Topological investigation of amyloid fibrils obtained from β2-microglobulin-Reference-Cited by-同舟云学术

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Topological investigation of amyloid fibrils obtained from β2-microglobulin

Published:2009-01-01 Issue:10 Volume:11 Page:2362-2369
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Monti Maria,Principe Serena,Giorgetti Sofia,Mangione Palma,Merlini Gianpaolo,Clark Anne,Bellotti Vittorio,Amoresano Angela,Pucci Piero

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference30 articles.

1. Binding of α-actinin to titin: Implications for Z-disk assembly;Atkinson;Biochemistry,2000

2. β2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils;Bellotti;Eur. J. Biochem.,1998

3. Conformational changes in human hepatitis C virus NS3 protease upon binding of product-based inhibitors;Bianchi;Biochemistry.,1999

4. Detection of two partially structured species in the folding process of the amyloidogenic protein β 2-microglobulin;Chiti;J. Mol. Biol.,2001a

5. A partially structured species of β 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis;Chiti;J. Biol. Chem.,2001b

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1. Predicting stable binding modes from simulated dimers of the D76N mutant of β2-microglobulin;2021-07-15

2. Predicting stable binding modes from simulated dimers of the D76N mutant of β2-microglobulin;Computational and Structural Biotechnology Journal;2021

3. Proline isomerization effects in the amyloidogenic protein β2-microglobulin;Physical Chemistry Chemical Physics;2021

4. The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations;Frontiers in Molecular Biosciences;2020-09-29

5. MS-based conformation analysis of recombinant proteins in design, optimization and development of biopharmaceuticals;Methods;2018-07

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