CN102471765B - 显示出缩短的生物学活性的神经毒素 - Google Patents
显示出缩短的生物学活性的神经毒素 Download PDFInfo
- Publication number
- CN102471765B CN102471765B CN201080027593.0A CN201080027593A CN102471765B CN 102471765 B CN102471765 B CN 102471765B CN 201080027593 A CN201080027593 A CN 201080027593A CN 102471765 B CN102471765 B CN 102471765B
- Authority
- CN
- China
- Prior art keywords
- polypeptide
- polynucleotides
- medicine
- present
- polynucleotide encoding
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Fee Related
Links
- 238000004904 shortening Methods 0.000 title claims description 4
- 239000002581 neurotoxin Substances 0.000 title description 27
- 231100000618 neurotoxin Toxicity 0.000 title description 27
- 101710138657 Neurotoxin Proteins 0.000 title description 25
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 66
- 229920001184 polypeptide Polymers 0.000 claims abstract description 59
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 59
- 108091033319 polynucleotide Proteins 0.000 claims abstract description 55
- 102000040430 polynucleotide Human genes 0.000 claims abstract description 55
- 239000002157 polynucleotide Substances 0.000 claims abstract description 55
- 239000003814 drug Substances 0.000 claims abstract description 43
- 101000795849 Calliactis parasitica Delta-hormotoxin-Cpt1b Proteins 0.000 claims abstract description 42
- 238000000034 method Methods 0.000 claims abstract description 21
- 238000011282 treatment Methods 0.000 claims abstract description 21
- 230000004071 biological effect Effects 0.000 claims abstract description 16
- 239000002773 nucleotide Substances 0.000 claims description 15
- 125000003729 nucleotide group Chemical group 0.000 claims description 15
- 238000002360 preparation method Methods 0.000 claims description 12
- 230000000694 effects Effects 0.000 claims description 9
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 8
- 230000001580 bacterial effect Effects 0.000 claims description 5
- 210000003205 muscle Anatomy 0.000 claims description 5
- 241000607479 Yersinia pestis Species 0.000 claims description 4
- 230000029663 wound healing Effects 0.000 claims description 4
- 208000002874 Acne Vulgaris Diseases 0.000 claims description 3
- 241000588724 Escherichia coli Species 0.000 claims description 3
- 102000006275 Ubiquitin-Protein Ligases Human genes 0.000 claims description 3
- 108010083111 Ubiquitin-Protein Ligases Proteins 0.000 claims description 3
- 206010000496 acne Diseases 0.000 claims description 3
- 210000000988 bone and bone Anatomy 0.000 claims description 3
- 239000004053 dental implant Substances 0.000 claims description 3
- 238000011540 hip replacement Methods 0.000 claims description 3
- 241000193830 Bacillus <bacterium> Species 0.000 claims description 2
- 210000000629 knee joint Anatomy 0.000 claims description 2
- 206010022998 Irritability Diseases 0.000 claims 1
- 230000000593 degrading effect Effects 0.000 claims 1
- 210000000936 intestine Anatomy 0.000 claims 1
- 229940079593 drug Drugs 0.000 abstract description 5
- 238000004519 manufacturing process Methods 0.000 abstract description 2
- 210000004027 cell Anatomy 0.000 description 34
- 239000000203 mixture Substances 0.000 description 16
- 150000001413 amino acids Chemical group 0.000 description 12
- 150000001875 compounds Chemical class 0.000 description 10
- 238000005516 engineering process Methods 0.000 description 10
- 108090000623 proteins and genes Proteins 0.000 description 10
- 102000004169 proteins and genes Human genes 0.000 description 10
- 101710117542 Botulinum neurotoxin type A Proteins 0.000 description 9
- 239000002537 cosmetic Substances 0.000 description 8
- 238000005520 cutting process Methods 0.000 description 8
- 108010055044 Tetanus Toxin Proteins 0.000 description 7
- 201000010099 disease Diseases 0.000 description 7
- 239000012634 fragment Substances 0.000 description 7
- 230000017854 proteolysis Effects 0.000 description 7
- 229940118376 tetanus toxin Drugs 0.000 description 7
- 101710117515 Botulinum neurotoxin type E Proteins 0.000 description 6
- 239000003053 toxin Substances 0.000 description 6
- 231100000765 toxin Toxicity 0.000 description 6
- 108030001720 Bontoxilysin Proteins 0.000 description 5
- 101000985023 Clostridium botulinum C phage Botulinum neurotoxin type C Proteins 0.000 description 5
- 241000700605 Viruses Species 0.000 description 5
- 210000005036 nerve Anatomy 0.000 description 5
- 239000008194 pharmaceutical composition Substances 0.000 description 5
- 230000001105 regulatory effect Effects 0.000 description 5
- 101710117524 Botulinum neurotoxin type B Proteins 0.000 description 4
- 101710117520 Botulinum neurotoxin type F Proteins 0.000 description 4
- 101000933563 Clostridium botulinum Botulinum neurotoxin type G Proteins 0.000 description 4
- 101000985020 Clostridium botulinum D phage Botulinum neurotoxin type D Proteins 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 239000003795 chemical substances by application Substances 0.000 description 4
- 239000013604 expression vector Substances 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 238000001556 precipitation Methods 0.000 description 4
- 241000193155 Clostridium botulinum Species 0.000 description 3
- 108020004414 DNA Proteins 0.000 description 3
- 206010033799 Paralysis Diseases 0.000 description 3
- 239000000427 antigen Substances 0.000 description 3
- 102000036639 antigens Human genes 0.000 description 3
- 108091007433 antigens Proteins 0.000 description 3
- 230000006652 catabolic pathway Effects 0.000 description 3
- 239000003085 diluting agent Substances 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- 230000003387 muscular Effects 0.000 description 3
- 239000003381 stabilizer Substances 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 239000013598 vector Substances 0.000 description 3
- 241001112695 Clostridiales Species 0.000 description 2
- 241000193403 Clostridium Species 0.000 description 2
- 241000193449 Clostridium tetani Species 0.000 description 2
- 241000605909 Fusobacterium Species 0.000 description 2
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 102000007474 Multiprotein Complexes Human genes 0.000 description 2
- 108010085220 Multiprotein Complexes Proteins 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 101710118538 Protease Proteins 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- 206010044684 Trismus Diseases 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 238000001647 drug administration Methods 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 230000002163 immunogen Effects 0.000 description 2
- 230000002779 inactivation Effects 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- 208000028774 intestinal disease Diseases 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 230000002045 lasting effect Effects 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 239000013600 plasmid vector Substances 0.000 description 2
- 231100000614 poison Toxicity 0.000 description 2
- 239000002574 poison Substances 0.000 description 2
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 2
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 2
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- FGDZQCVHDSGLHJ-UHFFFAOYSA-M rubidium chloride Chemical compound [Cl-].[Rb+] FGDZQCVHDSGLHJ-UHFFFAOYSA-M 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 238000002864 sequence alignment Methods 0.000 description 2
- 230000035939 shock Effects 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 208000024891 symptom Diseases 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 230000005026 transcription initiation Effects 0.000 description 2
- 241001430294 unidentified retrovirus Species 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- KIUKXJAPPMFGSW-DNGZLQJQSA-N (2S,3S,4S,5R,6R)-6-[(2S,3R,4R,5S,6R)-3-Acetamido-2-[(2S,3S,4R,5R,6R)-6-[(2R,3R,4R,5S,6R)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-2-carboxy-4,5-dihydroxyoxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylic acid Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 KIUKXJAPPMFGSW-DNGZLQJQSA-N 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 101100107610 Arabidopsis thaliana ABCF4 gene Proteins 0.000 description 1
- 241001076939 Artines Species 0.000 description 1
- 241000194107 Bacillus megaterium Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 208000003508 Botulism Diseases 0.000 description 1
- 241000701822 Bovine papillomavirus Species 0.000 description 1
- 241000219357 Cactaceae Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 101100382092 Clostridium botulinum D phage ntnha gene Proteins 0.000 description 1
- 101100004794 Clostridium botulinum ant gene Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 206010010904 Convulsion Diseases 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 241000702421 Dependoparvovirus Species 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241000192125 Firmicutes Species 0.000 description 1
- 208000018522 Gastrointestinal disease Diseases 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 241000175212 Herpesvirales Species 0.000 description 1
- 101000761717 Hydrophis lapemoides Short neurotoxin 1 Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 108091026898 Leader sequence (mRNA) Proteins 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 101000800747 Ophiophagus hannah Long neurotoxin 1 Proteins 0.000 description 1
- 102000052812 Ornithine decarboxylases Human genes 0.000 description 1
- 108700005126 Ornithine decarboxylases Proteins 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 241000714474 Rous sarcoma virus Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 101100068078 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GCN4 gene Proteins 0.000 description 1
- 101100174184 Serratia marcescens fosA gene Proteins 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 208000005392 Spasm Diseases 0.000 description 1
- 235000021355 Stearic acid Nutrition 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- 206010043376 Tetanus Diseases 0.000 description 1
- 108091036066 Three prime untranslated region Proteins 0.000 description 1
- 241000838698 Togo Species 0.000 description 1
- 108010057266 Type A Botulinum Toxins Proteins 0.000 description 1
- 102000044159 Ubiquitin Human genes 0.000 description 1
- 108090000848 Ubiquitin Proteins 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- 108010079650 abobotulinumtoxinA Proteins 0.000 description 1
- 235000010489 acacia gum Nutrition 0.000 description 1
- 239000001785 acacia senegal l. willd gum Substances 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 235000010419 agar Nutrition 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 150000001336 alkenes Chemical class 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 210000004507 artificial chromosome Anatomy 0.000 description 1
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 230000003796 beauty Effects 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 206010005159 blepharospasm Diseases 0.000 description 1
- 230000000744 blepharospasm Effects 0.000 description 1
- 229940089093 botox Drugs 0.000 description 1
- 239000000872 buffer Substances 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
- PASHVRUKOFIRIK-UHFFFAOYSA-L calcium sulfate dihydrate Chemical compound O.O.[Ca+2].[O-]S([O-])(=O)=O PASHVRUKOFIRIK-UHFFFAOYSA-L 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000008602 contraction Effects 0.000 description 1
- 230000036461 convulsion Effects 0.000 description 1
- 238000005336 cracking Methods 0.000 description 1
- 238000005034 decoration Methods 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 208000010643 digestive system disease Diseases 0.000 description 1
- 230000008034 disappearance Effects 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 229940098753 dysport Drugs 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 210000001163 endosome Anatomy 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 230000028023 exocytosis Effects 0.000 description 1
- 210000000744 eyelid Anatomy 0.000 description 1
- 101150078861 fos gene Proteins 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 208000018685 gastrointestinal system disease Diseases 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000001415 gene therapy Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 210000004907 gland Anatomy 0.000 description 1
- 235000011187 glycerol Nutrition 0.000 description 1
- 238000009499 grossing Methods 0.000 description 1
- -1 hnRNA Proteins 0.000 description 1
- 229920002674 hyaluronan Polymers 0.000 description 1
- 229960003160 hyaluronic acid Drugs 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000005462 in vivo assay Methods 0.000 description 1
- 108010024001 incobotulinumtoxinA Proteins 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 210000003127 knee Anatomy 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 231100000636 lethal dose Toxicity 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 210000003712 lysosome Anatomy 0.000 description 1
- 230000001868 lysosomic effect Effects 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 230000004118 muscle contraction Effects 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 230000001537 neural effect Effects 0.000 description 1
- 210000002569 neuron Anatomy 0.000 description 1
- 231100000189 neurotoxic Toxicity 0.000 description 1
- 230000002887 neurotoxic effect Effects 0.000 description 1
- 239000002858 neurotransmitter agent Substances 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- QIQXTHQIDYTFRH-UHFFFAOYSA-N octadecanoic acid Chemical compound CCCCCCCCCCCCCCCCCC(O)=O QIQXTHQIDYTFRH-UHFFFAOYSA-N 0.000 description 1
- OQCDKBAXFALNLD-UHFFFAOYSA-N octadecanoic acid Natural products CCCCCCCC(C)CCCCCCCCC(O)=O OQCDKBAXFALNLD-UHFFFAOYSA-N 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 239000001814 pectin Substances 0.000 description 1
- 235000010987 pectin Nutrition 0.000 description 1
- 229920001277 pectin Polymers 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000007319 proteasomal degradation pathway Effects 0.000 description 1
- 230000006916 protein interaction Effects 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- 230000001177 retroviral effect Effects 0.000 description 1
- 229940102127 rubidium chloride Drugs 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 210000004988 splenocyte Anatomy 0.000 description 1
- 238000000528 statistical test Methods 0.000 description 1
- 239000008117 stearic acid Substances 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 210000002504 synaptic vesicle Anatomy 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 235000012222 talc Nutrition 0.000 description 1
- 239000000454 talc Substances 0.000 description 1
- 229910052623 talc Inorganic materials 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 231100001274 therapeutic index Toxicity 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000005945 translocation Effects 0.000 description 1
- 230000017105 transposition Effects 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
- 241001515965 unidentified phage Species 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- 230000037303 wrinkles Effects 0.000 description 1
- 229940018272 xeomin Drugs 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
- A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
- A61K38/4886—Metalloendopeptidases (3.4.24), e.g. collagenase
- A61K38/4893—Botulinum neurotoxin (3.4.24.69)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/164—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
-
- 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
- A61K39/02—Bacterial antigens
- A61K39/08—Clostridium, e.g. Clostridium tetani
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/02—Stomatological preparations, e.g. drugs for caries, aphtae, periodontitis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/04—Drugs for disorders of the alimentary tract or the digestive system for ulcers, gastritis or reflux esophagitis, e.g. antacids, inhibitors of acid secretion, mucosal protectants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/10—Anti-acne agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/04—Drugs for skeletal disorders for non-specific disorders of the connective tissue
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P41/00—Drugs used in surgical methods, e.g. surgery adjuvants for preventing adhesion or for vitreum substitution
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/14—Vasoprotectives; Antihaemorrhoidals; Drugs for varicose therapy; Capillary stabilisers
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/33—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Clostridium (G)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1267—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria
- C07K16/1282—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria from Clostridium (G)
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/24—Metalloendopeptidases (3.4.24)
- C12Y304/24069—Bontoxilysin (3.4.24.69), i.e. botulinum neurotoxin
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
- A61Q19/08—Anti-ageing preparations
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/95—Fusion polypeptide containing a motif/fusion for degradation (ubiquitin fusions, PEST sequence)
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Genetics & Genomics (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Biochemistry (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Epidemiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Dermatology (AREA)
- Physical Education & Sports Medicine (AREA)
- Mycology (AREA)
- Birds (AREA)
- Toxicology (AREA)
- Rheumatology (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Heart & Thoracic Surgery (AREA)
- Vascular Medicine (AREA)
Abstract
Description
Claims (13)
Applications Claiming Priority (5)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US27019809P | 2009-07-02 | 2009-07-02 | |
EP09164365 | 2009-07-02 | ||
US61/270,198 | 2009-07-02 | ||
EP09164365.0 | 2009-07-02 | ||
PCT/EP2010/059398 WO2011000929A1 (en) | 2009-07-02 | 2010-07-01 | Neurotoxins exhibiting shortened biological activity |
Publications (3)
Publication Number | Publication Date |
---|---|
CN102471765A CN102471765A (zh) | 2012-05-23 |
CN102471765B true CN102471765B (zh) | 2016-05-11 |
CN102471765B9 CN102471765B9 (zh) | 2016-07-27 |
Family
ID=40911088
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN201080027593.0A Expired - Fee Related CN102471765B9 (zh) | 2009-07-02 | 2010-07-01 | 显示出缩短的生物学活性的神经毒素 |
Country Status (15)
Country | Link |
---|---|
US (4) | US8586329B2 (zh) |
EP (1) | EP2449101B1 (zh) |
JP (2) | JP6059986B2 (zh) |
KR (2) | KR20120104140A (zh) |
CN (1) | CN102471765B9 (zh) |
AU (1) | AU2010267963B2 (zh) |
BR (1) | BRPI1014253A2 (zh) |
CA (1) | CA2763692A1 (zh) |
ES (1) | ES2693705T3 (zh) |
HK (1) | HK1171246A1 (zh) |
IL (1) | IL216414A (zh) |
IN (1) | IN2012DN00733A (zh) |
MX (2) | MX2011013014A (zh) |
RU (1) | RU2582266C2 (zh) |
WO (1) | WO2011000929A1 (zh) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN111629762A (zh) * | 2018-03-20 | 2020-09-04 | 美国醣基生医股份有限公司 | 结合至ssea4的嵌合抗原受体及其用途 |
Families Citing this family (44)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE19925739A1 (de) * | 1999-06-07 | 2000-12-21 | Biotecon Ges Fuer Biotechnologische Entwicklung & Consulting Mbh | Therapeutikum mit einem Botulinum-Neurotoxin |
AR061669A1 (es) * | 2006-06-29 | 2008-09-10 | Merz Pharma Gmbh & Co Kgaa | Aplicacion de alta frecuencia de terapia con toxina botulinica |
WO2012125652A2 (en) * | 2011-03-14 | 2012-09-20 | University Of Southern California | Antibody and antibody mimetic for visualization and ablation of endogenous proteins |
RU2646110C2 (ru) * | 2011-11-09 | 2018-03-01 | Мерц Фарма Гмбх Унд Ко. Кгаа | Нейротоксины, проявляющие укороченную биологическую активность |
CA2881898A1 (en) | 2012-08-20 | 2014-02-27 | Merz Pharma Gmbh & Co. Kgaa | Novel method for the manufacturing of recombinant proteins harbouring an n-terminal lysine |
AP2015008328A0 (en) | 2012-10-16 | 2015-03-31 | Almirall Sa | Pyrrolotriazinone derivatives as pi3k inhibitors |
WO2014079495A1 (en) | 2012-11-21 | 2014-05-30 | Syntaxin Limited | Methods for the manufacture of proteolytically processed polypeptides |
EP2952205B1 (en) | 2014-06-06 | 2017-08-09 | Kleiner-Fisman, Galit | Botulinum toxin for use in the treatment of paratonia |
EP3154562A1 (en) * | 2014-06-13 | 2017-04-19 | Merz Pharma GmbH & Co. KGaA | Novel uses of recombinant clostridial neurotoxins with decreased duration of effect |
EP3154572A1 (en) * | 2014-06-13 | 2017-04-19 | Merz Pharma GmbH & Co. KGaA | Novel uses of recombinant clostridial neurotoxins with decreased duration of effect |
US20170189500A1 (en) | 2014-06-13 | 2017-07-06 | Merz Pharma Gmbh & Co. Kgaa | Use of recombinant clostridial neurotoxins for the treatment of patients having certain muscle-related disorders |
WO2015188945A1 (en) | 2014-06-13 | 2015-12-17 | Merz Pharma Gmbh & Co. Kgaa | Novel uses of recombinant clostridial neurotoxins with decreased duration of effect |
SG11201705019PA (en) | 2014-12-23 | 2017-07-28 | Merz Pharma Gmbh & Co Kgaa | Botulinum toxin prefilled container |
RU2733493C2 (ru) | 2015-01-09 | 2020-10-02 | Ипсен Байоинновейшн Лимитед | Катионные нейротоксины |
US20180327779A1 (en) * | 2015-03-03 | 2018-11-15 | Fondazione Telethon (IT/IT) | Multiple vector system and uses thereof |
WO2016168740A2 (en) * | 2015-04-16 | 2016-10-20 | Spencer Juliet V | Detection of human cytomegalovirus in breast cancer |
TW201718627A (zh) | 2015-06-11 | 2017-06-01 | 梅茲製藥有限兩合公司 | 重組梭菌神經毒素及其使用與形成方法、包括其之醫藥組合物及對應其之前驅物、編碼前驅物之核酸序列及其獲得方法與前驅物之形成方法、載體與包括核酸序列之重組宿主細胞 |
KR101793328B1 (ko) * | 2015-07-03 | 2017-11-03 | 씨제이제일제당 (주) | L-라이신 생산능을 갖는 미생물 및 이를 이용한 l-라이신 생산 방법 |
WO2017063743A1 (en) | 2015-10-14 | 2017-04-20 | Merz Pharma Gmbh & Co. Kgaa | Improvements to ultrasound-based therapy of photoaged tissue |
BR112018014445A2 (pt) | 2016-03-02 | 2018-12-11 | Merz Pharma Gmbh & Co Kgaa | composição que compreende toxina botulínica |
JP6381093B2 (ja) * | 2016-06-02 | 2018-08-29 | 学校法人藤田学園 | 卵アレルギーの抗原 |
TWI737742B (zh) | 2016-06-22 | 2021-09-01 | 德商梅茲製藥有限兩合公司 | 肉毒桿菌毒素的預填充式注射器系統、具有其之套組以及其之使用 |
EP3290437A1 (en) | 2016-08-31 | 2018-03-07 | Merz Pharma GmbH & Co. KGaA | Novel recombinant clostridial neurotoxins with decreased duration of effect |
EP3312193A1 (en) | 2016-10-19 | 2018-04-25 | Merz Pharma GmbH & Co. KGaA | Novel recombinant botulinum neurotoxins with accelerated onset of effect |
MY191843A (en) * | 2016-11-28 | 2022-07-18 | C Lecta Gmbh | Trehalose phosphorylase |
WO2018233813A1 (en) | 2017-06-20 | 2018-12-27 | Merz Pharma Gmbh & Co. Kgaa | NOVEL RECOMBINANT BOTULINUM TOXINS WITH INCREASED DURATION |
EP3649143B1 (en) | 2017-07-06 | 2022-08-31 | Merz Pharma GmbH & Co. KGaA | Novel recombinant botulinum neurotoxins with increased duration of effect |
US11707510B2 (en) * | 2018-02-16 | 2023-07-25 | Preclinics Discovery Gmbh | Nucleic acid-based botulinum neurotoxin for therapeutic use |
EP3765627A4 (en) * | 2018-03-12 | 2021-10-13 | Conagen Inc. | BIOSYNTHETIC PRODUCTION OF STEVIOL GLYCOSIDES REBAUDIOSIDE J AND REBAUDIOSIDE N |
CN112135840B (zh) * | 2018-03-13 | 2024-01-23 | 斯米维特公司 | 与破伤风神经毒素结合的单域抗体 |
CN108588087B (zh) * | 2018-05-16 | 2022-06-03 | 南京农业大学 | 一种提高植物抗病性的基因GmLecRK-R及其应用 |
US11535836B2 (en) * | 2018-12-21 | 2022-12-27 | Fornia Biosolutions, Inc. | Variant G6P G7P glucoamylase compositions and methods |
CN109998055B (zh) * | 2019-04-09 | 2022-03-25 | 黑龙江省科学院大庆分院 | 一种汉麻籽抗氧化多肽咀嚼片及其制备方法 |
CN110100945B (zh) * | 2019-05-05 | 2022-05-03 | 黑龙江省科学院大庆分院 | 一种汉麻降血脂肽组合物及其应用 |
WO2020253537A1 (zh) * | 2019-06-21 | 2020-12-24 | 苏州克睿基因生物科技有限公司 | 一种检测非洲猪瘟病毒的方法和试剂盒 |
CN110295150A (zh) * | 2019-07-17 | 2019-10-01 | 天津润德生物科技有限公司 | 一类腺依赖病毒病毒重组质粒、重组病毒及构建方法 |
CN110540996B (zh) * | 2019-08-29 | 2022-01-28 | 华中农业大学 | 一种克氏原螯虾i型溶菌酶gLysi2基因、其编码的gLysi2蛋白及其应用 |
AU2020357502A1 (en) * | 2019-09-30 | 2022-05-19 | Gilead Sciences, Inc. | HBV vaccines and methods treating HBV |
CN110643616A (zh) * | 2019-10-22 | 2020-01-03 | 云南省烟草农业科学研究院 | 一种烟草降烟碱合成调控基因NtERF91的克隆和应用 |
CN112540178B (zh) * | 2020-08-06 | 2023-12-19 | 武汉天德生物科技有限公司 | 一种检测早期老年痴呆症的免疫组化试剂盒及其使用方法 |
CN112662644B (zh) * | 2021-01-19 | 2022-04-22 | 华南理工大学 | 一种甘油磷酸二酯磷酸二酯酶突变体及其应用 |
CN113899907B (zh) * | 2021-09-07 | 2023-06-27 | 中国农业科学院油料作物研究所 | 一步式高效筛选黄曲霉毒素绿色防控材料的方法及其应用 |
CN115109759B (zh) * | 2022-06-24 | 2024-05-03 | 浙江工业大学 | 羰基还原酶LsCR突变体、工程菌及在不对称还原羰基化合物制备手性醇中的应用 |
CN117741160B (zh) * | 2023-12-21 | 2024-07-12 | 汉王科技股份有限公司 | 嗅觉受体在识别乙醇中的用途和检测乙醇的方法 |
Family Cites Families (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
TW574036B (en) | 1998-09-11 | 2004-02-01 | Elan Pharm Inc | Stable liquid compositions of botulinum toxin |
US6903187B1 (en) * | 2000-07-21 | 2005-06-07 | Allergan, Inc. | Leucine-based motif and clostridial neurotoxins |
US7491799B2 (en) * | 2000-07-21 | 2009-02-17 | Allergan, Inc. | Modified botulinum neurotoxins |
US20020127247A1 (en) * | 2000-11-17 | 2002-09-12 | Allergen Sales, Inc. | Modified clostridial neurotoxins with altered biological persistence |
DE10333317A1 (de) | 2003-07-22 | 2005-02-17 | Biotecon Therapeutics Gmbh | Formulierung für Proteinarzneimittel ohne Zusatz von humanem Serumalbumin (HSA) |
US7172764B2 (en) * | 2003-11-17 | 2007-02-06 | Allergan, Inc. | Rescue agents for treating botulinum toxin intoxications |
US20060004334A1 (en) | 2004-06-30 | 2006-01-05 | Kimberly-Clark Worldwide, Inc. | Stabilized absorbent structures |
EP1761558A1 (en) * | 2004-06-30 | 2007-03-14 | Allergan, Inc. | Optimizing expression of active botulinum toxin type e |
CN101005853B (zh) | 2004-07-26 | 2011-05-04 | 莫茨药物股份两合公司 | 包含肉毒杆菌神经毒素的治疗组合物 |
-
2010
- 2010-07-01 AU AU2010267963A patent/AU2010267963B2/en not_active Ceased
- 2010-07-01 JP JP2012516796A patent/JP6059986B2/ja not_active Expired - Fee Related
- 2010-07-01 BR BRPI1014253A patent/BRPI1014253A2/pt not_active Application Discontinuation
- 2010-07-01 KR KR1020127001754A patent/KR20120104140A/ko active Application Filing
- 2010-07-01 RU RU2012103376/10A patent/RU2582266C2/ru not_active IP Right Cessation
- 2010-07-01 ES ES10726549.8T patent/ES2693705T3/es active Active
- 2010-07-01 MX MX2011013014A patent/MX2011013014A/es active IP Right Grant
- 2010-07-01 CA CA2763692A patent/CA2763692A1/en active Pending
- 2010-07-01 MX MX2014014585A patent/MX352265B/es unknown
- 2010-07-01 WO PCT/EP2010/059398 patent/WO2011000929A1/en active Application Filing
- 2010-07-01 KR KR1020177003042A patent/KR101818895B1/ko active IP Right Grant
- 2010-07-01 IN IN733DEN2012 patent/IN2012DN00733A/en unknown
- 2010-07-01 CN CN201080027593.0A patent/CN102471765B9/zh not_active Expired - Fee Related
- 2010-07-01 EP EP10726549.8A patent/EP2449101B1/en active Active
- 2010-07-01 US US13/381,533 patent/US8586329B2/en active Active
-
2011
- 2011-11-17 IL IL216414A patent/IL216414A/en not_active IP Right Cessation
-
2012
- 2012-11-22 HK HK12111954.7A patent/HK1171246A1/zh not_active IP Right Cessation
-
2013
- 2013-10-17 US US14/056,247 patent/US9193771B2/en active Active
-
2015
- 2015-07-16 JP JP2015141904A patent/JP2015231378A/ja active Pending
- 2015-10-19 US US14/886,485 patent/US9511114B2/en active Active
-
2016
- 2016-11-03 US US15/342,376 patent/US9827298B2/en active Active
Non-Patent Citations (3)
Title |
---|
Botulinum neurotoxins: perspective on their existence and as polyproteins harboring viral proteases;DASGUPTA BIBHUTI R;《THE JOURNAL OF GENERAL AND APPLIED MICROBIOLOGY 》;20061231;1-8 * |
Modulation of the intracellular stability and toxicity of diphtheria toxin through degradation by the N-end rule pathway;FALNES P O ET AL;《EMBO JOURNAL》;19980101;615-625 * |
Modulation of the intracellular stability and toxicity of diphtheria toxin through degradation by the N-end rule pathway;OYLER G A ET AL;《TOXICON》;20080601;17 * |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN111629762A (zh) * | 2018-03-20 | 2020-09-04 | 美国醣基生医股份有限公司 | 结合至ssea4的嵌合抗原受体及其用途 |
Also Published As
Publication number | Publication date |
---|---|
US20120107362A1 (en) | 2012-05-03 |
US20170072030A1 (en) | 2017-03-16 |
US9827298B2 (en) | 2017-11-28 |
IL216414A0 (en) | 2012-02-29 |
RU2012103376A (ru) | 2013-08-10 |
US9511114B2 (en) | 2016-12-06 |
WO2011000929A1 (en) | 2011-01-06 |
US8586329B2 (en) | 2013-11-19 |
BRPI1014253A2 (pt) | 2016-04-12 |
JP6059986B2 (ja) | 2017-01-11 |
KR101818895B1 (ko) | 2018-01-15 |
EP2449101B1 (en) | 2018-10-10 |
CA2763692A1 (en) | 2011-01-06 |
AU2010267963A1 (en) | 2011-12-22 |
JP2015231378A (ja) | 2015-12-24 |
RU2582266C2 (ru) | 2016-04-20 |
KR20170016529A (ko) | 2017-02-13 |
CN102471765B9 (zh) | 2016-07-27 |
AU2010267963B2 (en) | 2015-09-24 |
CN102471765A (zh) | 2012-05-23 |
IN2012DN00733A (zh) | 2015-06-19 |
MX352265B (es) | 2017-11-16 |
IL216414A (en) | 2016-08-31 |
EP2449101A1 (en) | 2012-05-09 |
ES2693705T3 (es) | 2018-12-13 |
JP2012531191A (ja) | 2012-12-10 |
KR20120104140A (ko) | 2012-09-20 |
MX2011013014A (es) | 2012-01-27 |
US20140045760A1 (en) | 2014-02-13 |
HK1171246A1 (zh) | 2013-03-22 |
US20160030511A1 (en) | 2016-02-04 |
US9193771B2 (en) | 2015-11-24 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
CN102471765B (zh) | 显示出缩短的生物学活性的神经毒素 | |
CN103974973A (zh) | 显示出缩短的生物学活性的神经毒素 | |
EP1309618B1 (en) | Leucine-based motif and clostridial neurotoxins | |
US7514088B2 (en) | Multivalent Clostridial toxin derivatives and methods of their use | |
IL270769A (en) | Cationic neurotoxins | |
US7491799B2 (en) | Modified botulinum neurotoxins | |
CN116333158A (zh) | 嵌合神经毒素 | |
US20030219462A1 (en) | Clostridial neurotoxin compositions and modified clostridial neurotoxins | |
RU2017134357A (ru) | Сконструированный ботулинический нейротоксин | |
US9314514B2 (en) | Modified neurotoxins with poly-glycine and uses thereof | |
CN111454931A (zh) | 用于制备经蛋白水解处理的多肽的方法 | |
US10688162B2 (en) | Hybrid neurotoxins and uses thereof | |
WO2009015840A2 (en) | Polypeptide for targeting of neural cells | |
TW201639876A (zh) | 嵌合多肽 | |
CN109415750A (zh) | 活化的梭菌神经毒素的生产 | |
US11492391B1 (en) | Intracellular nanobody targeting T4SS effector inhibits ehrlichia infection | |
KR20230145411A (ko) | 변형된 독소 폴리펩티드의 제조 방법 | |
WO2023209403A1 (en) | Treatment of upper facial lines | |
KR20230144618A (ko) | 변형된 신경독소의 단일 사슬 폴리펩티드 및 이의 용도 |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
C06 | Publication | ||
PB01 | Publication | ||
C10 | Entry into substantive examination | ||
SE01 | Entry into force of request for substantive examination | ||
REG | Reference to a national code |
Ref country code: HK Ref legal event code: DE Ref document number: 1171246 Country of ref document: HK |
|
C14 | Grant of patent or utility model | ||
GR01 | Patent grant | ||
C53 | Correction of patent of invention or patent application | ||
CI03 | Correction of invention patent |
Correction item: Nucleotide or amino acid sequence table False: You Number: 19 Page: full text Volume: 32 |
|
REG | Reference to a national code |
Ref country code: HK Ref legal event code: GR Ref document number: 1171246 Country of ref document: HK |
|
CF01 | Termination of patent right due to non-payment of annual fee | ||
CF01 | Termination of patent right due to non-payment of annual fee |
Granted publication date: 20160511 Termination date: 20190701 |