Role of monomer arrangement in the amyloid self-assembly-Reference-Cited by-同舟云学术

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Role of monomer arrangement in the amyloid self-assembly

Published:2015-03 Issue:3 Volume:1854 Page:218-228
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Portillo Alexander,Hashemi Mohtadin,Zhang Yuliang,Breydo Leonid,Uversky Vladimir N.,Lyubchenko Yuri L.

Funder

NSF

NIH

UNMC graduate student research fellowship

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference43 articles.

1. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid;Balbirnie;Proc. Natl. Acad. Sci. U. S. A.,2001

2. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated b-sheet structure for amyloid;Eisenberg;PNAS,2001

3. Structure of the cross-beta spine of amyloid-like fibrils;Nelson;Nature,2005

4. Plasticity of amyloid fibrils;Wetzel;Biochemistry,2007

5. Assembling amyloid fibrils from designed structures containing a significant amyloid beta-peptide fragment;Tjernberg;Biochem. J.,2002

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