JP2009545756A - タンパク質凝集を予測し凝集阻害物質を設計する方法 - Google Patents

タンパク質凝集を予測し凝集阻害物質を設計する方法 Download PDF

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JP2009545756A
JP2009545756A JP2009523338A JP2009523338A JP2009545756A JP 2009545756 A JP2009545756 A JP 2009545756A JP 2009523338 A JP2009523338 A JP 2009523338A JP 2009523338 A JP2009523338 A JP 2009523338A JP 2009545756 A JP2009545756 A JP 2009545756A
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residues
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カイ イェー コールホフ
ヘスス スルド
ミケーレ ヴェンドルスコロ
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ロンザ バイオロジックス ピーエルシー
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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
    • G—PHYSICS
    • G16—INFORMATION AND COMMUNICATION TECHNOLOGY [ICT] SPECIALLY ADAPTED FOR SPECIFIC APPLICATION FIELDS
    • G16B—BIOINFORMATICS, i.e. INFORMATION AND COMMUNICATION TECHNOLOGY [ICT] SPECIALLY ADAPTED FOR GENETIC OR PROTEIN-RELATED DATA PROCESSING IN COMPUTATIONAL MOLECULAR BIOLOGY
    • G16B15/00—ICT specially adapted for analysing two-dimensional [2D] or three-dimensional [3D] molecular structures, e.g. structural or functional relations or structure alignment
    • G16B15/30—Drug targeting using structural data; Docking or binding prediction

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JP2009523338A 2006-08-04 2007-07-24 タンパク質凝集を予測し凝集阻害物質を設計する方法 Pending JP2009545756A (ja)

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US82155306P 2006-08-04 2006-08-04
PCT/GB2007/002789 WO2008015384A1 (en) 2006-08-04 2007-07-24 Method for predicting protein aggregation and designing aggregation inhibitors

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JP2009545756A true JP2009545756A (ja) 2009-12-24
JP2009545756A5 JP2009545756A5 (https=) 2010-09-09

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US (1) US8290713B2 (https=)
EP (1) EP2047393A1 (https=)
JP (1) JP2009545756A (https=)
KR (1) KR20090047470A (https=)
CN (1) CN101501694B (https=)
AU (1) AU2007280282B2 (https=)
CA (1) CA2657847A1 (https=)
EA (1) EA016884B1 (https=)
IL (1) IL196551A (https=)
SG (1) SG173405A1 (https=)
WO (1) WO2008015384A1 (https=)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
KR20170094798A (ko) * 2015-01-06 2017-08-21 노쓰 캐롤라이나 스테이트 유니버시티 이종 단백질 생성을 최적화하기 위한 리보좀 역학 모델링

Families Citing this family (21)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE10303974A1 (de) 2003-01-31 2004-08-05 Abbott Gmbh & Co. Kg Amyloid-β(1-42)-Oligomere, Verfahren zu deren Herstellung und deren Verwendung
US8691224B2 (en) 2005-11-30 2014-04-08 Abbvie Inc. Anti-Aβ globulomer 5F7 antibodies
HRP20140240T4 (hr) 2005-11-30 2017-02-24 Abbvie Inc. Monoklonalna antitijela protiv amiloidnih beta proteina i njihova upotreba
US8455626B2 (en) 2006-11-30 2013-06-04 Abbott Laboratories Aβ conformer selective anti-aβ globulomer monoclonal antibodies
US8895004B2 (en) 2007-02-27 2014-11-25 AbbVie Deutschland GmbH & Co. KG Method for the treatment of amyloidoses
GB2455102A (en) * 2007-11-28 2009-06-03 Cambridge Entpr Ltd Protein Aggregation Prediction Systems
WO2009128948A1 (en) 2008-04-17 2009-10-22 Peptimmune, Inc. Design and synthesis of directed sequence polymer compositions and antibodies thereof for the treatment of protein conformational disorders
CN107677828A (zh) * 2008-10-31 2018-02-09 耶鲁大学 子痫前期检测和治疗的方法和组合物
AU2010310895A1 (en) * 2009-10-23 2012-05-03 Garvan Institute Of Medical Research Modified variable domain molecules and methods for producing and using same
US8987419B2 (en) 2010-04-15 2015-03-24 AbbVie Deutschland GmbH & Co. KG Amyloid-beta binding proteins
FI20105629A0 (fi) * 2010-06-03 2010-06-03 Estaja Oy Menetelmä lipidiaktivoituvien entsyymien peptidi-inhibiittoreiden valmistamiseksi ja menetelmällä valmistettuja peptidejä
EP3533803B1 (en) 2010-08-14 2021-10-27 AbbVie Inc. Anti-amyloid-beta antibodies
US20120108904A1 (en) * 2010-10-20 2012-05-03 Yong Ma Cleaner for endoscope
CN103772487B (zh) * 2012-10-24 2015-11-25 国家纳米科学中心 一种抑制人胰淀素聚集或毒性的多肽、试剂及其应用
US9618524B2 (en) * 2014-03-26 2017-04-11 Plaxgen Inc. Method, composition, isolation and identification of a plaque particle and related biomarker
CN104502219B (zh) * 2014-12-18 2017-09-29 江苏大学 一种淀粉样多肽聚集抑制剂及其抑制效果评估和验证方法
GB201600176D0 (en) * 2016-01-06 2016-02-17 Cambridge Entpr Ltd Method of identifying novel protein aggregation inhibitors based on chemical kinetics
CA3011719A1 (en) * 2016-01-21 2017-07-27 Protein Dynamic Solutions Llc Method and system for spectral data analysis
US10815271B2 (en) * 2016-06-29 2020-10-27 The Regents Of The University Of California Structure-based peptide inhibitors of alpha-synuclein aggregation
CN106501550A (zh) * 2016-12-09 2017-03-15 江苏大学 基于原子力显微镜氨基酸影响鱼蛋白聚集行为的评价方法
CN111653310B (zh) * 2020-06-29 2023-06-20 北京大学深圳研究生院 含二硫键多肽的结构预测方法及装置

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2004513873A (ja) * 1999-11-05 2004-05-13 アクソニックス，インコーポレイティド アミロイド、アミロイド様沈着物またはそれらのβ−シートリッチな病理前駆体への異常タンパク質折り畳みに関係する疾患の治療における生体内使用に適するペプチド類似物および模倣物
WO2005000288A2 (en) * 2003-06-23 2005-01-06 Neurochem (International) Limited Treatment of protein aggregation disorders

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB0325817D0 (en) 2003-11-05 2003-12-10 Univ Cambridge Tech Method and apparatus for assessing polypeptide aggregation

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2004513873A (ja) * 1999-11-05 2004-05-13 アクソニックス，インコーポレイティド アミロイド、アミロイド様沈着物またはそれらのβ−シートリッチな病理前駆体への異常タンパク質折り畳みに関係する疾患の治療における生体内使用に適するペプチド類似物および模倣物
WO2005000288A2 (en) * 2003-06-23 2005-01-06 Neurochem (International) Limited Treatment of protein aggregation disorders

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
JPN5009011081; ＤＥ　ＧＲＯＯＴ　ＮＡＴＡＬＩＡ　ＳＡＮＣＨＥＺ: ＢＭＣ　ＳＴＲＵＣＴＵＲＡＬ　ＢＩＯＬＯＧＹ Ｖ５　Ｎ１８, 20050930, Ｐ１-１５, ＢＩＯＭＥＤ　ＣＥＮＴＲＡＬ　ＬＴＤ． *
JPN5009011082; ＰＡＷＡＲ　Ａ　Ｐ: ＪＯＵＲＮＡＬ　ＯＦ　ＭＯＬＥＣＵＬＡＲ　ＢＩＯＬＯＧＹ Ｖ３５０　Ｎ２, 20050708, Ｐ３７９-３９２ *
JPN6012062078; ＴＡＫＡＨＡＳＨＩ　Ｔｓｕｙｏｓｈｉ　ｅｔ　ａｌ．: 'Ｐｅｐｔｉｄｅ　ａｎｄ　Ｐｒｏｔｅｉｎ　Ｍｉｍｅｔｉｃｓ　Ｉｎｈｉｂｉｔｉｎｇ　Ａｍｙｌｏｉｄ　beta-Ｐｅｐｔｉｄｅ　Ａｇｇｒｅｇａｔｉｏｎ' Ａｃｃ．　Ｃｈｅｍ．　Ｒｅｓ． Ｖｏｌ．４１，Ｎｏ．１０, 200810, Ｐ．１３０９-１３１８ *

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
KR20170094798A (ko) * 2015-01-06 2017-08-21 노쓰 캐롤라이나 스테이트 유니버시티 이종 단백질 생성을 최적화하기 위한 리보좀 역학 모델링
KR102473180B1 (ko) 2015-01-06 2022-12-01 노쓰 캐롤라이나 스테이트 유니버시티 이종 단백질 생성을 최적화하기 위한 리보좀 역학 모델링

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WO2008015384A1 (en) 2008-02-07
IL196551A0 (en) 2009-11-18
AU2007280282A1 (en) 2008-02-07
EA200970180A1 (ru) 2009-08-28
SG173405A1 (en) 2011-08-29
AU2007280282B2 (en) 2012-02-02
CA2657847A1 (en) 2008-02-07
CN101501694A (zh) 2009-08-05
US20100160602A1 (en) 2010-06-24
CN101501694B (zh) 2011-11-30
EA016884B1 (ru) 2012-08-30
IL196551A (en) 2013-01-31
US8290713B2 (en) 2012-10-16
WO2008015384A8 (en) 2008-05-15
KR20090047470A (ko) 2009-05-12
HK1131239A1 (en) 2010-01-15
EP2047393A1 (en) 2009-04-15

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