The Intrachain Disulfide Bond of β_2-Microglobulin Is Not Essential for the Immunoglobulin Fold at Neutral pH, but Is Essential for Amyloid Fibril Formation at Acidic pH
スポンサーリンク
概要
- 論文の詳細を見る
- Japanese Biochemical Societyの論文
- 2002-01-01
著者
-
Goto Yuji
Inst. Protein. Res. Osaka Univ
-
Goto Yuji
大阪大学蛋白質研究所
-
Goto Yuji
Institute for Protein Research, Osaka University
-
Hasegawa Kazuhiro
Department of Oral Surgery, Nihon University School of Dentistry at Matsudo
-
Naiki Hironobu
Fac. Med. Sci. Univ Of Fukui
-
Naiki H
Fukui Medical Univ. Fukui
-
Naiki Hironobu
Department Of Pathology Fukui Medical University And Crest Japan Science And Technology Cooperation
-
Yamaguchi Itaru
Department Of Pathology Fukui Medical University
-
Hasegawa Kazuhiro
Fac. Med. Sci. Fukui Univ.
-
Hasegawa Kazuhiro
Department Of Oral Surgery Nihon University School Of Dentistry At Matsudo
-
Hagihara Yoshihisa
AIST
-
Goto Yuji
Institute For Protein Research Osaka University
-
Goto Yuji
Institute For Protein Research Osaka University And Crest Japan Science And Technology Corporation
-
OHHASHI Yumiko
Institute for Protein Research, Osaka University
-
HAGIHARA Yoshihisa
Institute for Protein Research, Osaka University
-
KOZHUKH Gennady
Institute for Protein Research, Osaka University
-
HOSHINO Masaru
Institute for Protein Research, Osaka University
-
Ohhashi Yumiko
Institute For Protein Research Osaka University And Crest Japan Science And Technology Cooperation
-
Hoshino M
Graduate School Of Pharmaceutical Sciences Kyoto University
-
Kozhukh Gennady
Institute For Protein Research Osaka University
-
Goto Yuji
CREST JST
-
Hoshino M
Institute For Protein Research Osaka University And Crest Japan Science And Technology Cooperation
-
Naiki Hironobu
Department Of Pathology Fukui Medical University And Crest
-
Hasegawa Kazuhiro
Department Of Internal Medicine School Of Medicine Keio University
-
Goto Yuji
Institute For Protein Research Osaka Univ
-
Hoshino Masaru
Institute For Protein Research Osaka University And Crest Japan Science And Technology Cooperation
関連論文
- Catechol derivatives inhibit the fibril formation of amyloid-β peptides(MEDICAL BIOTECHNOLOGY)
- 2P-083 Trp蛍光とH/D交換-NMR法をもちいたβ_2ミクログロブリンのアミロイド線維形成反応中間体の解析(蛋白質・物性(2),第46回日本生物物理学会年会)
- 2P-008 固体NMR法を用いたβ2ミクログロブリンが形成するアミロイド線維の構造解析(蛋白質・構造(2),第46回日本生物物理学会年会)
- An Unusually Large Submandibular Salivary Calculus: Case Report and Structural Analysis
- 1P-064 二重標識したマルトース結合蛋白質の基質結合と折りたたみの一分子観測(蛋白質-機能(反応機構,生物活性など),第47回日本生物物理学会年会)
- Malignant transformation of a lumbar intradural dermoid cyst
- 3P-022 一分子測定法を用いた緑濃菌由来シトクロムcの変性状態内の運動観察(蛋白質・物性(3),第46回日本生物物理学会年会)
- 3P074 一分子測定法によるβ-ラクトグロブリンの蛍光強度変化と拡散の観測(蛋白質-物性(安定性,折れたたみなど),第48回日本生物物理学会年会)
- 3P-010 重水素交換法を用いたアミロイド線維伸長反応機構の解析(蛋白質・物性(3),第46回日本生物物理学会年会)
- 3P-008 β2-ミクログロブリンとの比較による免疫グロブリン軽鎖C_Lのアミロイド線維形成能の評価(蛋白質・物性(3),第46回日本生物物理学会年会)
- 1P-087 β2ミクログロブリンのフラグメントが形成するアミロイド線維構造の構造解析(蛋白質・物性(1),第46回日本生物物理学会年会)
- 2P119 Reduction of disulfide bridge inhibits the amyloid fibril formation of β2-microglobulin(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 2P112 Heat Capacity Change Associated with Structural Conversion into Amyloid Fibril(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 2P109 Folding and Unfolding Kinetics of β2-Microglobulin as Probed by Tryptophan Fluorescence(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 2P106 Orientation of amyloid fibrils formed by β2-microglobulin and its peptide fragment in a flow(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 2P105 Structural polymorphism of β_2-microglobulin amyloid fibrils induced by the addition of trifluoroethanol(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- Effect of Methanol Concentration on the Production of Human β_2-Glycoprotein I Domain V by a Recombinant Pichia pastoris : A Simple System for the Control of Methanol Concentration Using a Semiconductor Gas Sensor
- Structure and function of the Recombinant Fifth Domain of Human β_2-Glycoprotein I: Effects of Specific Cleavage between Lys77 and Thr78^1
- Role of the N- and C- Terminal Domains of Bovine β_2- Glycoprotein I in Its Interaction with Cardiolipin^1
- 2P-098 新しいさや流セルを使用した蛋白質一分子の折り畳み軌跡の観測(蛋白質・物性(2),第46回日本生物物理学会年会)
- 1P112 Multiple time scales in the folding dynamics of single chain monellin revealed by single molecule measurements(3. Protein folding and misfolding (1),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 1P108 Development of sheath-flow system to observe protein folding events at a single-molecule level(3. Protein folding and misfolding (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- Dissolution of β_2-Microglobulin Amyloid Fibrils by Dimethylsulfoxide
- The Intrachain Disulfide Bond of β_2-Microglobulin Is Not Essential for the Immunoglobulin Fold at Neutral pH, but Is Essential for Amyloid Fibril Formation at Acidic pH
- 1P064 常磁性緩和促進を用いたβ2ミクログロブリンの中間状態構の解析(蛋白質-物性(安定性,折れたたみなど),第48回日本生物物理学会年会)
- 1P041 ヒトリポカリン型プロスタグランジンD合成酵素の脂溶性低分子に対する相互作用解析(蛋白質-構造機能相関,第48回日本生物物理学会年会)
- Structural Analysis of Amyloid-β Protein Fibrils Formed in Raft-Like Model Membranes
- 2P051 超音波による高速アミロイド線維形成反応(蛋白質-物性(安定性,折れたたみなど),第48回日本生物物理学会年会)
- 2P-052 SDSL-ESRを用いたアミロイド線維構造に関する研究(蛋白質-物性(安定性,折れたたみなど),第47回日本生物物理学会年会)
- 2P-048 重水素交換法を用いたアミロイド線維伸長機構の解析(蛋白質-物性(安定性,折れたたみなど),第47回日本生物物理学会年会)
- 2P-038 β2ミクログロブリンが形成するアミロイド線維の溶液NMRによる直接観察(蛋白質-物性(安定性,折れたたみなど),第47回日本生物物理学会年会)
- 1TP3-01 ウシβラクトグロブリン非天然中間体による折り畳み速度の促進機構(蛋白質-物性(安定性,折れたたみなど),第47回日本生物物理学会年会)
- 3P-007 β-ラクトグロブリンのαヘリックス中間体の寄与の解明(蛋白質・物性(3),第46回日本生物物理学会年会)
- 2P277 Promiscuous ligand binding of β-lactoglobulin allowed by hydrophobic interactions and structural variability(40. Membrane structure,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- Conformational Dynamics of β_2-Microglobulin Analyzed by Reduction and Reoxidation of the Disulfide Bond
- 2P-051 GM1ガングリオシドクラスターを介したアミロイドβタンパク質の凝集機構(蛋白質-物性(安定性,折れたたみなど),第47回日本生物物理学会年会)
- High-resolution Crystal Structure of β_2-Microglobulin Formed at pH 7.0
- Pioglitazone Lowers Systemic Asymmetric Dimethylarginine by Inducing Dimethylarginine Dimethylaminohydrolase in Rats
- 3P-042 ライン共焦点顕微鏡による蛋白質折り畳みのマイクロ秒分解一分子追跡(蛋白質-物性(安定性,折れたたみなど),第47回日本生物物理学会年会)
- 2P-050 一分子測定法による乳性蛋白質β-ラクトグロブリンの折り畳み過程の観測(蛋白質-物性(安定性,折れたたみなど),第47回日本生物物理学会年会)
- 1P-057 キャピラリー内トラップによる一分子の長時間観察 : 蛋白質の折り畳みへの応用(蛋白質-物性(安定性,折れたたみなど),第47回日本生物物理学会年会)
- 1P116 The Assessment of the New Apparatus for the Single Molecule Detection of Protein Folding(3. Protein folding and misfolding (1),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- Molecular Mechanism of Liposome Membrane Fusion Induced by Amphipathic Helical Peptides
- The β-Sheet Structure pH Dependence of the Core Fragments of β_2-Microglobulin Amyloid Fibrils
- 2P125 Relationship between pH-dependent conformational and stability changes of bovine β-lactoglobulin studied using NMR spectroscopy(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- An Experimental Study on the Interface Strength Between Titanium Mesh Cage and Vertebra in Reference to Vertebral Bone Mineral Density
- Peripheral Ameloblastoma Presenting as a Gingival Mass
- Effects of Stabilization in Extension in Cervical Ossification of a Posterior Longitudinal Ligament : A Case Report
- 3H1124 一分子計測法によるβ-ラクトグロブリンの観測(3H 蛋白質_物性4,日本生物物理学会第49回年会)
- 3D0948 CS-PCA法(化学シフト-主成分解析)を用いた蛋白質-多分子基質結合系の解析(3D 蛋白質_構造機能相関2,日本生物物理学会第49回年会)
- 2H1612 ヒト由来リポカリン型プロスタグランジンD合成酵素のフォールディング機構の解明(蛋白質_物性3,第49回日本生物物理学会年会)
- 1A1312 ガングリオシドクラスターを含むラフト様膜中でのAβのアミロイド形成機構(生体膜・人工膜1(構造・物性、ダイナミクス),第49回日本生物物理学会年会)
- 1D1648 ヘキサフルオロイソプロパノールによるIAPPのアミロイド線維形成(蛋白質_物性1,第49回日本生物物理学会年会)
- Mechanism of Amyloid β-Protein Aggregation Mediated by GM1 Ganglioside Clusters
- Low-Polarity Environment is Important for the Formation of Toxic Amyloid β Aggregates
- Visualization of polymorphism in apolipoprotein C-II amyloid fibrils
- 1E1436 Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation(Proteins: Property I,Oral Presentation,The 50th Annual Meeting of the Biophysical Society of Japan)
- Mechanisms of Ultrasonically Induced Fibrillation of Amyloid \beta_{1{\mbox{--}}40} Peptides
- Ultrasonication: An Efficient Agitation for Accelerating the Supersaturation-Limited Amyloid Fibrillation of Proteins
- A Large Calculus in the Parotid Duct
- Osteoma in Ethmoid Sinus: a case report
- 2P068 β2ミクログロブリンのアミロイド前駆状態の残余構造の特性化(01C.蛋白質:物性,ポスター,日本生物物理学会年会第51回(2013年度))
- 2P067 β_2-ミクログロブリンのアミロイド形成における様々な脂肪酸の効果(01C.蛋白質:物性,ポスター,日本生物物理学会年会第51回(2013年度))
- Dissolution of β2-Microglobulin Amyloid Fibrils by Dimethylsulfoxide
- Conformational Dynamics of β2-Microglobulin Analyzed by Reduction and Reoxidation of the Disulfide Bond