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Linking hIAPP misfolding and aggregation with type 2 diabetes mellitus: a structural perspective

Hassan, Shahab; White, Kenneth; Terry, Cassandra; (2022) Linking hIAPP misfolding and aggregation with type 2 diabetes mellitus: a structural perspective. Bioscience Reports , 42 (5) , Article BSR20211297. 10.1042/BSR20211297. Green open access

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Abstract

There are over 40 identified human disorders that involve certain proteins folding incorrectly, accumulating in the body causing damage to cells and organs and causing disease. Type 2 Diabetes Mellitus (T2DM) is one of these protein misfolding disorders (PMDs) and involves human islet amyloid polypeptide (hIAPP) misfolding and accumulating in parts of the body, primarily in the pancreas, causing damage to islet cells and affecting glucose regulation. In this review, we have summarised our current understanding of what causes hIAPP to misfold, what conformations are found in different parts of the body with a particular focus on what is known about the structure of hIAPP and how this links to T2DM. Understanding the molecular basis behind these misfolding events is essential for understanding the role of hIAPP to develop better therapeutics since type 2 diabetes currently affects over 4.9 million people in the United Kingdom alone and is predicted to increase as our population ages.

Type: Article
Title: Linking hIAPP misfolding and aggregation with type 2 diabetes mellitus: a structural perspective
Location: England
Open access status: An open access version is available from UCL Discovery
DOI: 10.1042/BSR20211297
Publisher version: https://doi.org/10.1042/BSR20211297
Language: English
Additional information: Copyright © 2022 The Author(s). This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (http://creativecommons.org/licenses/by/4.0/).
Keywords: amyloid, diabetes, hIAPP
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > UCL Institute of Prion Diseases
URI: https://discovery.ucl.ac.uk/id/eprint/10195750
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