- eller peptidkonjugat för framställning av ett läkemedel |
| US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US5686073A (en) | 1990-05-23 | 1997-11-11 | The University Of Iowa Research Foundation | Polyclonal and monoclonal antibodies against a 43 KDA dystrophin associated protein |
| US5580737A (en) | 1990-06-11 | 1996-12-03 | Nexstar Pharmaceuticals, Inc. | High-affinity nucleic acid ligands that discriminate between theophylline and caffeine |
| US5543293A (en) | 1990-06-11 | 1996-08-06 | Nexstar Pharmaceuticals, Inc. | DNA ligands of thrombin |
| US5503978A (en) | 1990-06-11 | 1996-04-02 | University Research Corporation | Method for identification of high affinity DNA ligands of HIV-1 reverse transcriptase |
| CA2090126C (en) | 1990-08-02 | 2002-10-22 | John W. Schrader | Methods for the production of proteins with a desired function |
| US6797492B2 (en) | 1991-05-17 | 2004-09-28 | Merck & Co., Inc. | Method for reducing the immunogenicity of antibody variable domains |
| EP0519596B1 (en) | 1991-05-17 | 2005-02-23 | Merck & Co. Inc. | A method for reducing the immunogenicity of antibody variable domains |
| ES2196002T3 (es) | 1991-07-25 | 2003-12-16 | Idec Pharma Corp | Anticuerpos recombinantes para terapia humana. |
| RU2212899C2 (ru) | 1991-09-13 | 2003-09-27 | Чирон Корпорейшн | Hcv иммунореактивные полипептидные композиции |
| ATE207080T1 (de) | 1991-11-25 | 2001-11-15 | Enzon Inc | Multivalente antigen-bindende proteine |
| EP0571613B1 (en) | 1991-12-13 | 2003-09-17 | Xoma Corporation | Methods and materials for preparation of modified antibody variable domains and therapeutic uses thereof |
| US5714350A (en) | 1992-03-09 | 1998-02-03 | Protein Design Labs, Inc. | Increasing antibody affinity by altering glycosylation in the immunoglobulin variable region |
| CA2118508A1 (en) | 1992-04-24 | 1993-11-11 | Elizabeth S. Ward | Recombinant production of immunoglobulin-like domains in prokaryotic cells |
| US5455338A (en) | 1993-11-05 | 1995-10-03 | Zymogenetics, Inc. | DNA encoding novel human kunitz-type inhibitors and methods relating thereto |
| US5827690A (en) | 1993-12-20 | 1998-10-27 | Genzyme Transgenics Corporatiion | Transgenic production of antibodies in milk |
| SE9400088D0 (sv) | 1994-01-14 | 1994-01-14 | Kabi Pharmacia Ab | Bacterial receptor structures |
| US5631146A (en) | 1995-01-19 | 1997-05-20 | The General Hospital Corporation | DNA aptamers and catalysts that bind adenosine or adenosine-5'-phosphates and methods for isolation thereof |
| US20050131222A1 (en) | 1995-04-21 | 2005-06-16 | Human Genome Sciences, Inc. | Nucleotide sequence of the haemophilus influenzae Rd genome, fragments thereof, and uses thereof |
| US5714352A (en) | 1996-03-20 | 1998-02-03 | Xenotech Incorporated | Directed switch-mediated DNA recombination |
| US6709659B1 (en) | 1996-08-02 | 2004-03-23 | Zymogenetics, Inc. | Antibodies that bind testis-specific insulin homolog polypeptides |
| DK1071700T3 (da) | 1998-04-20 | 2010-06-07 | Glycart Biotechnology Ag | Glykosylerings-modifikation af antistoffer til forbedring af antistofafhængig cellulær cytotoksicitet |
| ES2230848T3 (es) | 1998-04-28 | 2005-05-01 | Smithkline Beecham Corporation | Anticuerpos monoclonales con inmunogenicidad reducida. |
| US6322788B1 (en) | 1998-08-20 | 2001-11-27 | Stanley Arthur Kim | Anti-bacterial antibodies and methods of use |
| AU1728800A (en) | 1998-11-18 | 2000-06-05 | Genentech Inc. | Antibody variants with higher binding affinity compared to parent antibodies |
| US6303321B1 (en) | 1999-02-11 | 2001-10-16 | North Shore-Long Island Jewish Research Institute | Methods for diagnosing sepsis |
| US6939545B2 (en) | 1999-04-28 | 2005-09-06 | Genetics Institute, Llc | Composition and method for treating inflammatory disorders |
| US20020132753A1 (en) | 2000-01-31 | 2002-09-19 | Rosen Craig A. | Nucleic acids, proteins, and antibodies |
| ATE549347T1 (de) | 2000-09-08 | 2012-03-15 | Schering Corp | Gene von säugetiere, und damit verbundene reagentien, methoden |
| WO2004001058A2 (en) | 2001-05-04 | 2003-12-31 | Paratek Pharmaceuticals, Inc. | Transcription factor modulating compounds and methods of use thereof |
| CN100447154C (zh) | 2001-05-15 | 2008-12-31 | 费因斯坦医学研究学院 | 利用hmg片段作为抗炎症试剂 |
| AU2002328203C1 (en) | 2001-08-24 | 2009-01-08 | Migenix Inc. | Antimicrobial and anti-inflammatory peptides |
| ITMI20011986A1 (it) | 2001-09-25 | 2003-03-25 | San Raffaele Centro Fond | Metodo e composizione per l'attivazione di cellule presentanti l'antigene |
| US20030099602A1 (en) | 2001-10-25 | 2003-05-29 | Levin Gilbert V. | D-tagatose as an anti-biofilm agent |
| US20060057160A1 (en) | 2002-08-02 | 2006-03-16 | Ralph Biemans | Vaccine composition |
| JP2006510619A (ja) | 2002-11-20 | 2006-03-30 | クリティカル セラピューティクス，インコーポレイテッド | 抗炎症剤としてのｈｍｇｂ断片の使用 |
| US20060121047A1 (en) | 2002-11-20 | 2006-06-08 | Tracey Kevin J | Use of hmgb polypetides for increasing immune responses |
| WO2004061456A2 (de) | 2003-01-03 | 2004-07-22 | Alcedo Biotech Gmbh | Verwendungen von hmgb, hmgn, hmga proteinen |
| US7297340B2 (en) | 2003-01-07 | 2007-11-20 | University Of Iowa Research Foundation | Vaccine and method for preventing biofilm formation |
| WO2004072094A2 (en) | 2003-02-14 | 2004-08-26 | Fondazione Centro San Raffaele Del Monte Tabor | Hmgb1 modulator binding domain |
| CA2796381A1 (en) | 2003-03-06 | 2004-09-16 | Children's Hospital, Inc. | Genes of an otitis media isolate of nontypeable haemophilus influenzae |
| WO2005025604A2 (en) | 2003-09-10 | 2005-03-24 | The General Hospital Corporation | Use of hmgb and hmgb fragments to decrease specific immune response |
| US20090029929A1 (en) | 2004-03-26 | 2009-01-29 | Locomogene, Inc. | Decoy Nucleic Acid to Synoviolin Gene Promoter |
| GB0410866D0 (en) | 2004-05-14 | 2004-06-16 | Chiron Srl | Haemophilius influenzae |
| US20080305120A1 (en) | 2004-06-17 | 2008-12-11 | Medimmune, Inc. | Immunogenic Compositions Comprising Hmgb 1 Polypeptides |
| US20060030539A1 (en) | 2004-08-06 | 2006-02-09 | National Jewish Medical And Research Center | Product and process for inhibition of biofilm development |
| WO2007001422A2 (en) | 2004-10-22 | 2007-01-04 | Medimmune, Inc. | High affinity antibodies against hmgb1 and methods of use thereof |
| AU2005325801A1 (en) | 2005-01-31 | 2006-08-03 | Ablynx N.V. | Method for generating variable domain sequences of heavy chain antibodies |
| US7119179B1 (en) | 2005-03-21 | 2006-10-10 | Los Alamos National Security, Llc | Preparation of high nitrogen compound and materials therefrom |
| US20060228384A1 (en) | 2005-04-06 | 2006-10-12 | Sequoia Sciences, Inc. | Control of biofilm with a biofilm inhibitor |
| WO2006114805A2 (en) | 2005-04-28 | 2006-11-02 | Fondazione Centro San Raffaele Del Monte Tabor | Use of hmgb2 and hmgb3 proteins for medical applications |
| CA2631184A1 (en) | 2005-11-28 | 2007-05-31 | Genmab A/S | Recombinant monovalent antibodies and methods for production thereof |
| US20090264342A1 (en) | 2006-02-13 | 2009-10-22 | Trustees Of Boston University | Compositions and methods for antibiotic potentiation and drug discovery |
| CA2660668C (en) | 2006-08-21 | 2016-06-28 | The University Of British Columbia | Small cationic antimicrobial peptides |
| EP1980269A1 (en) | 2007-04-13 | 2008-10-15 | Katholieke Universiteit Leuven | Prevention of staphylococcus biofilm formation |
| CN103097399A (zh) | 2010-03-29 | 2013-05-08 | 南加利福尼亚大学 | 用于去除生物膜的组合物及方法 |
| ES2746971T3 (es) | 2013-06-13 | 2020-03-09 | Res Inst Nationwide Childrens Hospital | Composiciones y procedimientos para el tratamiento de infecciones por burkholderia |
| US9745366B2 (en) | 2013-09-23 | 2017-08-29 | University Of Southern California | Compositions and methods for the prevention of microbial infections |
| GB201508337D0 (en) * | 2015-05-15 | 2015-06-24 | Hmgbiotech S R L | Novel peptides |
| WO2018170178A1 (en) * | 2017-03-15 | 2018-09-20 | Research Institute At Nationwide Children's Hospital | Composition and methods for disruption of bacterial biofilms without accompanying inflammation |
| MX2020014006A (es) | 2018-06-29 | 2021-05-27 | Res Inst Nationwide Childrens Hospital | Composiciones y métodos para mediar la eps. |
| AU2019354829B2 (en) | 2018-10-05 | 2025-04-17 | Research Institute At Nationwide Children's Hospital | Hmgb1 protein derivatives for the removal of biofilms |
-
2018
- 2018-03-14 WO PCT/US2018/022508 patent/WO2018170178A1/en not_active Ceased
- 2018-03-14 JP JP2019550715A patent/JP7596069B2/ja active Active
- 2018-03-14 EP EP18718961.8A patent/EP3595445B1/en active Active
- 2018-03-14 US US16/492,582 patent/US11746136B2/en active Active
- 2018-03-14 CA CA3056088A patent/CA3056088A1/en active Pending
- 2018-03-14 AU AU2018236271A patent/AU2018236271B2/en active Active
-
2022
- 2022-12-05 JP JP2022194227A patent/JP2023014389A/ja active Pending
-
2025
- 2025-02-06 JP JP2025018512A patent/JP2025065351A/ja active Pending
- 2025-07-15 JP JP2025119036A patent/JP2025148518A/ja active Pending
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2013542185A (ja) | 2010-09-09 | 2013-11-21 | ユニバーシティー オブ サザン カリフォルニア | バイオフィルムを除去するための組成物および方法 |
| WO2014016417A1 (en) | 2012-07-26 | 2014-01-30 | Ospedale San Raffaele Srl | Hmgb1 variants and uses thereof |
Also Published As
| Publication number | Publication date |
|---|---|
| JP2025148518A (ja) | 2025-10-07 |
| AU2018236271B2 (en) | 2023-12-21 |
| JP2020513808A (ja) | 2020-05-21 |
| AU2018236271A1 (en) | 2019-10-03 |
| WO2018170178A1 (en) | 2018-09-20 |
| CA3056088A1 (en) | 2018-09-20 |
| EP3595445B1 (en) | 2024-09-04 |
| JP2023014389A (ja) | 2023-01-26 |
| WO2018170178A9 (en) | 2018-10-11 |
| EP3595445A1 (en) | 2020-01-22 |
| US11746136B2 (en) | 2023-09-05 |
| US20210139551A1 (en) | 2021-05-13 |
| JP2025065351A (ja) | 2025-04-17 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP7593979B2 (ja) | バイオフィルムの除去のためのペプチドおよび抗体 | |
| JP7596069B2 (ja) | 付随する炎症のない細菌バイオフィルムの破壊のための組成物および方法 | |
| US11690892B2 (en) | HU specific interfering agents | |
| JP7627255B2 (ja) | バイオフィルムを破壊するための抗体組成物 | |
| US20250368703A1 (en) | Hmgb1 protein derivatives for the removal of biofilms | |
| JP7514621B2 (ja) | Ｄｎａｂｉｉワクチンおよび強化された活性を有する抗体 | |
| JP7661008B2 (ja) | バイオフィルム関連障害の処置のための抗体断片 | |
| US20230406911A1 (en) | Compositions and methods for preventing, inhibiting, disrupting, or treating a polymicrobial biofilm | |
| RU2851685C2 (ru) | Композиции антител для разрушения биопленок |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20210309 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20210309 |
|
| A977 | Report on retrieval |
Free format text: JAPANESE INTERMEDIATE CODE: A971007 Effective date: 20211222 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20220111 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20220411 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20220805 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20221205 |
|
| C60 | Trial request (containing other claim documents, opposition documents) |
Free format text: JAPANESE INTERMEDIATE CODE: C60 Effective date: 20221205 |
|
| C11 | Written invitation by the commissioner to file amendments |
Free format text: JAPANESE INTERMEDIATE CODE: C11 Effective date: 20221214 |
|
| A911 | Transfer to examiner for re-examination before appeal (zenchi) |
Free format text: JAPANESE INTERMEDIATE CODE: A911 Effective date: 20221222 |
|
| C21 | Notice of transfer of a case for reconsideration by examiners before appeal proceedings |
Free format text: JAPANESE INTERMEDIATE CODE: C21 Effective date: 20221223 |
|
| A912 | Re-examination (zenchi) completed and case transferred to appeal board |
Free format text: JAPANESE INTERMEDIATE CODE: A912 Effective date: 20230203 |
|
| C211 | Notice of termination of reconsideration by examiners before appeal proceedings |
Free format text: JAPANESE INTERMEDIATE CODE: C211 Effective date: 20230207 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20240816 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20240930 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20241127 |
|
| R150 | Certificate of patent or registration of utility model |
Ref document number: 7596069 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 |