Nucleation of β-rich oligomers and β-barrels in the early aggregation of human islet amyloid polypeptide-Reference-Cited by-同舟云学术

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Nucleation of β-rich oligomers and β-barrels in the early aggregation of human islet amyloid polypeptide

Published:2019-02 Issue:2 Volume:1865 Page:434-444
ISSN:0925-4439
Container-title:Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease

Author:

Sun Yunxiang,Kakinen Aleksandr,Xing Yanting,Pilkington Emily H.,Davis Thomas P.,Ke Pu Chun,Ding Feng

Funder

NSF

NIH

AFTAM Research Collaboration Award

ARC

Publisher

Elsevier BV

Subject

Molecular Biology,Molecular Medicine

Reference79 articles.

1. Common mechanisms of amyloid oligomer pathogenesis in degenerative disease;Glabe;Neurobiol. Aging,2006

2. Abeta(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease;Xiao;Nat. Struct. Mol. Biol.,2015

3. Solid-state NMR structure of a pathogenic fibril of full-length human alpha-synuclein;Tuttle;Nat. Struct. Mol. Biol.,2016

4. Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin);Wiltzius;Protein Sci.,2008

5. Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR;Luca;Biochemistry,2007

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