Molecules with O-acetyl group protect protein glycation by acetylating lysine residues-Reference-Cited by-同舟云学术

Molecules with O-acetyl group protect protein glycation by acetylating lysine residues

Published:2016 Issue:70 Volume:6 Page:65572-65578
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Vannuruswamy Garikapati¹²³⁴⁵,Jagadeeshaprasad Mashanipalya G.¹²³⁴⁵,Kashinath K.⁶⁷⁵⁸³,Kesavan Suresh K.¹²³⁴⁵,Bhat Shweta¹²³⁴⁵,Korwar Arvind M.¹²³⁴⁵,Chougale Ashok D.¹²³⁴⁵,Boppana Ramanamurthy⁹¹⁰⁵,Reddy D. Srinivasa⁶⁷⁵⁸³,Kulkarni Mahesh J.¹²³⁴⁵

Affiliation:

1. Mass-Spectrometry and Proteomics Facility

2. Division of Biochemical Sciences

3. CSIR-National Chemical Laboratory

4. Pune-411008

5. India

6. Academy of Scientific and Innovative Research (AcSIR)

7. New Delhi

8. Organic Chemistry Division

9. National Center for Cell Science

10. Pune-411007

Abstract

In-vitro and in-vivo chemical proteomic studies of acetyl group molecules revealed that, O-acetyl molecules competitively inhibits the protein glycation by acetylating the lysine residues.

Funder

Council of Scientific and Industrial Research

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/RA/C6RA11313C

Reference26 articles.

1. The role of glycation cross-links in diabetic vascular stiffening

2. Advanced glycation end products and vascular inflammation: implications for accelerated atherosclerosis in diabetes

3. Advanced glycation end products: A nephrologist's perspective