Large potentials of small heat shock proteins

EV Mymrikov, AS Seit-Nebi… - Physiological …, 2011 - journals.physiology.org
Modern classification of the family of human small heat shock proteins (the so-called HSPB)
is presented, and the structure and properties of three members of this family are analyzed …

Extracellular release and signaling by heat shock protein 27: role in modifying vascular inflammation

Z Batulan, VK Pulakazhi Venu, Y Li… - Frontiers in …, 2016 - frontiersin.org
Heat shock protein 27 (HSP27) is traditionally viewed as an intracellular chaperone protein
with anti-apoptotic properties. However, recent data indicate that a number of heat shock …

Local unfolding of the HSP27 monomer regulates chaperone activity

TR Alderson, J Roche, HY Gastall, DM Dias… - Nature …, 2019 - nature.com
The small heat-shock protein HSP27 is a redox-sensitive molecular chaperone that is
expressed throughout the human body. Here, we describe redox-induced changes to the …

Site-specific glycation of human heat shock protein (Hsp27) enhances its chaperone activity

S Mukherjee, DP Vogl, CFW Becker - ACS Chemical Biology, 2023 - ACS Publications
Non-enzymatic posttranslational modifications are believed to affect at least 30% of human
proteins, commonly termed glycation. Many of these modifications are implicated in various …

Bmal1 regulates the redox rhythm of HSPB1, and homooxidized HSPB1 attenuates the oxidative stress injury of cardiomyocytes

X Liu, W Xiao, Y Jiang, L Zou, F Chen… - Oxidative medicine …, 2021 - Wiley Online Library
Oxidative stress is the main cause of acute myocardial infarction (AMI), which is related to
the disorder of the regulation of Bmal1 on the redox state. HSPB1 form homologous …

Identification of potential protein targets of isothiocyanates by proteomics

L Mi, BL Hood, NA Stewart, Z Xiao… - Chemical research in …, 2011 - ACS Publications
Isothiocyanates (ITCs), such as phenethyl isothiocyanate (PEITC) and sulforaphane (SFN),
are effective cancer chemopreventive compounds. It is believed that the major mechanism …

[HTML][HTML] Peeking from behind the veil of enigma: emerging insights on small heat shock protein structure and function

RE Klevit - Cell Stress and Chaperones, 2020 - Elsevier
This is a short paper on new ways to think about the structure and function of small heat
shock proteins (sHSPs), perhaps the most enigmatic family among protein chaperones. The …

[HTML][HTML] Pro-inflammatory cytokines downregulate Hsp27 and cause apoptosis of human retinal capillary endothelial cells

RB Nahomi, A Palmer, KM Green, PE Fort… - … et Biophysica Acta (BBA …, 2014 - Elsevier
The formation of acellular capillaries in the retina, a hallmark feature of diabetic retinopathy,
is caused by apoptosis of endothelial cells and pericytes. The biochemical mechanism of …

Heat shock protein-mediated protection against cisplatin-induced hair cell death

TG Baker, S Roy, CS Brandon, IK Kramarenko… - Journal of the …, 2015 - Springer
Cisplatin is a highly successful and widely used chemotherapy for the treatment of various
solid malignancies in both adult and pediatric patients. Side effects of cisplatin treatment …

[HTML][HTML] Key Role of Phosphorylation in Small Heat Shock Protein Regulation via Oligomeric Disaggregation and Functional Activation

ZB Sluzala, A Hamati, PE Fort - Cells, 2025 - mdpi.com
Heat shock proteins (HSPs) are essential molecular chaperones that protect cells by aiding
in protein folding and preventing aggregation under stress conditions. Small heat shock …