Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry-Reference-Cited by-同舟云学术

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Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry

Published:2015 Issue:20 Volume:140 Page:6990-6999
ISSN:0003-2654
Container-title:The Analyst
language:en
Short-container-title:Analyst

Author:

Young Lydia M.¹²³⁴,Mahood Rachel A.¹²³⁴,Saunders Janet C.¹²³⁴,Tu Ling-Hsien⁵⁶⁷⁸,Raleigh Daniel P.⁵⁶⁷⁸⁹,Radford Sheena E.¹²³⁴,Ashcroft Alison E.¹²³⁴

Affiliation:

1. Astbury Centre for Structural Molecular Biology

2. School of Molecular and Cellular Biology

3. University of Leeds

4. UK

5. Department of Chemistry

6. Stony Brook University

7. Stony Brook

8. USA

9. Research Department of Structural and Molecule Biology

Abstract

The precise molecular mechanisms by which different peptides and proteins assemble into highly ordered amyloid deposits remain elusive.

Funder

Biotechnology and Biological Sciences Research Council

Publisher

Royal Society of Chemistry (RSC)

Subject

Electrochemistry,Spectroscopy,Environmental Chemistry,Biochemistry,Analytical Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/AN/C5AN00865D

Reference69 articles.

1. Nomenclature 2014: Amyloid fibril proteins and clinical classification of the amyloidosis

2. IAPP Mimic Blocks Aβ Cytotoxic Self-Assembly: Cross-Suppression of Amyloid Toxicity of Aβ and IAPP Suggests a Molecular Link between Alzheimer's Disease and Type II Diabetes

3. Amyloid in the islets of Langerhans: Thoughts and some historical aspects

4. Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus

5. β-Cell Failure in Type 2 Diabetes: Postulated Mechanisms and Prospects for Prevention and Treatment

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