Lysine acetylation of Hsp16.3: Effect on its structure, chaperone function and influence towards the growth of Mycobacterium tuberculosis-Reference-Cited by-同舟云学术

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Lysine acetylation of Hsp16.3: Effect on its structure, chaperone function and influence towards the growth of Mycobacterium tuberculosis

Published:2024-05 Issue: Volume:268 Page:131763
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Barik Subhashree,Panda Alok Kumar,Biswas Viplov Kumar,Das Sheetal,Chakraborty Ayon,Beura Shibangini,Modak Rahul,Raghav Sunil Kumar,Kar Rajiv K.,Biswas Ashis

Funder

Science and Engineering Research Board

Indian Council of Medical Research

Publisher

Elsevier BV

Reference51 articles.

1. Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation;Chang;J. Biol. Chem.,1996

2. Mycobacterium tuberculosis heat-shock protein 16.3 activates macrophages probably through TLR4/MyD88 pathway;Qin;Inflammation,2017

3. Impact of nano- particles on amyloid beta-induced Alzheimer's disease, tuberculosis, leprosy and cancer: a systematic review;Chakraborty;Biosci. Rep.,2023

4. Role of ATP-small heat shock protein interaction in human diseases;Nandi;Front. Mol. Biosci.,2022

5. Global Tuberculosis Report 2022;G.J.G.T.R. WHO,2022

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