Three-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR Spectroscopy-Reference-Cited by-同舟云学术

Three-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR Spectroscopy

Published:2009-05-20 Issue:23 Volume:131 Page:8252-8261
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Nanga Ravi Prakash Reddy¹,Brender Jeffrey R.¹,Xu Jiadi¹,Hartman Kevin¹,Subramanian Vivekanandan¹,Ramamoorthy Ayyalusamy¹

Affiliation:

1. Department of Chemistry and Biophysics, University of Michigan, Ann Arbor, Michigan 48109, and Structural Biology/NMR Spectroscopy, U.S. Food and Drug Administration, Bethesda, Maryland 20892

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja9010095

Reference79 articles.

1. Islet Amyloid in Type 2 Diabetes, and the Toxic Oligomer Hypothesis

2. Membrane interaction of islet amyloid polypeptide

3. Recent Insights in Islet Amyloid Polypeptide-Induced Membrane Disruption and Its Role inβ-Cell Death in Type 2 Diabetes Mellitus

4. Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane

5. Amyloid ion channels: A common structural link for protein-misfolding disease

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