Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide
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Title
Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide
Authors
Keywords
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Journal
CHEMICAL COMMUNICATIONS
Volume 49, Issue 32, Pages 3339
Publisher
Royal Society of Chemistry (RSC)
Online
2013-03-06
DOI
10.1039/c3cc40383a
References
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Related references
Note: Only part of the references are listed.- Membrane Disruption and Early Events in the Aggregation of the Diabetes Related Peptide IAPP from a Molecular Perspective
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- Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus
- (2011) Per Westermark et al. PHYSIOLOGICAL REVIEWS
- The Molecular Basis of Distinct Aggregation Pathways of Islet Amyloid Polypeptide
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- Human pro-islet amyloid polypeptide (ProIAPP1–48) forms amyloid fibrils and amyloid spherulites in vitro
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- Role of Zinc in Human Islet Amyloid Polypeptide Aggregation
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- NMR Spectroscopic Investigation of Early Events in IAPP Amyloid Fibril Formation
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- Three-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR Spectroscopy
- (2009) Ravi Prakash Reddy Nanga et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Association of Highly Compact Type II Diabetes Related Islet Amyloid Polypeptide Intermediate Species at Physiological Temperature Revealed by Diffusion NMR Spectroscopy
- (2009) Ronald Soong et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Sedimentation Studies on Human Amylin Fail to Detect Low-Molecular-Weight Oligomers
- (2008) Sara M. Vaiana et al. BIOPHYSICAL JOURNAL
- Amyloid Fiber Formation and Membrane Disruption are Separate Processes Localized in Two Distinct Regions of IAPP, the Type-2-Diabetes-Related Peptide
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- Copper(II) inhibits the formation of amylin amyloid in vitro
- (2007) Benjamin Ward et al. JOURNAL OF INORGANIC BIOCHEMISTRY
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