Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human γD-Crystallin Protein-Reference-Cited by-同舟云学术

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Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human γD-Crystallin Protein

Published:2016-02 Issue:8 Volume:291 Page:4226-4235
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Garcia-Manyes Sergi,Giganti David,Badilla Carmen L.,Lezamiz Ainhoa,Perales-Calvo Judit,Beedle Amy E.M.,Fernández Julio M.

Funder

Biotechnology and Biological Sciences Research Council

Seventh Framework Programme

Engineering and Physical Sciences Research Council

Royal Society

National Institutes of Health

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference56 articles.

1. Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis;Mulligan;Proteins,2013

2. α1-antitrypsin deficiency: a model for conformational diseases;Carrell;N. Engl. J. Med,2002

3. Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer;Yamasaki;EMBO Rep,2011

4. 3D domain swapping: as domains continue to swap;Liu;Protein Sci,2002

5. Protein Misfolding Diseases: Current and Emerging Principles and Therapies;Wang,2010

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