CA2954738A1 - Human-derived anti-huntingtin (htt) antibodies and uses thereof - Google Patents
Human-derived anti-huntingtin (htt) antibodies and uses thereof Download PDFInfo
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- CA2954738A1 CA2954738A1 CA2954738A CA2954738A CA2954738A1 CA 2954738 A1 CA2954738 A1 CA 2954738A1 CA 2954738 A CA2954738 A CA 2954738A CA 2954738 A CA2954738 A CA 2954738A CA 2954738 A1 CA2954738 A1 CA 2954738A1
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Classifications
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
- A61K39/3955—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals against proteinaceous materials, e.g. enzymes, hormones, lymphokines
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- A61P25/00—Drugs for disorders of the nervous system
- A61P25/28—Drugs for disorders of the nervous system for treating neurodegenerative disorders of the central nervous system, e.g. nootropic agents, cognition enhancers, drugs for treating Alzheimer's disease or other forms of dementia
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
- C12Q1/6876—Nucleic acid products used in the analysis of nucleic acids, e.g. primers or probes
- C12Q1/6883—Nucleic acid products used in the analysis of nucleic acids, e.g. primers or probes for diseases caused by alterations of genetic material
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- 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
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
- G01N33/6896—Neurological disorders, e.g. Alzheimer's disease
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- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
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- 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
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
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- 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
- C07K2317/31—Immunoglobulins specific features characterized by aspects of specificity or valency multispecific
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- 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
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
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- 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
-
- 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]
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- 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
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q2600/00—Oligonucleotides characterized by their use
- C12Q2600/158—Expression markers
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- G—PHYSICS
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- 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
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/46—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans from vertebrates
- G01N2333/47—Assays involving proteins of known structure or function as defined in the subgroups
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- G—PHYSICS
- G01—MEASURING; TESTING
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- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/28—Neurological disorders
- G01N2800/2835—Movement disorders, e.g. Parkinson, Huntington, Tourette
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Neurosurgery (AREA)
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- Hematology (AREA)
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- Zoology (AREA)
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- Gastroenterology & Hepatology (AREA)
- Endocrinology (AREA)
- Epidemiology (AREA)
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Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP14179004.8 | 2014-07-29 | ||
| EP14179004 | 2014-07-29 | ||
| PCT/EP2015/067327 WO2016016278A2 (en) | 2014-07-29 | 2015-07-29 | Human-derived anti-huntingtin (htt) antibodies and uses thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2954738A1 true CA2954738A1 (en) | 2016-02-04 |
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| Application Number | Title | Priority Date | Filing Date |
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| CA2954738A Pending CA2954738A1 (en) | 2014-07-29 | 2015-07-29 | Human-derived anti-huntingtin (htt) antibodies and uses thereof |
Country Status (11)
| Country | Link |
|---|---|
| US (3) | US10556946B2 (enExample) |
| EP (2) | EP4406549A3 (enExample) |
| JP (3) | JP2017522886A (enExample) |
| KR (1) | KR102643395B1 (enExample) |
| CN (2) | CN107074937B (enExample) |
| AU (3) | AU2015295441B2 (enExample) |
| CA (1) | CA2954738A1 (enExample) |
| EA (1) | EA201790165A1 (enExample) |
| IL (2) | IL250180A0 (enExample) |
| MX (3) | MX391037B (enExample) |
| WO (1) | WO2016016278A2 (enExample) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| HRP20140049T1 (hr) | 2007-01-05 | 2014-02-28 | University Of Zürich | Anti beta-amiloid antitijela i njihova upotreba |
| CN107074937B (zh) * | 2014-07-29 | 2021-07-27 | 神经免疫控股公司 | 人源抗亨廷顿蛋白(htt)抗体及其用途 |
| MA41115A (fr) | 2014-12-02 | 2017-10-10 | Biogen Int Neuroscience Gmbh | Procédé de traitement de la maladie d'alzheimer |
| SI3672631T1 (sl) | 2017-08-22 | 2023-06-30 | Biogen Ma Inc. | Farmacevtski sestavki, ki vsebujejo protitelesa proti beta amiloidu |
| TW202110878A (zh) | 2019-05-16 | 2021-03-16 | 法商賽諾菲公司 | 在神經系統中表現抗原結合蛋白 |
| EP4041308A1 (en) | 2019-10-07 | 2022-08-17 | University of Virginia Patent Foundation | Modulating lymphatic vessels in neurological disease |
| US20230067811A1 (en) | 2020-01-24 | 2023-03-02 | University Of Virginia Patent Foundation | Modulating lymphatic vessels in neurological disease |
| JP2023535024A (ja) | 2020-07-23 | 2023-08-15 | オター プロシーナ リミテッド | 抗ａベータ抗体 |
| CN111909265B (zh) * | 2020-08-25 | 2022-02-11 | 中国人民解放军军事科学院军事医学研究院 | 一种结合破伤风毒素重链c端结构域的人源抗体及应用 |
| EP4286406A4 (en) | 2021-01-29 | 2025-07-23 | Illimis Therapeutics Inc | FUSION MOLECULE WITH NON-INFLAMMATORY PHAGOCYTOSIS-INDUCING ACTIVITY |
| CA3239708A1 (en) | 2021-12-03 | 2023-06-08 | Aubin MICHALON | Novel potency assay for antibody-based drugs and useful means therefor |
| CN114334076B (zh) * | 2021-12-23 | 2025-03-21 | 华中科技大学 | 一种药食同源中药玉竹的重金属概率风险评估方法及系统 |
| WO2024121347A1 (en) * | 2022-12-07 | 2024-06-13 | Alchemab Therapeutics Ltd | Anti-huntingtin antibodies |
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| US4741900A (en) | 1982-11-16 | 1988-05-03 | Cytogen Corporation | Antibody-metal ion complexes |
| EP0216846B2 (en) | 1985-04-01 | 1995-04-26 | Celltech Limited | Transformed myeloma cell-line and a process for the expression of a gene coding for a eukaryotic polypeptide employing same |
| GB8601597D0 (en) | 1986-01-23 | 1986-02-26 | Wilson R H | Nucleotide sequences |
| EP0272253A4 (en) | 1986-03-07 | 1990-02-05 | Massachusetts Inst Technology | METHOD FOR IMPROVING GLYCOPROTE INSTABILITY. |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| DE3853515T3 (de) | 1987-05-21 | 2005-08-25 | Micromet Ag | Multifunktionelle proteine mit vorbestimmter zielsetzung. |
| US5892019A (en) | 1987-07-15 | 1999-04-06 | The United States Of America, As Represented By The Department Of Health And Human Services | Production of a single-gene-encoded immunoglobulin |
| GB8717430D0 (en) | 1987-07-23 | 1987-08-26 | Celltech Ltd | Recombinant dna product |
| EP0362371A4 (en) | 1988-04-15 | 1990-10-24 | Protein Design Labs, Inc. | Il-2 receptor-specific chimeric antibodies |
| AU631802B2 (en) | 1988-06-14 | 1992-12-10 | Cetus Oncology Corporation | Coupling agents and sterically hindered disulfide linked conjugates prepared therefrom |
| IL162181A (en) | 1988-12-28 | 2006-04-10 | Pdl Biopharma Inc | A method of producing humanized immunoglubulin, and polynucleotides encoding the same |
| US5225538A (en) | 1989-02-23 | 1993-07-06 | Genentech, Inc. | Lymphocyte homing receptor/immunoglobulin fusion proteins |
| US5116964A (en) | 1989-02-23 | 1992-05-26 | Genentech, Inc. | Hybrid immunoglobulins |
| ZA902949B (en) | 1989-05-05 | 1992-02-26 | Res Dev Foundation | A novel antibody delivery system for biological response modifiers |
| DE69133566T2 (de) | 1990-01-12 | 2007-12-06 | Amgen Fremont Inc. | Bildung von xenogenen Antikörpern |
| US5314995A (en) | 1990-01-22 | 1994-05-24 | Oncogen | Therapeutic interleukin-2-antibody based fusion proteins |
| WO1991014438A1 (en) | 1990-03-20 | 1991-10-03 | The Trustees Of Columbia University In The City Of New York | Chimeric antibodies with receptor binding ligands in place of their constant region |
| ATE218889T1 (de) | 1990-11-09 | 2002-06-15 | Stephen D Gillies | Cytokine immunokonjugate |
| MX9204374A (es) | 1991-07-25 | 1993-03-01 | Idec Pharma Corp | Anticuerpo recombinante y metodo para su produccion. |
| WO1994002602A1 (en) | 1992-07-24 | 1994-02-03 | Cell Genesys, Inc. | Generation of xenogeneic antibodies |
| WO1994009817A1 (en) | 1992-11-04 | 1994-05-11 | City Of Hope | Novel antibody construct |
| DE669986T1 (de) | 1992-11-13 | 1996-10-10 | Idec Pharma Corp | Völlig unfunktionelle konsensus-kozak-sequenzen zur säugetier-exprimierung. |
| US5736137A (en) | 1992-11-13 | 1998-04-07 | Idec Pharmaceuticals Corporation | Therapeutic application of chimeric and radiolabeled antibodies to human B lymphocyte restricted differentiation antigen for treatment of B cell lymphoma |
| CA2116280A1 (en) | 1993-03-05 | 1994-09-06 | Marcy E. Macdonald | Huntingtin dna, protein and uses thereof |
| JP4312259B2 (ja) | 1995-04-27 | 2009-08-12 | アムジェン フレモント インク． | 免疫したゼノマウス（ＸｅｎｏＭｏｕｓｅ）に由来するヒト抗体 |
| EP0823941A4 (en) | 1995-04-28 | 2001-09-19 | Abgenix Inc | HUMAN ANTIBODIES DERIVED FROM IMMUNIZED XENO MOUSES |
| GB9524973D0 (en) | 1995-12-06 | 1996-02-07 | Lynxvale Ltd | Viral vectors |
| US6255455B1 (en) * | 1996-10-11 | 2001-07-03 | The Trustees Of The University Of Pennsylvania | Rh(D)-binding proteins and magnetically activated cell sorting method for production thereof |
| CA2283740C (en) | 1997-03-14 | 2006-06-27 | Idec Pharmaceuticals Corporation | Method for integrating genes at specific sites in mammalian cells via homologous recombination and vectors for accomplishing the same |
| ES2258817T3 (es) | 1997-05-21 | 2006-09-01 | Biovation Limited | Metodo para la produccion de proteinas no inmunogenas. |
| WO1999006838A2 (en) | 1997-08-01 | 1999-02-11 | MAX-PLANCK-Gesellschaft zur Förderung der Wissenschaften e.V. | Novel method of detecting amyloid-like fibrils or protein aggregates |
| WO2000030680A1 (en) | 1998-11-23 | 2000-06-02 | Idec Pharmaceuticals Corporation | Tumor antigen-specific antibody-gp39 chimeric protein constructs |
| ATE352559T1 (de) | 1998-12-08 | 2007-02-15 | Biovation Ltd | Verfahren zur verminderung der immunogenität von proteinen |
| WO2001006989A2 (en) * | 1999-07-27 | 2001-02-01 | Abgenix, Inc. | Methods and compositions for inhibiting polypeptide accumulation associated with neurological disorders |
| AU2001297872B2 (en) | 2000-11-17 | 2006-11-09 | University Of Rochester | In vitro methods of producing and identifying immunoglobulin molecules in eukaryotic cells |
| NZ545176A (en) | 2001-01-29 | 2008-05-30 | Biogen Idec Inc | Modified antibodies reactive with CD20 and methods of use |
| WO2002096948A2 (en) | 2001-01-29 | 2002-12-05 | Idec Pharmaceuticals Corporation | Engineered tetravalent antibodies and methods of use |
| ATE532874T1 (de) * | 2001-02-15 | 2011-11-15 | Univ Chicago | Verfahren zum nachweis in hefe für mittels die proteinfaltung beeinflussen |
| US20030157641A1 (en) | 2001-11-16 | 2003-08-21 | Idec Pharmaceuticals Corporation | Polycistronic expression of antibodies |
| US7375194B2 (en) * | 2002-01-28 | 2008-05-20 | California Institute Of Technology | Antibodies that bind to an epitope on the Huntington's disease protein |
| AU2004239114B2 (en) * | 2003-05-14 | 2008-03-13 | Japan Science And Technology Agency | Inhibition of the expression of huntingtin gene |
| NZ545776A (en) | 2003-08-22 | 2009-05-31 | Biogen Idec Inc | Improved antibodies having altered effector function and methods for making the same |
| WO2005052002A2 (en) | 2003-11-20 | 2005-06-09 | Massachusetts Institute Of Technology | Single-domain antibodies and uses thereof |
| US8906367B2 (en) * | 2007-01-05 | 2014-12-09 | University Of Zurich | Method of providing disease-specific binding molecules and targets |
| US20090304590A1 (en) * | 2007-05-29 | 2009-12-10 | Wyeth | Therapeutic compositions and methods |
| US8022268B2 (en) * | 2007-06-11 | 2011-09-20 | The University Of Zurich | Transgenic animal model for alzheimer's disease |
| WO2010069603A1 (en) | 2008-12-19 | 2010-06-24 | Neurimmune Therapeutics Ag | Human anti-alpha-synuclein autoantibodies |
| LT2627672T (lt) | 2010-10-11 | 2018-12-10 | Biogen International Neuroscience Gmbh | Žmogaus antikūnai prieš tau baltymą |
| CN103380145B (zh) | 2010-12-17 | 2016-10-12 | 生物控股有限公司 | 人类抗-sod1抗体 |
| WO2012113775A1 (en) | 2011-02-21 | 2012-08-30 | University Of Zurich | Ankyrin g and modulators thereof for the treatment of neurodegenerative disorders |
| WO2013013025A2 (en) * | 2011-07-20 | 2013-01-24 | Medimmune Limited | Anti-cxcr4 antibodies and methods of use |
| ES2883212T3 (es) | 2011-10-28 | 2021-12-07 | Biogen Int Neuroscience Gmbh | Moléculas de unión específica a TDP-43 |
| CN105531287B (zh) * | 2013-05-29 | 2020-01-21 | 维拜昂公司 | 改变亨廷顿蛋白突变体降解的单链胞内抗体 |
| CN106687475A (zh) * | 2014-07-10 | 2017-05-17 | 阿费里斯股份公司 | 用于预防和/或治疗亨廷顿氏病的物质和方法 |
| RU2021100991A (ru) * | 2014-07-10 | 2021-03-01 | Аффирис Аг | Вещества и способы для применения при предупреждении и/или лечении болезни гентингтона |
| CN107074937B (zh) * | 2014-07-29 | 2021-07-27 | 神经免疫控股公司 | 人源抗亨廷顿蛋白(htt)抗体及其用途 |
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