Structural Basis for the Inhibition of Truncated Islet Amyloid Polypeptide Aggregation by Cu(II): Insights into the Bioinorganic Chemistry of Type II Diabetes-Reference-Cited by-同舟云学术

Structural Basis for the Inhibition of Truncated Islet Amyloid Polypeptide Aggregation by Cu(II): Insights into the Bioinorganic Chemistry of Type II Diabetes

Published:2015-03-31 Issue:8 Volume:54 Page:3788-3796
ISSN:0020-1669
Container-title:Inorganic Chemistry
language:en
Short-container-title:Inorg. Chem.

Author:

Rivillas-Acevedo Lina¹²,Sánchez-López Carolina¹,Amero Carlos²,Quintanar Liliana¹

Affiliation:

1. Departamento de Química, Centro de Investigación y de Estudios Avanzados (Cinvestav), México, D.F., México

2. Centro de Investigaciones Químicas, Instituto de Investigación en Ciencias Básicas y Aplicadas, Universidad Autónoma del Estado de Morelos, Cuernavaca, Morelos México

Funder

Consejo Nacional de Ciencia y Tecnología

Publisher

American Chemical Society (ACS)

Subject

Inorganic Chemistry,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ic502945k

Reference58 articles.

1. Olefsky, J. M.Endocrinology;De Groot, L. J., Ed.Saunders:London, U.K., 1989; Vol.2, pp1369–1399.

2. THE RELATION OE DIABETES MELLITUS TO LESIONS OF THE PANCREAS. HYALINE DEGENERATION OF THE ISLANDS OE LANGERHANS

3. A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas

4. Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets

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