EA017203B1 - Связывающие молекулы человека, способные нейтрализовать вирус гриппа h5n1, и их применение - Google Patents
Связывающие молекулы человека, способные нейтрализовать вирус гриппа h5n1, и их применение Download PDFInfo
- Publication number
- EA017203B1 EA017203B1 EA200970255A EA200970255A EA017203B1 EA 017203 B1 EA017203 B1 EA 017203B1 EA 200970255 A EA200970255 A EA 200970255A EA 200970255 A EA200970255 A EA 200970255A EA 017203 B1 EA017203 B1 EA 017203B1
- Authority
- EA
- Eurasian Patent Office
- Prior art keywords
- region
- heavy chain
- binding molecule
- light chain
- chain
- Prior art date
Links
- 230000027455 binding Effects 0.000 title claims abstract description 523
- 241000712461 unidentified influenza virus Species 0.000 title claims abstract description 157
- 230000003472 neutralizing effect Effects 0.000 title claims abstract description 43
- 208000015181 infectious disease Diseases 0.000 claims abstract description 85
- 238000000034 method Methods 0.000 claims abstract description 81
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 56
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 47
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 47
- 206010022000 influenza Diseases 0.000 claims abstract description 40
- 238000011282 treatment Methods 0.000 claims abstract description 26
- 238000011321 prophylaxis Methods 0.000 claims abstract description 9
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 192
- 210000004027 cell Anatomy 0.000 claims description 139
- 101710154606 Hemagglutinin Proteins 0.000 claims description 135
- 101710093908 Outer capsid protein VP4 Proteins 0.000 claims description 135
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 claims description 135
- 101710176177 Protein A56 Proteins 0.000 claims description 135
- 239000000185 hemagglutinin Substances 0.000 claims description 120
- 108090000623 proteins and genes Proteins 0.000 claims description 44
- 102000004169 proteins and genes Human genes 0.000 claims description 37
- 150000001413 amino acids Chemical class 0.000 claims description 23
- 239000008194 pharmaceutical composition Substances 0.000 claims description 21
- 101100327398 Anopheles gambiae CecA gene Proteins 0.000 claims description 20
- 101100059601 Ceratitis capitata CEC1 gene Proteins 0.000 claims description 20
- 239000003814 drug Substances 0.000 claims description 17
- 230000009870 specific binding Effects 0.000 claims description 16
- 102100040837 Galactoside alpha-(1,2)-fucosyltransferase 2 Human genes 0.000 claims description 13
- 101000893710 Homo sapiens Galactoside alpha-(1,2)-fucosyltransferase 2 Proteins 0.000 claims description 13
- 101000882403 Staphylococcus aureus Enterotoxin type C-2 Proteins 0.000 claims description 13
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 12
- 101000882406 Staphylococcus aureus Enterotoxin type C-1 Proteins 0.000 claims description 9
- 238000004519 manufacturing process Methods 0.000 claims description 9
- 210000004602 germ cell Anatomy 0.000 claims description 6
- 101150007309 SOK3 gene Proteins 0.000 claims 15
- 101150060303 SOK2 gene Proteins 0.000 claims 14
- 101000628693 Homo sapiens Serine/threonine-protein kinase 25 Proteins 0.000 claims 13
- 102100026737 Serine/threonine-protein kinase 25 Human genes 0.000 claims 13
- 101000688543 Homo sapiens Shugoshin 2 Proteins 0.000 claims 6
- 102100024238 Shugoshin 2 Human genes 0.000 claims 6
- 101000909637 Homo sapiens Transcription factor COE1 Proteins 0.000 claims 1
- 102100024207 Transcription factor COE1 Human genes 0.000 claims 1
- 239000000203 mixture Substances 0.000 abstract description 42
- 238000003745 diagnosis Methods 0.000 abstract description 14
- 238000001727 in vivo Methods 0.000 abstract description 3
- 241000699670 Mus sp. Species 0.000 description 103
- 241000700605 Viruses Species 0.000 description 96
- 239000012634 fragment Substances 0.000 description 72
- 241001465754 Metazoa Species 0.000 description 51
- 239000000427 antigen Substances 0.000 description 39
- 108091007433 antigens Proteins 0.000 description 39
- 102000036639 antigens Human genes 0.000 description 39
- 229940127121 immunoconjugate Drugs 0.000 description 36
- 108090000765 processed proteins & peptides Proteins 0.000 description 34
- 235000018102 proteins Nutrition 0.000 description 34
- 230000037396 body weight Effects 0.000 description 33
- 238000004458 analytical method Methods 0.000 description 32
- 125000003729 nucleotide group Chemical group 0.000 description 32
- 239000013598 vector Substances 0.000 description 32
- 102000004196 processed proteins & peptides Human genes 0.000 description 31
- 239000002773 nucleotide Chemical group 0.000 description 29
- 235000001014 amino acid Nutrition 0.000 description 25
- 239000000243 solution Substances 0.000 description 22
- 239000000126 substance Substances 0.000 description 22
- 101100273868 Anopheles gambiae CecC gene Proteins 0.000 description 21
- 101100059604 Ceratitis capitata CEC2 gene Proteins 0.000 description 21
- 108060003951 Immunoglobulin Proteins 0.000 description 21
- 102000018358 immunoglobulin Human genes 0.000 description 21
- 241000282412 Homo Species 0.000 description 20
- 229940024606 amino acid Drugs 0.000 description 20
- 101100273858 Anopheles gambiae CecB gene Proteins 0.000 description 18
- 101100059603 Drosophila virilis Cec3 gene Proteins 0.000 description 18
- 239000002609 medium Substances 0.000 description 18
- 229920001184 polypeptide Polymers 0.000 description 18
- 230000001225 therapeutic effect Effects 0.000 description 18
- 102100027842 Fibroblast growth factor receptor 3 Human genes 0.000 description 17
- 101000917148 Homo sapiens Fibroblast growth factor receptor 3 Proteins 0.000 description 17
- 239000003795 chemical substances by application Substances 0.000 description 17
- 230000014509 gene expression Effects 0.000 description 17
- 230000002068 genetic effect Effects 0.000 description 17
- 238000002360 preparation method Methods 0.000 description 17
- 230000035772 mutation Effects 0.000 description 16
- 239000013642 negative control Substances 0.000 description 16
- 241000894006 Bacteria Species 0.000 description 15
- 239000000523 sample Substances 0.000 description 15
- 210000002966 serum Anatomy 0.000 description 15
- 108091028043 Nucleic acid sequence Proteins 0.000 description 14
- 238000006467 substitution reaction Methods 0.000 description 14
- 239000000872 buffer Substances 0.000 description 13
- 230000000069 prophylactic effect Effects 0.000 description 13
- 125000000539 amino acid group Chemical group 0.000 description 12
- 210000004369 blood Anatomy 0.000 description 12
- 239000008280 blood Substances 0.000 description 12
- 201000010099 disease Diseases 0.000 description 12
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 12
- 231100000636 lethal dose Toxicity 0.000 description 12
- 108020004414 DNA Proteins 0.000 description 11
- 241000196324 Embryophyta Species 0.000 description 11
- 238000003556 assay Methods 0.000 description 11
- 230000000903 blocking effect Effects 0.000 description 11
- 230000003993 interaction Effects 0.000 description 11
- 239000000725 suspension Substances 0.000 description 11
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 10
- 241000699666 Mus <mouse, genus> Species 0.000 description 10
- 230000000120 cytopathologic effect Effects 0.000 description 10
- 210000001806 memory b lymphocyte Anatomy 0.000 description 10
- 238000004806 packaging method and process Methods 0.000 description 10
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 9
- 241000124008 Mammalia Species 0.000 description 9
- 229920001213 Polysorbate 20 Polymers 0.000 description 9
- 210000003719 b-lymphocyte Anatomy 0.000 description 9
- 238000011081 inoculation Methods 0.000 description 9
- 230000004048 modification Effects 0.000 description 9
- 238000012986 modification Methods 0.000 description 9
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 9
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 9
- 239000000047 product Substances 0.000 description 9
- 230000009261 transgenic effect Effects 0.000 description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 206010038687 Respiratory distress Diseases 0.000 description 8
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 description 8
- 230000001133 acceleration Effects 0.000 description 8
- 230000003321 amplification Effects 0.000 description 8
- 230000000890 antigenic effect Effects 0.000 description 8
- 229940079593 drug Drugs 0.000 description 8
- 230000000694 effects Effects 0.000 description 8
- 239000001963 growth medium Substances 0.000 description 8
- 238000003199 nucleic acid amplification method Methods 0.000 description 8
- 239000011534 wash buffer Substances 0.000 description 8
- 229940098773 bovine serum albumin Drugs 0.000 description 7
- 239000000969 carrier Substances 0.000 description 7
- 230000008859 change Effects 0.000 description 7
- 238000002474 experimental method Methods 0.000 description 7
- 238000000684 flow cytometry Methods 0.000 description 7
- 230000001900 immune effect Effects 0.000 description 7
- 238000003119 immunoblot Methods 0.000 description 7
- 238000002156 mixing Methods 0.000 description 7
- 239000000843 powder Substances 0.000 description 7
- 239000003826 tablet Substances 0.000 description 7
- 238000002965 ELISA Methods 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 241000238631 Hexapoda Species 0.000 description 6
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 6
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 6
- 241000283973 Oryctolagus cuniculus Species 0.000 description 6
- 239000002202 Polyethylene glycol Substances 0.000 description 6
- 230000000295 complement effect Effects 0.000 description 6
- 239000002299 complementary DNA Substances 0.000 description 6
- 230000002354 daily effect Effects 0.000 description 6
- 238000012217 deletion Methods 0.000 description 6
- 230000037430 deletion Effects 0.000 description 6
- 238000011156 evaluation Methods 0.000 description 6
- 239000013604 expression vector Substances 0.000 description 6
- 210000005260 human cell Anatomy 0.000 description 6
- 229940072221 immunoglobulins Drugs 0.000 description 6
- 239000002054 inoculum Substances 0.000 description 6
- 238000003780 insertion Methods 0.000 description 6
- 230000037431 insertion Effects 0.000 description 6
- 231100000518 lethal Toxicity 0.000 description 6
- 230000001665 lethal effect Effects 0.000 description 6
- 229920001223 polyethylene glycol Polymers 0.000 description 6
- 108091033319 polynucleotide Proteins 0.000 description 6
- 102000040430 polynucleotide Human genes 0.000 description 6
- 239000002157 polynucleotide Substances 0.000 description 6
- 230000008569 process Effects 0.000 description 6
- 230000014616 translation Effects 0.000 description 6
- 229960005486 vaccine Drugs 0.000 description 6
- 230000004580 weight loss Effects 0.000 description 6
- 241000271566 Aves Species 0.000 description 5
- 108091026890 Coding region Proteins 0.000 description 5
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 5
- 101710104662 Enterotoxin type C-3 Proteins 0.000 description 5
- 102100030844 Exocyst complex component 1 Human genes 0.000 description 5
- 101100012877 Gallus gallus FGFR1 gene Proteins 0.000 description 5
- 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 5
- 230000001580 bacterial effect Effects 0.000 description 5
- 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 5
- 101150115874 cek1 gene Proteins 0.000 description 5
- 238000010367 cloning Methods 0.000 description 5
- 230000009137 competitive binding Effects 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 229960001031 glucose Drugs 0.000 description 5
- 239000008103 glucose Substances 0.000 description 5
- 230000001965 increasing effect Effects 0.000 description 5
- 238000002955 isolation Methods 0.000 description 5
- 210000004698 lymphocyte Anatomy 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 238000005259 measurement Methods 0.000 description 5
- 238000006386 neutralization reaction Methods 0.000 description 5
- 230000002265 prevention Effects 0.000 description 5
- 102000005962 receptors Human genes 0.000 description 5
- 108020003175 receptors Proteins 0.000 description 5
- 230000002829 reductive effect Effects 0.000 description 5
- 238000011160 research Methods 0.000 description 5
- 208000023504 respiratory system disease Diseases 0.000 description 5
- 238000012216 screening Methods 0.000 description 5
- 241000894007 species Species 0.000 description 5
- 238000010561 standard procedure Methods 0.000 description 5
- 239000006228 supernatant Substances 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 238000001890 transfection Methods 0.000 description 5
- 238000013519 translation Methods 0.000 description 5
- 241000701447 unidentified baculovirus Species 0.000 description 5
- 238000001262 western blot Methods 0.000 description 5
- 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 4
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 4
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 4
- 208000000059 Dyspnea Diseases 0.000 description 4
- 206010013975 Dyspnoeas Diseases 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 241000588724 Escherichia coli Species 0.000 description 4
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 4
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 4
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 4
- 102000003992 Peroxidases Human genes 0.000 description 4
- 101710172711 Structural protein Proteins 0.000 description 4
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 4
- 238000007792 addition Methods 0.000 description 4
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 4
- 229960000723 ampicillin Drugs 0.000 description 4
- 239000003443 antiviral agent Substances 0.000 description 4
- 239000011230 binding agent Substances 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 230000018109 developmental process Effects 0.000 description 4
- 238000010494 dissociation reaction Methods 0.000 description 4
- 230000005593 dissociations Effects 0.000 description 4
- 238000009826 distribution Methods 0.000 description 4
- 239000012636 effector Substances 0.000 description 4
- 108020001507 fusion proteins Proteins 0.000 description 4
- 102000037865 fusion proteins Human genes 0.000 description 4
- 239000008187 granular material Substances 0.000 description 4
- 230000003053 immunization Effects 0.000 description 4
- 230000002779 inactivation Effects 0.000 description 4
- 230000002458 infectious effect Effects 0.000 description 4
- 239000000543 intermediate Substances 0.000 description 4
- 239000011159 matrix material Substances 0.000 description 4
- 230000001404 mediated effect Effects 0.000 description 4
- 239000002184 metal Substances 0.000 description 4
- 229910052751 metal Inorganic materials 0.000 description 4
- 108040007629 peroxidase activity proteins Proteins 0.000 description 4
- 239000013612 plasmid Substances 0.000 description 4
- 230000003449 preventive effect Effects 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 238000010188 recombinant method Methods 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 230000001932 seasonal effect Effects 0.000 description 4
- 208000013220 shortness of breath Diseases 0.000 description 4
- 238000002741 site-directed mutagenesis Methods 0.000 description 4
- 239000007787 solid Substances 0.000 description 4
- 238000010186 staining Methods 0.000 description 4
- 238000012546 transfer Methods 0.000 description 4
- 229910021642 ultra pure water Inorganic materials 0.000 description 4
- 239000012498 ultrapure water Substances 0.000 description 4
- 241001515965 unidentified phage Species 0.000 description 4
- 239000004474 valine Substances 0.000 description 4
- 230000009385 viral infection Effects 0.000 description 4
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- 229920001817 Agar Polymers 0.000 description 3
- 241000283707 Capra Species 0.000 description 3
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 3
- 108010052285 Membrane Proteins Proteins 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 241001494479 Pecora Species 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 240000005499 Sasa Species 0.000 description 3
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 3
- 239000004098 Tetracycline Substances 0.000 description 3
- 239000002671 adjuvant Substances 0.000 description 3
- 239000008272 agar Substances 0.000 description 3
- 210000004436 artificial bacterial chromosome Anatomy 0.000 description 3
- 239000012472 biological sample Substances 0.000 description 3
- 238000004113 cell culture Methods 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 239000012707 chemical precursor Substances 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 230000021615 conjugation Effects 0.000 description 3
- 230000009260 cross reactivity Effects 0.000 description 3
- 230000034994 death Effects 0.000 description 3
- 239000002552 dosage form Substances 0.000 description 3
- 238000004520 electroporation Methods 0.000 description 3
- 230000002708 enhancing effect Effects 0.000 description 3
- 238000000605 extraction Methods 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 235000013922 glutamic acid Nutrition 0.000 description 3
- 239000004220 glutamic acid Substances 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 238000002649 immunization Methods 0.000 description 3
- 238000003018 immunoassay Methods 0.000 description 3
- 238000011532 immunohistochemical staining Methods 0.000 description 3
- 230000000977 initiatory effect Effects 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 238000013507 mapping Methods 0.000 description 3
- 230000001717 pathogenic effect Effects 0.000 description 3
- 238000002823 phage display Methods 0.000 description 3
- 210000004180 plasmocyte Anatomy 0.000 description 3
- 239000013641 positive control Substances 0.000 description 3
- 238000012545 processing Methods 0.000 description 3
- 230000001681 protective effect Effects 0.000 description 3
- 238000003127 radioimmunoassay Methods 0.000 description 3
- 230000009257 reactivity Effects 0.000 description 3
- 238000011084 recovery Methods 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 230000029058 respiratory gaseous exchange Effects 0.000 description 3
- 235000020183 skimmed milk Nutrition 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 208000024891 symptom Diseases 0.000 description 3
- 230000002195 synergetic effect Effects 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 229960002180 tetracycline Drugs 0.000 description 3
- 229930101283 tetracycline Natural products 0.000 description 3
- 235000019364 tetracycline Nutrition 0.000 description 3
- 150000003522 tetracyclines Chemical class 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 230000009466 transformation Effects 0.000 description 3
- -1 troches Substances 0.000 description 3
- PUPZLCDOIYMWBV-UHFFFAOYSA-N (+/-)-1,3-Butanediol Chemical compound CC(O)CCO PUPZLCDOIYMWBV-UHFFFAOYSA-N 0.000 description 2
- UBCHPRBFMUDMNC-UHFFFAOYSA-N 1-(1-adamantyl)ethanamine Chemical compound C1C(C2)CC3CC2CC1(C(N)C)C3 UBCHPRBFMUDMNC-UHFFFAOYSA-N 0.000 description 2
- 241000272814 Anser sp. Species 0.000 description 2
- 108091035707 Consensus sequence Proteins 0.000 description 2
- 102100023600 Fibroblast growth factor receptor 2 Human genes 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 101100113588 Homo sapiens CS gene Proteins 0.000 description 2
- 101000827688 Homo sapiens Fibroblast growth factor receptor 2 Proteins 0.000 description 2
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- 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 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 101000633946 Lophiotoma olangoensis Turripeptide Lol6.2 Proteins 0.000 description 2
- 108010090054 Membrane Glycoproteins Proteins 0.000 description 2
- 102000012750 Membrane Glycoproteins Human genes 0.000 description 2
- 241000282339 Mustela Species 0.000 description 2
- 102000005348 Neuraminidase Human genes 0.000 description 2
- 108010006232 Neuraminidase Proteins 0.000 description 2
- 102000011931 Nucleoproteins Human genes 0.000 description 2
- 108010061100 Nucleoproteins Proteins 0.000 description 2
- 206010057249 Phagocytosis Diseases 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- 108700019146 Transgenes Proteins 0.000 description 2
- 102000004142 Trypsin Human genes 0.000 description 2
- 108090000631 Trypsin Proteins 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- DZBUGLKDJFMEHC-UHFFFAOYSA-N acridine Chemical compound C1=CC=CC2=CC3=CC=CC=C3N=C21 DZBUGLKDJFMEHC-UHFFFAOYSA-N 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- DKNWSYNQZKUICI-UHFFFAOYSA-N amantadine Chemical compound C1C(C2)CC3CC2CC1(N)C3 DKNWSYNQZKUICI-UHFFFAOYSA-N 0.000 description 2
- 229960003805 amantadine Drugs 0.000 description 2
- 238000010171 animal model Methods 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 230000000692 anti-sense effect Effects 0.000 description 2
- 229940088710 antibiotic agent Drugs 0.000 description 2
- 239000003963 antioxidant agent Substances 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 206010064097 avian influenza Diseases 0.000 description 2
- VEZXCJBBBCKRPI-UHFFFAOYSA-N beta-propiolactone Chemical compound O=C1CCO1 VEZXCJBBBCKRPI-UHFFFAOYSA-N 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 229940041514 candida albicans extract Drugs 0.000 description 2
- 239000002738 chelating agent Substances 0.000 description 2
- 238000004140 cleaning Methods 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 239000012502 diagnostic product Substances 0.000 description 2
- 239000003085 diluting agent Substances 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 229940042406 direct acting antivirals neuraminidase inhibitors Drugs 0.000 description 2
- 235000013601 eggs Nutrition 0.000 description 2
- 210000002257 embryonic structure Anatomy 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 230000002349 favourable effect Effects 0.000 description 2
- 239000012894 fetal calf serum Substances 0.000 description 2
- 238000004108 freeze drying Methods 0.000 description 2
- 230000002538 fungal effect Effects 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 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 2
- 230000013595 glycosylation Effects 0.000 description 2
- 238000006206 glycosylation reaction Methods 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 238000003384 imaging method Methods 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 239000004615 ingredient Substances 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- 229960000318 kanamycin Drugs 0.000 description 2
- 229930027917 kanamycin Natural products 0.000 description 2
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 2
- 229930182823 kanamycin A Natural products 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 230000011987 methylation Effects 0.000 description 2
- 238000007069 methylation reaction Methods 0.000 description 2
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 2
- 229960003752 oseltamivir Drugs 0.000 description 2
- VSZGPKBBMSAYNT-RRFJBIMHSA-N oseltamivir Chemical compound CCOC(=O)C1=C[C@@H](OC(CC)CC)[C@H](NC(C)=O)[C@@H](N)C1 VSZGPKBBMSAYNT-RRFJBIMHSA-N 0.000 description 2
- 238000007911 parenteral administration Methods 0.000 description 2
- 210000005259 peripheral blood Anatomy 0.000 description 2
- 239000011886 peripheral blood Substances 0.000 description 2
- 230000008782 phagocytosis Effects 0.000 description 2
- 239000012071 phase Substances 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 239000004033 plastic Substances 0.000 description 2
- 229920003023 plastic Polymers 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 244000144977 poultry Species 0.000 description 2
- 235000013594 poultry meat Nutrition 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 239000003755 preservative agent Substances 0.000 description 2
- 230000000644 propagated effect Effects 0.000 description 2
- 229960000380 propiolactone Drugs 0.000 description 2
- ZCCUUQDIBDJBTK-UHFFFAOYSA-N psoralen Chemical compound C1=C2OC(=O)C=CC2=CC2=C1OC=C2 ZCCUUQDIBDJBTK-UHFFFAOYSA-N 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
- 230000002285 radioactive effect Effects 0.000 description 2
- 239000000941 radioactive substance Substances 0.000 description 2
- 210000002345 respiratory system Anatomy 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 210000003705 ribosome Anatomy 0.000 description 2
- 229960000888 rimantadine Drugs 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 239000002911 sialidase inhibitor Substances 0.000 description 2
- 238000009097 single-agent therapy Methods 0.000 description 2
- 238000005063 solubilization Methods 0.000 description 2
- 230000007928 solubilization Effects 0.000 description 2
- 229940043517 specific immunoglobulins Drugs 0.000 description 2
- 230000000087 stabilizing effect Effects 0.000 description 2
- 210000000130 stem cell Anatomy 0.000 description 2
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 2
- 230000004083 survival effect Effects 0.000 description 2
- 238000001308 synthesis method Methods 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 229940124597 therapeutic agent Drugs 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 2
- 238000004448 titration Methods 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 230000001131 transforming effect Effects 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- 239000012138 yeast extract Substances 0.000 description 2
- 229960001028 zanamivir Drugs 0.000 description 2
- ARAIBEBZBOPLMB-UFGQHTETSA-N zanamivir Chemical compound CC(=O)N[C@@H]1[C@@H](N=C(N)N)C=C(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO ARAIBEBZBOPLMB-UFGQHTETSA-N 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- VXGRJERITKFWPL-UHFFFAOYSA-N 4',5'-Dihydropsoralen Natural products C1=C2OC(=O)C=CC2=CC2=C1OCC2 VXGRJERITKFWPL-UHFFFAOYSA-N 0.000 description 1
- OXEUETBFKVCRNP-UHFFFAOYSA-N 9-ethyl-3-carbazolamine Chemical compound NC1=CC=C2N(CC)C3=CC=CC=C3C2=C1 OXEUETBFKVCRNP-UHFFFAOYSA-N 0.000 description 1
- 101150011812 AADAC gene Proteins 0.000 description 1
- 101150018711 AASS gene Proteins 0.000 description 1
- 206010069754 Acquired gene mutation Diseases 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 102100034112 Alkyldihydroxyacetonephosphate synthase, peroxisomal Human genes 0.000 description 1
- 235000006576 Althaea officinalis Nutrition 0.000 description 1
- 101001053395 Arabidopsis thaliana Acid beta-fructofuranosidase 4, vacuolar Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000182988 Assa Species 0.000 description 1
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 241000283153 Cetacea Species 0.000 description 1
- 241000128735 Chapsa Species 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 206010011224 Cough Diseases 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 102000012410 DNA Ligases Human genes 0.000 description 1
- 108010061982 DNA Ligases Proteins 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 206010012735 Diarrhoea Diseases 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 241000192125 Firmicutes Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 239000001828 Gelatine Substances 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 1
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 1
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 1
- 108010093488 His-His-His-His-His-His Proteins 0.000 description 1
- 102100039121 Histone-lysine N-methyltransferase MECOM Human genes 0.000 description 1
- 101000799143 Homo sapiens Alkyldihydroxyacetonephosphate synthase, peroxisomal Proteins 0.000 description 1
- 101001033728 Homo sapiens Histone-lysine N-methyltransferase MECOM Proteins 0.000 description 1
- 101001090813 Homo sapiens Proteasome subunit alpha type-6 Proteins 0.000 description 1
- 101000912352 Homo sapiens Putative uncharacterized protein DANCR Proteins 0.000 description 1
- 101000772888 Homo sapiens Ubiquitin-protein ligase E3A Proteins 0.000 description 1
- 101000693630 Homo sapiens Uncharacterized serine/threonine-protein kinase SBK3 Proteins 0.000 description 1
- 229940124873 Influenza virus vaccine Drugs 0.000 description 1
- 102100034343 Integrase Human genes 0.000 description 1
- 206010022678 Intestinal infections Diseases 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
- 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
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- 206010025327 Lymphopenia 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
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 101000966481 Mus musculus Dihydrofolate reductase Proteins 0.000 description 1
- GXCLVBGFBYZDAG-UHFFFAOYSA-N N-[2-(1H-indol-3-yl)ethyl]-N-methylprop-2-en-1-amine Chemical compound CN(CCC1=CNC2=C1C=CC=C2)CC=C GXCLVBGFBYZDAG-UHFFFAOYSA-N 0.000 description 1
- 238000005481 NMR spectroscopy Methods 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108010067902 Peptide Library Proteins 0.000 description 1
- 229920002732 Polyanhydride Polymers 0.000 description 1
- 239000004698 Polyethylene Substances 0.000 description 1
- 229920000954 Polyglycolide Polymers 0.000 description 1
- 108010039918 Polylysine Proteins 0.000 description 1
- 229920001710 Polyorthoester Polymers 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 206010036790 Productive cough Diseases 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 206010037660 Pyrexia Diseases 0.000 description 1
- 239000013614 RNA sample Substances 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 206010057190 Respiratory tract infections Diseases 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 241000700584 Simplexvirus Species 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 239000004809 Teflon Substances 0.000 description 1
- 229920006362 Teflon® Polymers 0.000 description 1
- RYYWUUFWQRZTIU-UHFFFAOYSA-N Thiophosphoric acid Chemical class OP(O)(S)=O RYYWUUFWQRZTIU-UHFFFAOYSA-N 0.000 description 1
- 108020004440 Thymidine kinase Proteins 0.000 description 1
- 102100030434 Ubiquitin-protein ligase E3A Human genes 0.000 description 1
- 208000025865 Ulcer Diseases 0.000 description 1
- 102100025558 Uncharacterized serine/threonine-protein kinase SBK3 Human genes 0.000 description 1
- 108010067390 Viral Proteins Proteins 0.000 description 1
- 230000010530 Virus Neutralization Effects 0.000 description 1
- 108010084455 Zeocin Proteins 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 238000010306 acid treatment Methods 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 230000010933 acylation Effects 0.000 description 1
- 238000005917 acylation reaction Methods 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 230000009824 affinity maturation Effects 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 239000002168 alkylating agent Substances 0.000 description 1
- 238000000848 angular dependent Auger electron spectroscopy Methods 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 229940127219 anticoagulant drug Drugs 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 1
- 125000003118 aryl group Chemical group 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
- 230000002238 attenuated effect Effects 0.000 description 1
- 108010029566 avian influenza A virus hemagglutinin Proteins 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 230000008901 benefit Effects 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
- 102000023732 binding proteins Human genes 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 238000002306 biochemical method Methods 0.000 description 1
- 229920000249 biocompatible polymer Polymers 0.000 description 1
- 239000012620 biological material Substances 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 210000001185 bone marrow Anatomy 0.000 description 1
- DQXBYHZEEUGOBF-UHFFFAOYSA-N but-3-enoic acid;ethene Chemical compound C=C.OC(=O)CC=C DQXBYHZEEUGOBF-UHFFFAOYSA-N 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 150000004657 carbamic acid derivatives Chemical class 0.000 description 1
- 230000007910 cell fusion Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 235000013339 cereals Nutrition 0.000 description 1
- 239000013522 chelant Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- ZYWFEOZQIUMEGL-UHFFFAOYSA-N chloroform;3-methylbutan-1-ol;phenol Chemical compound ClC(Cl)Cl.CC(C)CCO.OC1=CC=CC=C1 ZYWFEOZQIUMEGL-UHFFFAOYSA-N 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 239000003086 colorant Substances 0.000 description 1
- 238000010835 comparative analysis Methods 0.000 description 1
- 238000012875 competitive assay Methods 0.000 description 1
- 230000006957 competitive inhibition Effects 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 239000013256 coordination polymer Substances 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 229940039227 diagnostic agent Drugs 0.000 description 1
- 239000000032 diagnostic agent Substances 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- ZMXDDKWLCZADIW-UHFFFAOYSA-N dimethylformamide Substances CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 1
- NAGJZTKCGNOGPW-UHFFFAOYSA-N dithiophosphoric acid Chemical class OP(O)(S)=S NAGJZTKCGNOGPW-UHFFFAOYSA-N 0.000 description 1
- 239000008298 dragée Substances 0.000 description 1
- 230000035622 drinking Effects 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- UXOLDCOJRAMLTQ-UHFFFAOYSA-N ethyl 2-chloro-2-hydroxyiminoacetate Chemical compound CCOC(=O)C(Cl)=NO UXOLDCOJRAMLTQ-UHFFFAOYSA-N 0.000 description 1
- 239000005038 ethylene vinyl acetate Substances 0.000 description 1
- 230000003203 everyday effect Effects 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 239000000796 flavoring agent Substances 0.000 description 1
- 235000019634 flavors Nutrition 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 235000003599 food sweetener Nutrition 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 238000001415 gene therapy Methods 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 238000005469 granulation Methods 0.000 description 1
- 230000003179 granulation Effects 0.000 description 1
- 239000005090 green fluorescent protein Substances 0.000 description 1
- 244000144993 groups of animals Species 0.000 description 1
- 239000007902 hard capsule Substances 0.000 description 1
- 230000003067 hemagglutinative effect Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 102000051411 human PSMA6 Human genes 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000033444 hydroxylation Effects 0.000 description 1
- 238000005805 hydroxylation reaction Methods 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000010166 immunofluorescence Methods 0.000 description 1
- 230000002055 immunohistochemical effect Effects 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000003701 inert diluent Substances 0.000 description 1
- 229960003971 influenza vaccine Drugs 0.000 description 1
- 108700010900 influenza virus proteins Proteins 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 150000002484 inorganic compounds Chemical group 0.000 description 1
- 229910010272 inorganic material Inorganic materials 0.000 description 1
- 210000000936 intestine Anatomy 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 230000007794 irritation Effects 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 239000003589 local anesthetic agent Substances 0.000 description 1
- 229960005015 local anesthetics Drugs 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 239000007937 lozenge Substances 0.000 description 1
- 239000000314 lubricant Substances 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 231100001023 lymphopenia Toxicity 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 210000003071 memory t lymphocyte Anatomy 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- YACKEPLHDIMKIO-UHFFFAOYSA-N methylphosphonic acid Chemical class CP(O)(O)=O YACKEPLHDIMKIO-UHFFFAOYSA-N 0.000 description 1
- 238000000520 microinjection 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
- 230000003278 mimic effect Effects 0.000 description 1
- 239000002480 mineral oil Substances 0.000 description 1
- 230000009149 molecular binding Effects 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 150000002894 organic compounds Chemical group 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 238000004091 panning Methods 0.000 description 1
- 230000005298 paramagnetic effect Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000007918 pathogenicity Effects 0.000 description 1
- 231100000915 pathological change Toxicity 0.000 description 1
- 230000036285 pathological change Effects 0.000 description 1
- 230000006320 pegylation Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 1
- CWCMIVBLVUHDHK-ZSNHEYEWSA-N phleomycin D1 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@@H](N=1)C=1SC=C(N=1)C(=O)NCCCCNC(N)=N)[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 CWCMIVBLVUHDHK-ZSNHEYEWSA-N 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 150000008298 phosphoramidates Chemical class 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 229920001200 poly(ethylene-vinyl acetate) Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 239000004633 polyglycolic acid Substances 0.000 description 1
- 229920002704 polyhistidine Polymers 0.000 description 1
- 229920000656 polylysine Polymers 0.000 description 1
- 210000002729 polyribosome Anatomy 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 229950010131 puromycin Drugs 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000000241 respiratory effect Effects 0.000 description 1
- 210000001525 retina Anatomy 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 239000003161 ribonuclease inhibitor Substances 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 238000007790 scraping Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 239000013049 sediment Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 150000003384 small molecules Chemical group 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 230000037439 somatic mutation Effects 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 238000011895 specific detection Methods 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 208000024794 sputum Diseases 0.000 description 1
- 210000003802 sputum Anatomy 0.000 description 1
- 230000010473 stable expression Effects 0.000 description 1
- 239000008174 sterile solution Substances 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 230000035882 stress Effects 0.000 description 1
- 238000013268 sustained release Methods 0.000 description 1
- 239000012730 sustained-release form Substances 0.000 description 1
- 239000003765 sweetening agent Substances 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 230000004797 therapeutic response Effects 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 231100000167 toxic agent Toxicity 0.000 description 1
- 239000003440 toxic substance Substances 0.000 description 1
- 230000002110 toxicologic effect Effects 0.000 description 1
- 231100000759 toxicological effect Toxicity 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000011830 transgenic mouse model Methods 0.000 description 1
- 230000010474 transient expression Effects 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 238000011269 treatment regimen Methods 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 231100000397 ulcer Toxicity 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 238000002255 vaccination Methods 0.000 description 1
- 238000001291 vacuum drying Methods 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- 210000002268 wool Anatomy 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
- C07K16/1018—Orthomyxoviridae, e.g. influenza virus
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/12—Viral antigens
- A61K39/145—Orthomyxoviridae, e.g. influenza virus
-
- 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
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
- A61P31/16—Antivirals for RNA viruses for influenza or rhinoviruses
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/10—Cells modified by introduction of foreign genetic material
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
- G01N33/56983—Viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/33—Crossreactivity, e.g. for species or epitope, or lack of said crossreactivity
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
- C07K2317/62—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising only variable region components
- C07K2317/622—Single chain antibody (scFv)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2760/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses negative-sense
- C12N2760/00011—Details
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2760/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses negative-sense
- C12N2760/00011—Details
- C12N2760/00061—Methods of inactivation or attenuation
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2760/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses negative-sense
- C12N2760/00011—Details
- C12N2760/16011—Orthomyxoviridae
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2760/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses negative-sense
- C12N2760/00011—Details
- C12N2760/16011—Orthomyxoviridae
- C12N2760/16061—Methods of inactivation or attenuation
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2760/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses negative-sense
- C12N2760/00011—Details
- C12N2760/16011—Orthomyxoviridae
- C12N2760/16111—Influenzavirus A, i.e. influenza A virus
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/005—Assays involving biological materials from specific organisms or of a specific nature from viruses
- G01N2333/08—RNA viruses
- G01N2333/11—Orthomyxoviridae, e.g. influenza virus
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2469/00—Immunoassays for the detection of microorganisms
- G01N2469/10—Detection of antigens from microorganism in sample from host
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Virology (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Biomedical Technology (AREA)
- Pulmonology (AREA)
- Biotechnology (AREA)
- Biophysics (AREA)
- Communicable Diseases (AREA)
- Microbiology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Engineering & Computer Science (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Cell Biology (AREA)
- Physics & Mathematics (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Food Science & Technology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Analytical Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Mycology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
Applications Claiming Priority (6)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US84293006P | 2006-09-07 | 2006-09-07 | |
| EP06120316 | 2006-09-07 | ||
| EP06120644 | 2006-09-14 | ||
| EP06125107 | 2006-11-30 | ||
| EP07111235 | 2007-06-28 | ||
| PCT/EP2007/059356 WO2008028946A2 (en) | 2006-09-07 | 2007-09-06 | Human binding molecules capable of neutralizing influenza virus h5n1 and uses thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EA200970255A1 EA200970255A1 (ru) | 2009-10-30 |
| EA017203B1 true EA017203B1 (ru) | 2012-10-30 |
Family
ID=39027173
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EA200970255A EA017203B1 (ru) | 2006-09-07 | 2007-09-06 | Связывающие молекулы человека, способные нейтрализовать вирус гриппа h5n1, и их применение |
Country Status (15)
| Country | Link |
|---|---|
| US (5) | US8192927B2 (OSRAM) |
| EP (2) | EP2450377A1 (OSRAM) |
| JP (2) | JP5161882B2 (OSRAM) |
| KR (1) | KR101485197B1 (OSRAM) |
| AU (1) | AU2007293662B2 (OSRAM) |
| CA (1) | CA2663388C (OSRAM) |
| EA (1) | EA017203B1 (OSRAM) |
| HR (1) | HRP20130163T1 (OSRAM) |
| IL (2) | IL197390A (OSRAM) |
| MX (1) | MX2009002174A (OSRAM) |
| MY (1) | MY170607A (OSRAM) |
| NO (1) | NO20091321L (OSRAM) |
| PL (1) | PL2059532T3 (OSRAM) |
| WO (1) | WO2008028946A2 (OSRAM) |
| ZA (1) | ZA200901171B (OSRAM) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2701694C2 (ru) * | 2013-03-14 | 2019-09-30 | Контрафект Корпорейшн | Композиции и способы, основанные на нейтрализующих антителах, доставляемых интраназально, для улучшенной терапевтической эффективности |
Families Citing this family (155)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20160279239A1 (en) | 2011-05-02 | 2016-09-29 | Immunomedics, Inc. | Subcutaneous administration of anti-cd74 antibody for systemic lupus erythematosus and autoimmune disease |
| SI1523496T1 (sl) | 2002-07-18 | 2011-11-30 | Merus B V | Rekombinantno proizvajanje zmesi protiteles |
| USRE47770E1 (en) | 2002-07-18 | 2019-12-17 | Merus N.V. | Recombinant production of mixtures of antibodies |
| US20100069614A1 (en) | 2008-06-27 | 2010-03-18 | Merus B.V. | Antibody producing non-human mammals |
| EP2395017A3 (en) | 2003-05-30 | 2012-12-19 | Merus B.V. | Design and use of paired variable regions of specific binding molecules |
| KR101206206B1 (ko) * | 2003-07-22 | 2012-11-29 | 크루셀 홀란드 비.브이. | 사스-코로나바이러스에 대한 결합분자 및 그것의 용도 |
| CN102139106B (zh) * | 2004-05-27 | 2014-10-08 | 克鲁塞尔荷兰公司 | 能中和狂犬病病毒的结合分子及其应用 |
| JP4852046B2 (ja) * | 2004-10-12 | 2012-01-11 | クルセル ホランド ベー ヴェー | 癌の治療及び検出に用いる結合分子 |
| US20160355591A1 (en) | 2011-05-02 | 2016-12-08 | Immunomedics, Inc. | Subcutaneous anti-hla-dr monoclonal antibody for treatment of hematologic malignancies |
| WO2006120230A2 (en) | 2005-05-12 | 2006-11-16 | Crucell Holland B.V. | Host cell specific binding molecules capable of neutralizing viruses and uses thereof |
| US8148085B2 (en) | 2006-05-15 | 2012-04-03 | Sea Lane Biotechnologies, Llc | Donor specific antibody libraries |
| EP3018142A1 (en) | 2006-06-06 | 2016-05-11 | Crucell Holland B.V. | Human binding molecules having killing activity against staphylococci and uses thereof |
| MY170607A (en) | 2006-09-07 | 2019-08-20 | Crucell Holland Bv | Human binding molecules capable of neutralizing influenza virus h5n1 and uses thereof |
| EP2125886A2 (en) | 2007-03-13 | 2009-12-02 | Humabs LLC | Antibodies against h5n1 strains of influenza a virus |
| CA2680237C (en) | 2007-03-27 | 2018-11-06 | Sea Lane Biotechnologies, Llc | Constructs and libraries comprising antibody surrogate light chain sequences |
| EP2036045A1 (en) * | 2007-07-11 | 2009-03-18 | Cairos technologies AG | Video tracking method and appartus arrangement for performing the method |
| US8444986B2 (en) | 2007-09-13 | 2013-05-21 | Temasek Life Sciences Laboratory Limited | Monoclonal antibodies specific to hemagglutinin from influenza virus H5-subtype and uses thereof |
| EP2947094B1 (en) | 2007-09-13 | 2018-11-14 | Temasek Life Sciences Laboratory Limited | Monoclonal antibodies specific to hemagglutinin and neuraminidase from influenza virus h5-subtype or n1-subtype and uses thereof |
| WO2009079259A2 (en) * | 2007-12-06 | 2009-06-25 | Dana-Farber Cancer Institute, Inc. | Antibodies against influenza virus and methods of use thereof |
| ITTO20080204A1 (it) | 2008-03-17 | 2009-09-18 | Pomona Biotechnologies Llc | Anticorpi monoclonali atti a reagire con una pluralita di sottotipi del virus influenzale a |
| AU2009228058A1 (en) | 2008-03-28 | 2009-10-01 | Sea Lane Biotechnologies, Llc | Neutralizing molecules to viral antigens |
| ITTO20080398A1 (it) | 2008-05-27 | 2009-11-28 | Pomona Biotechnologies Llc | Anticorpi monoclonali aventi proprieta' di cross-neutralizzazione omosubtipica per virus influenzali di tipo a sottotipo h1 |
| US8871207B2 (en) | 2008-07-25 | 2014-10-28 | Humabs, LLC | Neutralizing anti-influenza A virus antibodies and uses thereof |
| KR20110049802A (ko) | 2008-07-25 | 2011-05-12 | 인스티튜트 포 리서치 인 바이오메드슨 | 중화 항-인플루엔자 ａ 바이러스 항체 및 이의 용도 |
| GB0818356D0 (en) * | 2008-10-07 | 2008-11-12 | Istituto Superiore Di Sanito | Antibodies |
| AR073770A1 (es) * | 2008-10-20 | 2010-12-01 | Imclone Llc | Anticuerpo aislado que se enlaza especificamente con, e induce la degradacion del receptor-3 del factor de crecimiento del fibroblasto humano (fgfr-3), fragmento de enlace fgfr-3 humano del mismo, composicion farmaceutica y producto que lo comprenden |
| US9347043B2 (en) | 2008-10-22 | 2016-05-24 | Institute For Research In Biomedicine | Methods for producing antibodies from plasma cells |
| CN102438652B (zh) * | 2008-11-12 | 2014-08-13 | 米迪缪尼有限公司 | 抗体制剂 |
| SG172333A1 (en) | 2008-12-24 | 2011-07-28 | Temasek Life Sciences Lab Ltd | Monoclonal antibodies specific to the fusion peptide from hemagglutinin from influenza a viruses and uses thereof |
| EP3009145A1 (en) | 2009-03-30 | 2016-04-20 | Mount Sinai School of Medicine of New York University | Influenza virus vaccines and uses thereof |
| US8894997B2 (en) | 2009-04-30 | 2014-11-25 | Vanderbilt University | Monoclonal antibodies to influenza H1N1 virus uses thereof |
| US8470327B2 (en) * | 2009-05-11 | 2013-06-25 | Crucell Holland B.V. | Human binding molecules capable of neutralizing influenza virus H3N2 and uses thereof |
| WO2010132604A2 (en) | 2009-05-13 | 2010-11-18 | Sea Lane Biotechnologies, Llc | Neutralizing molecules to influenza viruses |
| AU2010254136B2 (en) | 2009-05-26 | 2016-09-29 | Mount Sinai School Of Medicine | Monoclonal antibodies against influenza virus generated by cyclical administration and uses thereof |
| EP2464383A4 (en) * | 2009-08-14 | 2013-02-13 | Theraclone Sciences Inc | COMPOSITIONS AND METHODS FOR THE TREATMENT AND DIAGNOSIS OF FLU |
| US9458226B2 (en) | 2009-10-09 | 2016-10-04 | Emory University | Recombinant antibodies against H1N1 influenza |
| AU2011210840B2 (en) * | 2010-01-27 | 2014-12-11 | Massachusetts Institute Of Technology | Engineered polypeptide agents for targeted broad spectrum influenza neutralization |
| BR112012020839A2 (pt) | 2010-02-18 | 2017-11-21 | Sinai School Medicine | vacinas para uso na profilaxe e tratamento de doença de vírus da influenza |
| JP5795340B2 (ja) * | 2010-03-08 | 2015-10-14 | セルトリオン インクＣｅｌｌｔｒｉｏｎ，Ｉｎｃ． | インフルエンザａ型ウイルスに対して中和活性を有するヒトｂ細胞由来のヒトモノクローナル抗体 |
| JP2013526849A (ja) | 2010-03-30 | 2013-06-27 | モウント シナイ スクール オフ メディシネ | インフルエンザウイルスワクチン及びその使用 |
| CN102241768B (zh) * | 2010-05-14 | 2013-12-25 | 中国科学院上海生命科学研究院 | 一种抗甲型h1n1流感病毒血凝素蛋白的抗体 |
| JP6050747B2 (ja) * | 2010-06-17 | 2016-12-21 | トレリス バイオサイエンス リミテッド ライアビリティー カンパニー | インフルエンザ受動免疫化に有用な抗体 |
| CA2806250C (en) | 2010-07-22 | 2020-09-22 | John W. Schrader | Cross-protective pathogen protection, methods and compositions thereof |
| EP3578205A1 (en) | 2010-08-06 | 2019-12-11 | ModernaTX, Inc. | A pharmaceutical formulation comprising engineered nucleic acids and medical use thereof |
| JP2013540701A (ja) * | 2010-08-12 | 2013-11-07 | セラクローン サイエンシーズ， インコーポレイテッド | 抗赤血球凝集素抗体組成物およびその使用方法 |
| US9534042B2 (en) | 2010-09-03 | 2017-01-03 | Fujita Health University | Influenza virus-neutralizing antibody and screening method therefor |
| WO2012036993A1 (en) | 2010-09-14 | 2012-03-22 | University Of Pittsburgh-Of The Commonwealth System Of Higher Education | Computationally optimized broadly reactive antigens for influenza |
| CN103429606A (zh) | 2010-10-01 | 2013-12-04 | 现代治疗公司 | 设计核酸及其使用方法 |
| EP2663334A4 (en) * | 2011-01-10 | 2016-01-13 | Univ Emory | ANTIBODIES AGAINST INFLUENZA |
| JP2014506580A (ja) * | 2011-02-14 | 2014-03-17 | セラクローン サイエンシーズ， インコーポレイテッド | インフルエンザの治療および診断のための組成物および方法 |
| CN103649118A (zh) * | 2011-03-01 | 2014-03-19 | 安进公司 | 双特异性结合剂 |
| CA2831613A1 (en) | 2011-03-31 | 2012-10-04 | Moderna Therapeutics, Inc. | Delivery and formulation of engineered nucleic acids |
| WO2012151199A1 (en) * | 2011-05-02 | 2012-11-08 | Immunomedics, Inc. | Ultrafiltration concentration of allotype selected antibodies for small-volume administration |
| RU2612900C2 (ru) | 2011-06-20 | 2017-03-13 | Юниверсити Оф Питтсбург - Оф Зе Коммонвэлс Систем Оф Хайе Эдьюкейшн | Антигены вируса гриппа h1n1 с широким спектром активности, оптимизированные с применением вычислительных средств |
| US8961978B2 (en) * | 2011-07-14 | 2015-02-24 | Crucell Holland B.V. | Human binding molecules capable of neutralizing influenza A viruses of phylogenetic group 1 and phylogenetic group 2 and influenza B viruses |
| LT2734545T (lt) | 2011-07-18 | 2019-05-10 | Institute For Research In Biomedicine | Antikūnai, neutralizuojantys influenza a virusą, ir jų panaudojimo būdai |
| US10300140B2 (en) | 2011-07-28 | 2019-05-28 | I2 Pharmaceuticals, Inc. | Sur-binding proteins against ERBB3 |
| WO2013033319A2 (en) * | 2011-08-30 | 2013-03-07 | The Board Of Trustees Of The Leland Stanford Junior University | A cluster of neutralizing antibodies to hepatitis c virus |
| GB201115214D0 (en) | 2011-09-02 | 2011-10-19 | Health Prot Agency | Influenza virus antibody compositions |
| US9464124B2 (en) | 2011-09-12 | 2016-10-11 | Moderna Therapeutics, Inc. | Engineered nucleic acids and methods of use thereof |
| BR112014006694A2 (pt) | 2011-09-20 | 2020-11-17 | Mount Sinai School Of Medicine | vacinas contra o vírus influenza e usos dessas |
| CA2791109C (en) | 2011-09-26 | 2021-02-16 | Merus B.V. | Generation of binding molecules |
| KR20190099538A (ko) | 2011-10-03 | 2019-08-27 | 모더나 세라퓨틱스, 인코포레이티드 | 변형된 뉴클레오사이드, 뉴클레오타이드, 및 핵산, 및 이들의 용도 |
| CA2852474A1 (en) * | 2011-10-18 | 2013-04-25 | Emory University | Antibodies directed against influenza |
| WO2013079473A1 (en) | 2011-11-28 | 2013-06-06 | Crucell Holland B.V. | Influenza virus vaccines and uses thereof |
| SG11201402780UA (en) * | 2011-12-02 | 2014-10-30 | Aimm Therapeutics Bv | Influenza a virus specific antibodies |
| CN104302321A (zh) | 2011-12-05 | 2015-01-21 | 特瑞利斯生物科学有限责任公司 | 可用于被动流感免疫的抗体 |
| KR101749316B1 (ko) | 2011-12-15 | 2017-06-21 | (주) 에이프로젠 | Ｈ１ｎ１―감염된 환자들로부터 유도된 매우 잠재력 있는 넓은-스펙트럼 중화 단일클론 항체 및 이를 포함하는 바이러스의 치료용 조성물 |
| EP4144378A1 (en) | 2011-12-16 | 2023-03-08 | ModernaTX, Inc. | Modified nucleoside, nucleotide, and nucleic acid compositions |
| CA2859744A1 (en) | 2011-12-22 | 2013-06-27 | Sea Lane Biotechnologies, Llc | Surrogate binding proteins |
| RU2653756C2 (ru) | 2012-02-07 | 2018-05-14 | Юниверсити Оф Питтсбург - Оф Зе Коммонвэлс Систем Оф Хайе Эдьюкейшн | Оптимизированные с помощью компьютера антигены с широким спектром реактивности для вирусов гриппа h3n2 |
| EP3305806B1 (en) | 2012-02-13 | 2020-08-26 | University of Pittsburgh - Of the Commonwealth System of Higher Education | Computationally optimized broadly reactive antigens for human and avian h5n1 influenza |
| ES2664625T3 (es) | 2012-03-08 | 2018-04-20 | Janssen Vaccines & Prevention B.V. | Moléculas de unión humanas que pueden unirse a los virus de la influenza b y neutralizarlos, y sus usos |
| JP2015513902A (ja) | 2012-03-30 | 2015-05-18 | ユニバーシティ オブ ピッツバーグ − オブ ザ コモンウェルス システム オブ ハイヤー エデュケイション | 計算で最適化した広い反応性を示す、ｈ５ｎ１およびｈ１ｎ１インフルエンザウイルスの抗原 |
| AU2013243954A1 (en) | 2012-04-02 | 2014-10-30 | Moderna Therapeutics, Inc. | Modified polynucleotides for the production of cosmetic proteins and peptides |
| US9254311B2 (en) | 2012-04-02 | 2016-02-09 | Moderna Therapeutics, Inc. | Modified polynucleotides for the production of proteins |
| US9572897B2 (en) | 2012-04-02 | 2017-02-21 | Modernatx, Inc. | Modified polynucleotides for the production of cytoplasmic and cytoskeletal proteins |
| US9283287B2 (en) | 2012-04-02 | 2016-03-15 | Moderna Therapeutics, Inc. | Modified polynucleotides for the production of nuclear proteins |
| CA2870821C (en) | 2012-04-20 | 2022-06-14 | Merus B.V. | Methods and means for the production of ig-like molecules |
| US9969794B2 (en) | 2012-05-10 | 2018-05-15 | Visterra, Inc. | HA binding agents |
| EP2712626A1 (en) * | 2012-09-28 | 2014-04-02 | Fabentech | Passive immunisation against influenza, in particular H5N1 |
| PH12019501031A1 (en) | 2012-11-13 | 2022-11-14 | Genentech Inc | Anti-hemagglutinin antibodies and methods of use |
| DK2922554T3 (en) | 2012-11-26 | 2022-05-23 | Modernatx Inc | Terminalt modificeret rna |
| KR20150089005A (ko) | 2012-11-27 | 2015-08-04 | 유니버시티 오브 피츠버그 - 오브 더 커먼웰쓰 시스템 오브 하이어 에듀케이션 | H1n1에 대한 계산적으로 최적화되고 넓은 반응성의 항원 |
| JP2016508133A (ja) | 2012-12-18 | 2016-03-17 | アイカーン スクール オブ メディシン アット マウント サイナイ | インフルエンザウイルスワクチン及びその使用 |
| WO2014159960A1 (en) * | 2013-03-14 | 2014-10-02 | Icahn School Of Medicine At Mount Sinai | Antibodies against influenza virus hemagglutinin and uses thereof |
| EP2970397A2 (en) | 2013-03-14 | 2016-01-20 | University Of Washington Through Its Center For Commercialization | Polypeptides for treating and/or limiting influenza infection |
| US8980864B2 (en) | 2013-03-15 | 2015-03-17 | Moderna Therapeutics, Inc. | Compositions and methods of altering cholesterol levels |
| EP2982691B1 (en) | 2013-04-02 | 2020-05-06 | Xiamen University | Broad spectrum monoclonal antibody identifying ha1 structural domain of influenza virus hemagglutinin proteins |
| BR112015029635B1 (pt) | 2013-05-30 | 2023-05-02 | Janssen Vaccines & Prevention B.V | Polipeptídeo do domínio de haste da hemaglutinina da gripe e composição |
| EP3037819A4 (en) * | 2013-08-23 | 2017-03-29 | Fujita Health University | Method of determining resistance to influenza virus |
| US20160200799A1 (en) | 2013-08-23 | 2016-07-14 | Fujita Health University | Anti-influenza virus neutralizing antibody |
| US10023626B2 (en) | 2013-09-30 | 2018-07-17 | Modernatx, Inc. | Polynucleotides encoding immune modulating polypeptides |
| LT3052192T (lt) | 2013-10-02 | 2020-12-10 | Medimmune, Llc | Neutralizuojantys antikūnai prieš gripą a ir jų naudojimas |
| BR112016007255A2 (pt) | 2013-10-03 | 2017-09-12 | Moderna Therapeutics Inc | polinucleotídeos que codificam receptor de lipoproteína de baixa densidade |
| WO2015068781A1 (ja) * | 2013-11-06 | 2015-05-14 | 国立大学法人大阪大学 | インフルエンザウイルスａ型のグループ１に対して広域な中和活性を有する抗体 |
| JP6712428B2 (ja) | 2014-02-04 | 2020-06-24 | コントラフェクト コーポレイション | インフルエンザ受動免疫に有用な抗体ならびにその使用のための組成物、組合せおよび方法 |
| US10639370B2 (en) | 2014-02-04 | 2020-05-05 | Contrafect Corporation | Antibodies useful in passive influenza immunization, and compositions, combinations and methods for use thereof |
| BR112016018313A8 (pt) | 2014-02-10 | 2018-06-12 | Igm Biosciences Inc | Moléculas de ligação multiespecíficas iga |
| CA2940196C (en) | 2014-03-19 | 2023-03-07 | Wayne Marasco | Immunogenetic restriction on elicitation of antibodies |
| PT3981437T (pt) | 2014-04-23 | 2025-01-15 | Modernatx Inc | Vacinas de ácidos nucleicos |
| JP7094103B2 (ja) * | 2014-07-10 | 2022-07-01 | ヤンセン ファッシンズ アンド プリベンション ベーフェー | インフルエンザウイルスワクチンおよびその使用 |
| EP3166962B1 (en) | 2014-07-10 | 2019-08-21 | Janssen Vaccines & Prevention B.V. | Influenza virus vaccines and uses thereof |
| AU2015289805B2 (en) | 2014-07-15 | 2020-06-25 | Humabs Biomed Sa | Neutralizing anti-influenza B antibodies and uses thereof |
| TWI702229B (zh) | 2014-12-19 | 2020-08-21 | 美商再生元醫藥公司 | 流行性感冒病毒血球凝集素之人類抗體 |
| US10736956B2 (en) | 2015-01-23 | 2020-08-11 | Icahn School Of Medicine At Mount Sinai | Influenza virus vaccination regimens |
| CA2975655C (en) | 2015-02-05 | 2023-09-19 | Janssen Vaccines & Prevention B.V. | Binding molecules directed against influenza hemagglutinin and uses thereof |
| WO2016124682A1 (en) | 2015-02-05 | 2016-08-11 | Janssen Vaccines & Prevention B.V. | Human neutralizing antibodies binding to influenza neuraminidase |
| CA2985402A1 (en) | 2015-05-11 | 2016-11-17 | Janssen Vaccines & Prevention B.V. | Influenza virus neutralizing peptidomimetic compounds |
| PL3303384T3 (pl) | 2015-06-01 | 2022-01-03 | Medimmune, Llc | Neutralizujące cząsteczki wiążące przeciw grypie i ich zastosowania |
| EP3374390A1 (en) | 2015-11-13 | 2018-09-19 | Visterra, Inc. | Compositions and methods for treating and preventing influenza |
| CA3010313A1 (en) | 2016-01-13 | 2017-07-20 | Medimmune, Llc | Method of treating influenza a |
| CA3015347A1 (en) | 2016-02-24 | 2017-08-31 | Visterra, Inc. | Formulations of antibody molecules to influenza virus |
| WO2017148889A1 (en) | 2016-03-01 | 2017-09-08 | Janssen Vaccines & Prevention B.V. | Human neutralizing antibodies binding to influenza b neuraminidase |
| JP7237344B2 (ja) | 2016-06-15 | 2023-03-13 | アイカーン スクール オブ メディシン アット マウント サイナイ | インフルエンザウイルス血球凝集素タンパク質及びその使用 |
| KR101835009B1 (ko) | 2016-08-19 | 2018-03-07 | 주식회사 하이딥 | 터치 입력 장치 |
| EP3529272A2 (en) | 2016-10-21 | 2019-08-28 | Adimab, LLC | Anti-respiratory syncytial virus antibodies, and methods of their generation and use |
| EP3974447A3 (en) * | 2016-10-21 | 2022-09-07 | Adimab, LLC | Anti-respiratory syncytial virus antibodies, and methods of their generation and use |
| JP2020503844A (ja) | 2016-10-21 | 2020-02-06 | アディマブ， エルエルシー | 抗呼吸器合胞体ウイルス抗体、及び、それらの生成及び使用の方法 |
| AU2017350304B2 (en) | 2016-10-27 | 2022-03-03 | Janssen Vaccines & Prevention B.V. | Influenza virus neutralizing compounds |
| EP3574008B1 (en) | 2017-01-27 | 2023-11-08 | National Research Council of Canada | Hemagglutinin-specific antibodies and uses thereof |
| WO2018141854A1 (en) | 2017-02-02 | 2018-08-09 | Janssen Vaccines & Prevention B.V. | Piperazine derivatives for influenza virus inhibition |
| US11040963B2 (en) | 2017-02-02 | 2021-06-22 | Janssen Vaccines & Prevention B.V. | Piperazine derivatives for influenza virus inhibitions |
| JP2020506971A (ja) | 2017-02-08 | 2020-03-05 | ドラゴンフライ セラピューティクス， インコーポレイテッド | ナチュラルキラー細胞の活性化のための多重特異性結合タンパク質およびがんを処置するためのその治療的使用 |
| SG11201907646YA (en) | 2017-02-20 | 2019-09-27 | Dragonfly Therapeutics Inc | Proteins binding her2, nkg2d and cd16 |
| EP3606964A4 (en) | 2017-04-03 | 2020-12-09 | Immunomedics, Inc. | SUBCUTANE ADMINISTRATION OF ANTIBODY DRUG CONJUGATES FOR CANCER THERAPY |
| EP3606555A4 (en) | 2017-04-07 | 2021-08-04 | Icahn School of Medicine at Mount Sinai | INFLUENZA VIRUS TYPE B ANTI-NEURAMINIDASE ANTIBODIES AND THEIR USES |
| WO2019035630A2 (ko) * | 2017-08-14 | 2019-02-21 | 사회복지법인 삼성생명공익재단 | 인간 상피 성장 인자 수용체 변이체 ⅲ에 결합하는 항체 및 그의 항체 단편 |
| EP3681903B1 (en) * | 2017-09-15 | 2023-07-19 | Lentigen Technology, Inc. | Compositions and methods for treating cancer with anti-cd19 immunotherapy |
| SMT202200354T1 (it) | 2018-01-23 | 2022-09-14 | Janssen Vaccines & Prevention Bv | Vaccino per virus dell'influenza e suoi usi |
| JP7372925B2 (ja) | 2018-01-26 | 2023-11-01 | リジェネロン・ファーマシューティカルズ・インコーポレイテッド | インフルエンザヘマグルチニンに対するヒト抗体 |
| PE20210375A1 (es) | 2018-02-08 | 2021-03-02 | Dragonfly Therapeutics Inc | Terapia de combinacion del cancer que incluye proteinas de union multiespecificas que activan a las celulas asesinas naturales |
| FI3749346T3 (fi) | 2018-02-08 | 2024-09-04 | Dragonfly Therapeutics Inc | Nkg2d-reseptoriin kohdistuvat vasta-aineen vaihtelevan domeenin yhdistelmät |
| MX2020008684A (es) | 2018-02-20 | 2020-12-07 | Dragonfly Therapeutics Inc | Proteinas de union multiespecificas que se unen a cd33, nkg2d y cd16 y metodos de uso. |
| WO2019246363A1 (en) | 2018-06-21 | 2019-12-26 | Icahn School Of Medicine At Mount Sinai | Mosaic influenza virus hemagglutinin polypeptides and uses thereof |
| US12384851B2 (en) | 2018-08-08 | 2025-08-12 | Dragonfly Therapeutics, Inc. | Multi-specific binding proteins that bind BCMA, NKG2D and CD16, and methods of use |
| EA202091888A1 (ru) | 2018-08-08 | 2020-10-23 | Драгонфлай Терапьютикс, Инк. | Вариабельные домены антител, нацеленные на рецептор nkg2d |
| JP7482363B2 (ja) | 2018-08-08 | 2024-05-14 | ドラゴンフライ セラピューティクス， インコーポレイテッド | Ｎｋｇ２ｄ、ｃｄ１６及び腫瘍関連抗原に結合するタンパク質 |
| CN111057718A (zh) * | 2018-10-17 | 2020-04-24 | 南京大学 | 一种稳定表达绿色荧光蛋白的egfp-sp2/0细胞株及其构建方法 |
| KR102113302B1 (ko) * | 2018-12-24 | 2020-05-20 | 원광대학교산학협력단 | 상보성결정부 기반 조류 인플루엔자 바이러스의 h5 아형에 특이적으로 결합하는 펩티드 및 이의 용도 |
| EP3946613A1 (en) | 2019-03-25 | 2022-02-09 | Visterra, Inc. | Compositions and methods for treating and preventing influenza |
| CA3152957A1 (en) | 2019-09-05 | 2021-03-11 | Janssen Vaccines & Prevention B.V. | Influenza virus vaccines and uses thereof |
| WO2021173965A1 (en) | 2020-02-28 | 2021-09-02 | Massachusetts Institute Of Technology | Identification of variable influenza residues and uses thereof |
| CN111440228B (zh) * | 2020-03-09 | 2021-08-24 | 扬州大学 | 多种亚型流感病毒ha2蛋白共同抗原表位、抗体、鉴定方法和应用 |
| WO2021201677A1 (en) | 2020-04-01 | 2021-10-07 | Kiadis Pharma Intellectual Property B.V. | Compositions and methods targeting influenza |
| US20210325367A1 (en) * | 2020-04-20 | 2021-10-21 | Satish Mahna | Controlled Exposure to Pathogens for Generating Immunity |
| TW202208428A (zh) | 2020-05-06 | 2022-03-01 | 美商蜻蜓醫療公司 | 結合ｎｋｇ２ｄ、ｃｄ１６及ｃｌｅｃ１２ａ之蛋白質 |
| CN116761605A (zh) * | 2021-02-04 | 2023-09-15 | 四川海思科制药有限公司 | Ha抑制剂化合物的盐及晶型 |
| EP4301774A4 (en) | 2021-03-03 | 2025-08-13 | Dragonfly Therapeutics Inc | METHODS OF TREATING CANCER USING MULTI-SPECIFIC BINDING PROTEINS THAT BIND TO NKG2D, CD16, AND A TUMOR-ASSOCIATED ANTIGEN |
| TW202309075A (zh) * | 2021-04-30 | 2023-03-01 | 美商亞得捷歐治療公司 | 對冠狀病毒s蛋白質具特異性之化合物及其用途 |
| WO2024104947A2 (en) | 2022-11-14 | 2024-05-23 | Janssen Vaccines & Prevention B.V. | Influenza b virus vaccines and uses thereof |
| WO2025019631A1 (en) | 2023-07-19 | 2025-01-23 | Icahn School Of Medicine At Mount Sinai | Immunogenic compositions containing inactivated influenza a virus and cpg oligonucleotide adjuvant and uses thereof |
| US20250090650A1 (en) | 2023-09-06 | 2025-03-20 | Sanofi | Modified influenza b hemagglutinin polypeptides and nucleic acids and uses thereof |
| WO2025090499A1 (en) * | 2023-10-24 | 2025-05-01 | University Of Pittsburgh - Of The Commonwealth System Of Higher Education | Monoclonal antibodies that bind an antigen of epithelial ovarian cancer and their use |
| WO2025149667A1 (en) | 2024-01-12 | 2025-07-17 | Pheon Therapeutics Ltd | Antibody drug conjugates and uses thereof |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5631350A (en) * | 1992-09-17 | 1997-05-20 | Takara Shuzo Co., Ltd. | Anti-human influenza virus antibody |
Family Cites Families (42)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4625015A (en) | 1982-08-23 | 1986-11-25 | Scripps Clinic & Research Foundation | Broad spectrum influenza antisera |
| ZA836080B (en) * | 1982-08-23 | 1984-04-25 | Scripps Clinic Res | Broad spectrum influenza antisera |
| NZ207394A (en) | 1983-03-08 | 1987-03-06 | Commw Serum Lab Commission | Detecting or determining sequence of amino acids |
| NL9101953A (nl) | 1991-11-21 | 1993-06-16 | Seed Capital Investments | Testinrichting omvattende een plaat met een veelvoud van putjes met een bijbehorende doseerinrichting, alsmede een kit die deze inrichtingen omvat en toepassing van de inrichtingen. |
| JP3037554B2 (ja) * | 1993-04-20 | 2000-04-24 | 寳酒造株式会社 | 免疫原性人工ポリペプチド |
| JP3061960B2 (ja) * | 1992-09-17 | 2000-07-10 | 寳酒造株式会社 | 抗ヒトインフルエンザウイルス抗体 |
| US5624949A (en) | 1993-12-07 | 1997-04-29 | Eli Lilly And Company | Protein kinase C inhibitors |
| JP3584990B2 (ja) * | 1994-05-09 | 2004-11-04 | タカラバイオ株式会社 | 抗ヒトインフルエンザウイルス抗体 |
| US6265150B1 (en) | 1995-06-07 | 2001-07-24 | Becton Dickinson & Company | Phage antibodies |
| CA2267139A1 (en) | 1996-10-08 | 1998-04-16 | Ton Logtenberg | Methods and means for selecting peptides and proteins having specific affinity for a target |
| US20030161813A1 (en) | 1998-04-30 | 2003-08-28 | Ton Logtenberg | Altering the properties of cells or of particles with membranes derived from cells by means of lipid-modified proteinaceous molecules |
| US6440736B1 (en) | 1998-10-16 | 2002-08-27 | U-Bisys B.V. | Altering the properties of cells or of particles with membranes derived from cells by means of lipid-modified proteinaceous molecules |
| US7091324B2 (en) * | 1998-11-05 | 2006-08-15 | Board Of Trustees Of Leland Stanford Junior University | Prevention and treatment of HCV infection employing antibodies directed against conformational epitopes |
| WO2000063403A2 (en) | 1999-04-15 | 2000-10-26 | Crucell Holland B.V. | Recombinant protein production in a human cell using sequences encoding adenovirus e1 protein |
| US7521220B2 (en) | 1999-11-26 | 2009-04-21 | Crucell Holland B.V. | Production of vaccines |
| EP1224943A1 (en) | 2001-01-19 | 2002-07-24 | Crucell Holland B.V. | Fibronectin as a tumor marker detected by phage antibodies |
| DK1402025T3 (da) | 2001-06-15 | 2006-06-06 | Crucell Holland Bv | Kimære fager |
| US7070926B2 (en) | 2001-06-15 | 2006-07-04 | Crucell Holland B.V. | Chimaeric phages |
| WO2003086458A1 (en) * | 2002-04-12 | 2003-10-23 | Medimmune, Inc. | Recombinant anti-interleukin-9 antibodies |
| US20100069614A1 (en) | 2008-06-27 | 2010-03-18 | Merus B.V. | Antibody producing non-human mammals |
| WO2005012337A2 (en) | 2003-07-15 | 2005-02-10 | Crucell Holland B.V. | Antigenic peptides of sars coronavirus and uses thereof |
| KR101206206B1 (ko) | 2003-07-22 | 2012-11-29 | 크루셀 홀란드 비.브이. | 사스-코로나바이러스에 대한 결합분자 및 그것의 용도 |
| ES2378767T3 (es) | 2003-12-23 | 2012-04-17 | Crucell Holland B.V. | Molécula de unión humana contra CD1a |
| WO2005111623A1 (en) | 2004-05-17 | 2005-11-24 | Crucell Holland B.V. | Methods for diagnosis of acute myeloid leukemia |
| CN102139106B (zh) | 2004-05-27 | 2014-10-08 | 克鲁塞尔荷兰公司 | 能中和狂犬病病毒的结合分子及其应用 |
| JP4852046B2 (ja) | 2004-10-12 | 2012-01-11 | クルセル ホランド ベー ヴェー | 癌の治療及び検出に用いる結合分子 |
| ATE550037T1 (de) | 2004-11-11 | 2012-04-15 | Crucell Holland Bv | Zusammensetzungen gegen das sars-coronavirus und ihre verwendungen |
| CA2591665C (en) | 2004-12-20 | 2015-05-05 | Crucell Holland B.V. | Binding molecules capable of neutralizing west nile virus and uses thereof |
| JP4580338B2 (ja) | 2004-12-23 | 2010-11-10 | エーエスエムエル ネザーランズ ビー．ブイ． | リソグラフィ装置、エキシマ・レーザ、およびデバイス製造方法 |
| WO2006120230A2 (en) | 2005-05-12 | 2006-11-16 | Crucell Holland B.V. | Host cell specific binding molecules capable of neutralizing viruses and uses thereof |
| JP4758148B2 (ja) * | 2005-06-14 | 2011-08-24 | 泰三 宇田 | インフルエンザウイルスのヘマグルチニンに対する抗体酵素 |
| EP1893645A1 (en) | 2005-06-23 | 2008-03-05 | Crucell Holland B.V. | Optimization of west nile virus antibodies |
| KR101274790B1 (ko) | 2005-07-22 | 2013-06-13 | 크루셀 홀란드 비.브이. | 코로나바이러스 생산용 세포주 |
| WO2007031550A2 (en) | 2005-09-15 | 2007-03-22 | Crucell Holland B.V. | Method for preparing immunoglobulin libraries |
| JP5586952B2 (ja) | 2006-06-06 | 2014-09-10 | クルセル ホランド ベー ヴェー | 腸球菌に対する殺活性を有するヒトの結合分子及びその使用方法 |
| EP3018142A1 (en) | 2006-06-06 | 2016-05-11 | Crucell Holland B.V. | Human binding molecules having killing activity against staphylococci and uses thereof |
| MY170607A (en) | 2006-09-07 | 2019-08-20 | Crucell Holland Bv | Human binding molecules capable of neutralizing influenza virus h5n1 and uses thereof |
| US8802089B2 (en) | 2008-01-03 | 2014-08-12 | Genmab A/S | Monoclonal antibodies against CD32B |
| US8148797B2 (en) | 2008-06-26 | 2012-04-03 | Taiwan Semiconductor Manufacturing Co., Ltd. | Chip pad resistant to antenna effect and method |
| US8470327B2 (en) | 2009-05-11 | 2013-06-25 | Crucell Holland B.V. | Human binding molecules capable of neutralizing influenza virus H3N2 and uses thereof |
| CA2791109C (en) | 2011-09-26 | 2021-02-16 | Merus B.V. | Generation of binding molecules |
| CA2870821C (en) | 2012-04-20 | 2022-06-14 | Merus B.V. | Methods and means for the production of ig-like molecules |
-
2007
- 2007-09-06 MY MYPI2013000314A patent/MY170607A/en unknown
- 2007-09-06 WO PCT/EP2007/059356 patent/WO2008028946A2/en not_active Ceased
- 2007-09-06 US US12/310,812 patent/US8192927B2/en active Active
- 2007-09-06 CA CA2663388A patent/CA2663388C/en active Active
- 2007-09-06 EP EP20120153010 patent/EP2450377A1/en not_active Withdrawn
- 2007-09-06 AU AU2007293662A patent/AU2007293662B2/en not_active Ceased
- 2007-09-06 KR KR20097005413A patent/KR101485197B1/ko not_active Expired - Fee Related
- 2007-09-06 JP JP2009527144A patent/JP5161882B2/ja active Active
- 2007-09-06 PL PL07803310T patent/PL2059532T3/pl unknown
- 2007-09-06 MX MX2009002174A patent/MX2009002174A/es active IP Right Grant
- 2007-09-06 HR HRP20130163TT patent/HRP20130163T1/hr unknown
- 2007-09-06 EP EP07803310A patent/EP2059532B1/en active Active
- 2007-09-06 EA EA200970255A patent/EA017203B1/ru unknown
-
2009
- 2009-02-18 ZA ZA2009/01171A patent/ZA200901171B/en unknown
- 2009-03-03 IL IL197390A patent/IL197390A/en active IP Right Grant
- 2009-03-31 NO NO20091321A patent/NO20091321L/no not_active Application Discontinuation
-
2011
- 2011-12-09 US US13/315,475 patent/US8691223B2/en active Active
-
2012
- 2012-04-27 US US13/458,964 patent/US9011848B2/en active Active
- 2012-08-13 JP JP2012179593A patent/JP5701827B2/ja active Active
-
2013
- 2013-10-01 US US14/043,677 patent/US9109017B2/en active Active
-
2015
- 2015-08-04 US US14/817,707 patent/US10005831B2/en active Active
-
2016
- 2016-11-29 IL IL249291A patent/IL249291B/en active IP Right Grant
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5631350A (en) * | 1992-09-17 | 1997-05-20 | Takara Shuzo Co., Ltd. | Anti-human influenza virus antibody |
Non-Patent Citations (3)
| Title |
|---|
| HORIMOTO T. et al., "Antigenic differences between H5N1 human influenza viruses isolated in 1997 and 2003", J. Vet. Med. Sci., 2004 Mar; 66 (3) 303-5, referat [naydeno 07.09.2009]. Naydeno iz PubMed. PM1D: 15107562 * |
| OKUNO Y., et al., "A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains", Journal of Virology, May 1993, 67(5), p. 2552-2558 * |
| SMIRNOV Y.A. et al., "An epitope shared by the hemagglutinins of H1, H2, H5, and H6 subtypes of influenza A virus", Acta Virol, 1999 Aug; 43(4):237-44, referat [naydeno 07.09.2009]. Naydeno iz PubMed. PMID: 10749369 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2701694C2 (ru) * | 2013-03-14 | 2019-09-30 | Контрафект Корпорейшн | Композиции и способы, основанные на нейтрализующих антителах, доставляемых интраназально, для улучшенной терапевтической эффективности |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EA017203B1 (ru) | Связывающие молекулы человека, способные нейтрализовать вирус гриппа h5n1, и их применение | |
| US10851155B2 (en) | Middle east respiratory syndrome coronavirus neutralizing antibodies and methods of use thereof | |
| TWI589300B (zh) | 中和流感病毒ｈ３ｎ２之人類結合分子及其用途 | |
| US9005621B2 (en) | Human binding molecules capable of binding to and neutralizing influenza B viruses and uses thereof | |
| CA3081694C (en) | Monoclonal antibodies for ebola and marburg viruses | |
| JP2023130499A (ja) | ヒト化インフルエンザモノクローナル抗体およびその使用方法 | |
| EA027054B1 (ru) | Связывающие молекулы человека, способные нейтрализовать вирусы гриппа a филогенетической группы 1 и филогенетической группы 2 и вирусы гриппа b | |
| EA010785B1 (ru) | Связывающие молекулы, способные нейтрализовать вирус бешенства, и их применение | |
| RS52688B (sr) | Humani vezni molekuli sposobni da neutrališu virus influence h5n1 i njihova upotreba | |
| HK1200176B (en) | Human binding molecules capable of binding to and neutralizing influenza b viruses and uses thereof |