Rifampicin Does Not Prevent Amyloid Fibril Formation by Human Islet Amyloid Polypeptide but Does Inhibit Fibril Thioflavin-T Interactions: Implications for Mechanistic Studies of β-Cell Death-Reference-Cited by-同舟云学术

Rifampicin Does Not Prevent Amyloid Fibril Formation by Human Islet Amyloid Polypeptide but Does Inhibit Fibril Thioflavin-T Interactions: Implications for Mechanistic Studies of β-Cell Death

Published:2008-05-06 Issue:22 Volume:47 Page:6016-6024
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Meng Fanling¹,Marek Peter¹,Potter Kathryn J.¹,Verchere C. Bruce¹,Raleigh Daniel P.¹

Affiliation:

1. Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400, Department of Pathology and Laboratory Medicine and Child and Family Research Institute, University of British Columbia, Vancouver, BC, Canada V5Z 4H4, and Graduate Program in Biochemistry and Structural Biology and Graduate Program in Biophysics, State University of New York at Stony Brook, Stony Brook, New York 11794-3400

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi702518m

Reference51 articles.

1. Protein Misfolding, Functional Amyloid, and Human Disease

2. Protein folding and misfolding: a paradigm of self–assembly and regulation in complex biological systems

3. Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes.

4. Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells.

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