The N-terminal fragment of human islet amyloid polypeptide is non-fibrillogenic in the presence of membranes and does not cause leakage of bilayers of physiologically relevant lipid composition-Reference-Cited by-同舟云学术

The N-terminal fragment of human islet amyloid polypeptide is non-fibrillogenic in the presence of membranes and does not cause leakage of bilayers of physiologically relevant lipid composition

Published:2010-09 Issue:9 Volume:1798 Page:1805-1811
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Khemtémourian Lucie,Engel Maarten F.M.,Liskamp Rob M.J.,Höppener Jo W.M.,Killian J. Antoinette

Funder

European Commission

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference35 articles.

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2. Islet amyloid polypeptide inhibits glucagon release and exerts a dual action on insulin release from isolated islets;Akesson;Regul. Pept.,2003

3. Amylin, food intake, and obesity;Reda;Obes. Res.,2002

4. Inhibition of central amylin signaling increases food intake and body adiposity in rats;Rushing;Endocrinology,2001

5. The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies;Porat;Biochemistry,2003

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