The role of disulfide bond in the amyloidogenic state of β2-microglobulin studied by heteronuclear NMR-Reference-Cited by-同舟云学术

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The role of disulfide bond in the amyloidogenic state of β2-microglobulin studied by heteronuclear NMR

Published:2009-01-01 Issue:9 Volume:11 Page:2218-2229
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Katou Hidenori,Kanno Takashi,Hoshino Masaru,Hagihara Yoshihisa,Tanaka Hiroyuki,Kawai Tomoji,Hasegawa Kazuhiro,Naiki Hironobu,Goto Yuji

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference51 articles.

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2. Structural and dynamic characterization of an unfolded state of polar apo-plastocyanin formed under nondenaturing conditions;Bai;Protein Sci.,2001

3. Structure of the human class I histocompatibility antigen, HLA-A2;Bjorkman;Nature,1987

4. Toward understanding insulin fibrillation;Brange;J. Pharm. Sci.,1997

5. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases;Bucciantini;Nature,2002

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