Kinetic and Conformational Insights into Islet Amyloid Polypeptide Self-Assembly Using a Biarsenical Fluorogenic Probe-Reference-Cited by-同舟云学术

Kinetic and Conformational Insights into Islet Amyloid Polypeptide Self-Assembly Using a Biarsenical Fluorogenic Probe

Published:2018-02-12 Issue:2 Volume:29 Page:517-527
ISSN:1043-1802
Container-title:Bioconjugate Chemistry
language:en
Short-container-title:Bioconjugate Chem.

Author:

Quittot Noé¹,Sebastiao Mathew¹,Al-Halifa Soultan¹,Bourgault Steve¹^ORCID

Affiliation:

1. Department of Chemistry, Quebec Network for Research on Protein Function, Engineering and Applications, PROTEO, University of Québec in Montreal, C.P. 8888, Succursale Centre-Ville, Montreal, Québec H3C 3P8, Canada

Funder

Fonds de Recherche du Qu?bec - Nature et Technologies

Natural Sciences and Engineering Research Council of Canada

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry,Pharmaceutical Science,Pharmacology,Biomedical Engineering,Bioengineering,Biotechnology

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.bioconjchem.7b00827

Reference64 articles.

1. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

2. Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1

3. Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity

4. Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis

5. Structural Classification of Toxic Amyloid Oligomers

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