Population of Nonnative States of Lysozyme Variants Drives Amyloid Fibril Formation-Reference-Cited by-同舟云学术

Population of Nonnative States of Lysozyme Variants Drives Amyloid Fibril Formation

Published:2011-04-29 Issue:20 Volume:133 Page:7737-7743
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Buell Alexander K.¹,Dhulesia Anne²,Mossuto Maria F.³,Cremades Nunilo²,Kumita Janet R.²,Dumoulin Mireille⁴,Welland Mark E.¹,Knowles Tuomas P. J.²,Salvatella Xavier³⁵,Dobson Christopher M.²

Affiliation:

1. Nanoscience Centre, University of Cambridge, 11 JJ Thomson Avenue, Cambridge CB3 0FF, United Kingdom

2. Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom

3. Institute for Research in Biomedicine, Baldiri Reixac 10, 08028 Barcelona, Spain

4. Centre for Protein Engineering, University of Liège, Sart Tilman, 4000 Liège, Belgium

5. Institució Catalana de Recerca i Estudis Avançats (ICREA), Passeig Lluis Companys 23, 08010 Barcelona, Spain

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja109620d

Reference44 articles.

1. Human lysozyme gene mutations cause hereditary systemic amyloidosis

2. The stability and folding process of amyloidogenic mutant human lysozymes

3. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

4. Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme

5. Reduced Global Cooperativity is a Common Feature Underlying the Amyloidogenicity of Pathogenic Lysozyme Mutations

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