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Investigation of post-translational modifications in type 2 diabetes

The investigation of post-translational modifications (PTMs) plays an important role for the study of type 2 diabetes. The importance of PTMs has been realized with the advancement of analytical techniques. The challenging detection and analysis of post-translational modifications is eased by differ...

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Detalles Bibliográficos
Autores principales: Chatterjee, Bhaswati, Thakur, Suman S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6154926/
https://www.ncbi.nlm.nih.gov/pubmed/30258344
http://dx.doi.org/10.1186/s12014-018-9208-y
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author Chatterjee, Bhaswati
Thakur, Suman S.
author_facet Chatterjee, Bhaswati
Thakur, Suman S.
author_sort Chatterjee, Bhaswati
collection PubMed
description The investigation of post-translational modifications (PTMs) plays an important role for the study of type 2 diabetes. The importance of PTMs has been realized with the advancement of analytical techniques. The challenging detection and analysis of post-translational modifications is eased by different enrichment methods and by high throughput mass spectrometry based proteomics studies. This technology along with different quantitation methods provide accurate knowledge about the changes happening in disease conditions as well as in normal conditions. In this review, we have discussed PTMs such as phosphorylation, N-glycosylation, O-GlcNAcylation, acetylation and advanced glycation end products in type 2 diabetes which have been characterized by high throughput mass spectrometry based proteomics analysis.
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spelling pubmed-61549262018-09-26 Investigation of post-translational modifications in type 2 diabetes Chatterjee, Bhaswati Thakur, Suman S. Clin Proteomics Review The investigation of post-translational modifications (PTMs) plays an important role for the study of type 2 diabetes. The importance of PTMs has been realized with the advancement of analytical techniques. The challenging detection and analysis of post-translational modifications is eased by different enrichment methods and by high throughput mass spectrometry based proteomics studies. This technology along with different quantitation methods provide accurate knowledge about the changes happening in disease conditions as well as in normal conditions. In this review, we have discussed PTMs such as phosphorylation, N-glycosylation, O-GlcNAcylation, acetylation and advanced glycation end products in type 2 diabetes which have been characterized by high throughput mass spectrometry based proteomics analysis. BioMed Central 2018-09-24 /pmc/articles/PMC6154926/ /pubmed/30258344 http://dx.doi.org/10.1186/s12014-018-9208-y Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Review
Chatterjee, Bhaswati
Thakur, Suman S.
Investigation of post-translational modifications in type 2 diabetes
title Investigation of post-translational modifications in type 2 diabetes
title_full Investigation of post-translational modifications in type 2 diabetes
title_fullStr Investigation of post-translational modifications in type 2 diabetes
title_full_unstemmed Investigation of post-translational modifications in type 2 diabetes
title_short Investigation of post-translational modifications in type 2 diabetes
title_sort investigation of post-translational modifications in type 2 diabetes
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6154926/
https://www.ncbi.nlm.nih.gov/pubmed/30258344
http://dx.doi.org/10.1186/s12014-018-9208-y
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