EA020979B1 - ПЭГИЛИРОВАННЫЕ Fab-ФРАГМЕНТЫ АНТИТЕЛ К ПЕПТИДУ Aβ - Google Patents
ПЭГИЛИРОВАННЫЕ Fab-ФРАГМЕНТЫ АНТИТЕЛ К ПЕПТИДУ Aβ Download PDFInfo
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- EA020979B1 EA020979B1 EA200970694A EA200970694A EA020979B1 EA 020979 B1 EA020979 B1 EA 020979B1 EA 200970694 A EA200970694 A EA 200970694A EA 200970694 A EA200970694 A EA 200970694A EA 020979 B1 EA020979 B1 EA 020979B1
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Landscapes
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| PCT/US2008/050554 WO2008088983A1 (en) | 2007-01-18 | 2008-01-09 | PEGYLATED Aβ FAB |
Publications (2)
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| AU2010256410B2 (en) * | 2009-06-04 | 2016-10-20 | Massachusetts Institute Of Technology | Methods for identification of sites for IgG conjugation |
| EP2542579A1 (en) | 2010-03-03 | 2013-01-09 | Boehringer Ingelheim International GmbH | Biparatopic abeta binding polypeptides |
| JP6231263B2 (ja) * | 2012-07-17 | 2017-11-15 | 株式会社島津製作所 | アフィニティ支持体及びそれを用いた物質の捕捉方法 |
| US10431325B2 (en) | 2012-08-03 | 2019-10-01 | Novartis Ag | Methods to identify amino acid residues involved in macromolecular binding and uses therefor |
| WO2015036553A1 (en) * | 2013-09-16 | 2015-03-19 | Novo Nordisk Health Care Ag | Thiol functionalized polymers |
| KR20150133576A (ko) | 2014-05-20 | 2015-11-30 | 삼성전자주식회사 | 화학적 개질된 표적화 단백질 및 그의 이용 |
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| WO2017079835A1 (en) | 2015-11-09 | 2017-05-18 | The University Of British Columbia | Amyloid beta epitopes and antibodies thereto |
| EP3374379A4 (en) | 2015-11-09 | 2019-05-15 | The University Of British Columbia | N-TERMINAL EPITOPES IN AMYLOID BETA AND CONFORMATION-SELECTIVE ANTIBODIES |
| TWI735600B (zh) | 2016-07-01 | 2021-08-11 | 美商美國禮來大藥廠 | 抗－N3pGlu類澱粉β肽抗體及其用途 |
| CN109476729A (zh) | 2016-07-18 | 2019-03-15 | 英属哥伦比亚大学 | 淀粉样蛋白β的抗体 |
| CN109562167A (zh) | 2016-08-09 | 2019-04-02 | 伊莱利利公司 | 联合治疗 |
| US20180125920A1 (en) | 2016-11-09 | 2018-05-10 | The University Of British Columbia | Methods for preventing and treating A-beta oligomer-associated and/or -induced diseases and conditions |
| US12286469B2 (en) | 2017-07-18 | 2025-04-29 | The University Of British Columbia | Humanized antibodies binding to amyloid-beta (A-beta) |
| CA3070085A1 (en) | 2017-07-18 | 2019-01-24 | Promis Neurosciences Inc. | Antibodies to amyloid beta |
| WO2019023247A1 (en) | 2017-07-25 | 2019-01-31 | Immutics, Inc. | TREATMENT OF CANCER BY BLOCKING THE INTERACTION OF TIM-3 AND ITS LIGAND |
| WO2019134039A1 (en) * | 2018-01-04 | 2019-07-11 | Septa Therapeutics, Inc. | Septapeptides associated with neurodegeneracy |
| EP3918323A4 (en) | 2019-01-30 | 2022-12-28 | TrueBinding, Inc. | ANTI-GAL3 ANTIBODIES AND USES THEREOF |
| WO2021242776A2 (en) | 2020-05-26 | 2021-12-02 | Truebinding, Inc. | Methods of treating inflammatory diseases by blocking galectin-3 |
| TW202300518A (zh) | 2021-03-12 | 2023-01-01 | 美商美國禮來大藥廠 | 抗N3pGlu類澱粉β抗體及其用途 |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004071408A2 (en) * | 2003-02-10 | 2004-08-26 | Applied Molecular Evolution, Inc. | Aβ BINDING MOLECULES |
| WO2006040153A2 (en) * | 2004-10-13 | 2006-04-20 | Ablynx N.V. | Single domain camelide anti -amyloid beta antibodies and polypeptides comprising the same for the treatment and diagnosis of degenarative neural diseases such as alzheimer's disease |
| US20060257396A1 (en) * | 2004-12-15 | 2006-11-16 | Jacobsen Jack S | Abeta antibodies for use in improving cognition |
Family Cites Families (52)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US5278049A (en) * | 1986-06-03 | 1994-01-11 | Incyte Pharmaceuticals, Inc. | Recombinant molecule encoding human protease nexin |
| US5004697A (en) | 1987-08-17 | 1991-04-02 | Univ. Of Ca | Cationized antibodies for delivery through the blood-brain barrier |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5753624A (en) * | 1990-04-27 | 1998-05-19 | Milkhaus Laboratory, Inc. | Materials and methods for treatment of plaquing disease |
| US5445090A (en) | 1991-07-25 | 1995-08-29 | Mim Industries, Inc. | Interchangeable clamp for use in a sewing machine |
| US5766846A (en) * | 1992-07-10 | 1998-06-16 | Athena Neurosciences | Methods of screening for compounds which inhibit soluble β-amyloid peptide production |
| US5837672A (en) * | 1992-07-10 | 1998-11-17 | Athena Neurosciences, Inc. | Methods and compositions for the detection of soluble β-amyloid peptide |
| CA2115900A1 (en) | 1993-02-22 | 1994-08-23 | Gerald W. Becker | Pharmaceutical screens and antibodies |
| US5446090A (en) | 1993-11-12 | 1995-08-29 | Shearwater Polymers, Inc. | Isolatable, water soluble, and hydrolytically stable active sulfones of poly(ethylene glycol) and related polymers for modification of surfaces and molecules |
| CA2182731A1 (en) * | 1994-02-03 | 1995-08-10 | Michael P. Vitek | Compositions and methods for advanced glycosylation endproduct-mediated modulation of amyloidosis |
| US5668651A (en) * | 1994-03-18 | 1997-09-16 | Sharp Kabushiki Kaisha | Polymer-wall LCD having liquid crystal molecules having a plane-symmetrical bend orientation |
| US6114133A (en) * | 1994-11-14 | 2000-09-05 | Elan Pharmaceuticals, Inc. | Methods for aiding in the diagnosis of Alzheimer's disease by measuring amyloid-β peptide (x-≧41) |
| US5688651A (en) | 1994-12-16 | 1997-11-18 | Ramot University Authority For Applied Research And Development Ltd. | Prevention of protein aggregation |
| US5932462A (en) | 1995-01-10 | 1999-08-03 | Shearwater Polymers, Inc. | Multiarmed, monofunctional, polymer for coupling to molecules and surfaces |
| US5786180A (en) | 1995-02-14 | 1998-07-28 | Bayer Corporation | Monoclonal antibody 369.2B specific for β A4 peptide |
| US6214966B1 (en) | 1996-09-26 | 2001-04-10 | Shearwater Corporation | Soluble, degradable poly(ethylene glycol) derivatives for controllable release of bound molecules into solution |
| US20040121415A1 (en) * | 1996-12-10 | 2004-06-24 | King David John | Monovalent antibody fragments |
| US6218506B1 (en) * | 1997-02-05 | 2001-04-17 | Northwestern University | Amyloid β protein (globular assembly and uses thereof) |
| US6413940B1 (en) | 1997-02-07 | 2002-07-02 | Nymox Corporation | Pharmaceutically active agents that impede the formation of amyloid by impeding the genesis of DMS |
| WO1998044955A1 (en) | 1997-04-09 | 1998-10-15 | Mindset Ltd. | Recombinant antibodies specific for beta-amyloid ends, dna encoding and methods of use thereof |
| US20020086847A1 (en) * | 1997-04-09 | 2002-07-04 | Mindset Biopharmaceuticals (Usa) | Recombinant antibodies specific for beta-amyloid ends, DNA encoding and methods of use thereof |
| US6787319B2 (en) * | 1997-04-16 | 2004-09-07 | American Home Products Corp. | β-amyloid peptide-binding proteins and polynucleotides encoding the same |
| US6227999B1 (en) | 1997-07-09 | 2001-05-08 | Transmisiones Tsp, S.A. De C.V. | Method and apparatus for operating a clutch in an automated mechanical transmission |
| IT1293511B1 (it) | 1997-07-30 | 1999-03-01 | Gentili Ist Spa | Anticorpi monoclonali catalitici ad attivita' proteasica per la lisi selettiva della componente proteica di placche e aggregati correlati |
| AU8777898A (en) * | 1997-08-11 | 1999-03-01 | Chiron Corporation | Methods for genetically modifying t cells |
| US6448369B1 (en) | 1997-11-06 | 2002-09-10 | Shearwater Corporation | Heterobifunctional poly(ethylene glycol) derivatives and methods for their preparation |
| TWI239847B (en) * | 1997-12-02 | 2005-09-21 | Elan Pharm Inc | N-terminal fragment of Abeta peptide and an adjuvant for preventing and treating amyloidogenic disease |
| US7964192B1 (en) | 1997-12-02 | 2011-06-21 | Janssen Alzheimer Immunotherapy | Prevention and treatment of amyloidgenic disease |
| CA2323048C (en) | 1998-03-12 | 2006-10-10 | Shearwater Polymers, Inc. | Poly(ethylene glycol) derivatives with proximal reactive groups |
| WO1999060024A1 (en) | 1998-05-21 | 1999-11-25 | The University Of Tennessee Research Corporation | Methods for amyloid removal using anti-amyloid antibodies |
| ATE405636T1 (de) * | 1999-06-16 | 2008-09-15 | Boston Biomedical Res Inst | Immunologische kontrolle des beta-amyloid gehaltes in vivo |
| EP1200470B1 (en) | 1999-08-04 | 2004-11-24 | The University Of Southern California | Globular assembly of amyloid beta protein and uses thereof |
| CA2349434A1 (en) | 1999-09-03 | 2001-03-15 | Ramot University Authority For Applied Research & Industrial Development Ltd. | Agents and compositions and methods utilizing same useful in diagnosing and/or treating or preventing plaque forming diseases |
| US6294171B2 (en) | 1999-09-14 | 2001-09-25 | Milkhaus Laboratory, Inc. | Methods for treating disease states comprising administration of low levels of antibodies |
| KR100653153B1 (ko) | 1999-12-22 | 2006-12-01 | 넥타르 테라퓨틱스 에이엘, 코포레이션 | 수용성 중합체의 입체장애 유도체 |
| US6413507B1 (en) | 1999-12-23 | 2002-07-02 | Shearwater Corporation | Hydrolytically degradable carbamate derivatives of poly (ethylene glycol) |
| WO2001062801A2 (en) | 2000-02-24 | 2001-08-30 | Washington University | Humanized antibodies that sequester amyloid beta peptide |
| US20020009445A1 (en) * | 2000-07-12 | 2002-01-24 | Yansheng Du | Human beta-amyloid antibody and use thereof for treatment of alzheimer's disease |
| AU2001290638C1 (en) | 2000-09-06 | 2009-04-30 | Aventis Pharma S.A. | Methods and compositions for diseases associated with amyloidosis |
| US6436386B1 (en) | 2000-11-14 | 2002-08-20 | Shearwater Corporation | Hydroxyapatite-targeting poly (ethylene glycol) and related polymers |
| TWI255272B (en) | 2000-12-06 | 2006-05-21 | Guriq Basi | Humanized antibodies that recognize beta amyloid peptide |
| EP1944040B1 (en) * | 2001-08-17 | 2012-08-01 | Washington University | Assay method for Alzheimer's disease |
| CA2452104A1 (en) * | 2001-08-17 | 2003-02-27 | Eli Lilly And Company | Use of antibodies having high affinity for soluble ass to treat conditions and diseases related to ass |
| WO2003015691A2 (en) | 2001-08-17 | 2003-02-27 | Eli Lilly And Company | RAPID IMPROVEMENT OF COGNITION IN CONDITIONS RELATED TO A$g(b) |
| WO2003015617A2 (en) | 2001-08-17 | 2003-02-27 | Washington University | Assay method for alzheimer's disease |
| EP1432444A4 (en) | 2001-08-17 | 2005-11-02 | Lilly Co Eli | ANTI-BETA ANTIBODIES |
| US7166478B2 (en) * | 2002-03-12 | 2007-01-23 | Enzo Life Sciences, Inc., C/O Enzo Biochem, Inc. | Labeling reagents and labeled targets, target labeling processes and other processes for using same in nucleic acid determinations and analyses |
| JP2005523335A (ja) | 2002-04-25 | 2005-08-04 | イーライ・リリー・アンド・カンパニー | 高齢被検体の不安障害および気分障害の治療方法 |
| KR101025143B1 (ko) * | 2002-12-31 | 2011-04-01 | 넥타르 테라퓨틱스 | 가수분해상으로 안정한 말레이미드－종결 중합체 |
| CA2529819A1 (en) * | 2003-06-30 | 2004-09-23 | Domantis Limited | Pegylated single domain antibodies |
-
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Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004071408A2 (en) * | 2003-02-10 | 2004-08-26 | Applied Molecular Evolution, Inc. | Aβ BINDING MOLECULES |
| WO2006040153A2 (en) * | 2004-10-13 | 2006-04-20 | Ablynx N.V. | Single domain camelide anti -amyloid beta antibodies and polypeptides comprising the same for the treatment and diagnosis of degenarative neural diseases such as alzheimer's disease |
| US20060257396A1 (en) * | 2004-12-15 | 2006-11-16 | Jacobsen Jack S | Abeta antibodies for use in improving cognition |
Non-Patent Citations (1)
| Title |
|---|
| CHAPMAN ANDREW P.: "PEGylated antibodies and antibody fragments for improved therapy: A review", 20020617, vol. 54, no. 4, 17 June 2002 (2002-06-17), pages 531-545, XP001199533, page 532, right-hand column, paragraph 1 - page 534, right-hand column, paragraph 1 page 537, right-hand column, paragraph 3 - page 539, right-hand column, paragraph 1, page 542, left-hand column, paragraph 2 - right-hand column, paragraph 1, page 543, right-hand column, paragraph 2 * |
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