Effect of methylglyoxal modification on the structure and properties of human small heat shock protein HspB6 (Hsp20)-Reference-Cited by-同舟云学术

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Effect of methylglyoxal modification on the structure and properties of human small heat shock protein HspB6 (Hsp20)

Published:2016-04-09 Issue:4 Volume:21 Page:617-629
ISSN:1355-8145
Container-title:Cell Stress and Chaperones
language:en
Short-container-title:Cell Stress and Chaperones

Author:

Muranova Lydia K.,Perfilov Maxim M.,Serebryakova Marina V.,Gusev Nikolai B.

Funder

Russian Science Foundation

Russian Foundation for Basic Research (RU)

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s12192-016-0686-4.pdf

Reference54 articles.

1. Bakthisaran R, Tangirala R, Rao CM (2015) Small heat shock proteins: role in cellular functions and pathology. Biochim Biophys Acta 1854:291–319. doi: 10.1016/j.bbapap.2014.12.019

2. Beall A et al (1999) The small heat shock-related protein, HSP20, is phosphorylated on serine 16 during cyclic nucleotide-dependent relaxation. J Biol Chem 274:11344–11351

3. Bento CF, Marques F, Fernandes R, Pereira P (2010) Methylglyoxal alters the function and stability of critical components of the protein quality control. PLoS One 5:e13007. doi: 10.1371/journal.pone.0013007

4. Bose T, Bhattacherjee A, Banerjee S, Chakraborti AS (2013) Methylglyoxal-induced modifications of hemoglobin: structural and functional characteristics. Arch Biochem Biophys 529:99–104. doi: 10.1016/j.abb.2012.12.001

5. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254

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