scholarly journals A Novel Mechanism for Small Heat Shock Proteins to Function as Molecular Chaperones

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Kaiming Zhang ◽  
Anastasia N. Ezemaduka ◽  
Zhao Wang ◽  
Hongli Hu ◽  
Xiaodong Shi ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

scholarly journals Structural and functional homology between periplasmic bacterial molecular chaperones and small heat shock proteins

1995 ◽  
Vol 11 (4) ◽  
pp. 265-272 ◽  
Author(s):  
Vladimir P. Zav'yalov ◽  
Galina A. Zav'yalova ◽  
Alexander I. Denesyuk ◽  
Matthias Gaestel ◽  
Timo Korpela
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Small Heat Shock Proteins ◽  
Functional Homology ◽  
Shock Proteins

scholarly journals Small heat shock proteins are molecular chaperones.

1993 ◽  
Vol 268 (3) ◽  
pp. 1517-1520 ◽  
Author(s):  
U. Jakob ◽  
M. Gaestel ◽  
K. Engel ◽  
J. Buchner
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

scholarly journals Molecular chaperones: Small heat shock proteins in the limelight

1999 ◽  
Vol 9 (3) ◽  
pp. R103-R105 ◽  
Author(s):  
Paul van den IJssel ◽  
David G. Norman ◽  
Roy A. Quinlan
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

The function of small heat-shock proteins and their implication in proteostasis

2016 ◽  
Vol 60 (2) ◽  
pp. 163-172 ◽  
Author(s):  
Annika Strauch ◽  
Martin Haslbeck
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Small Heat Shock Proteins ◽  
Independent Manner ◽  
Native Proteins ◽  
Domains Of Life ◽  
Broad Variety ◽  
Chaperone Network ◽  
Shock Proteins

All organisms rely on a conserved cellular machinery supporting and controlling the life cycle of proteins: the proteostasis network. Within this network, the main players that determine the fate of proteins are molecular chaperones, the ubiquitin–proteasome and the lysosome–autophagy systems. sHsps (small heat-shock proteins) represent one family of molecular chaperones found in all domains of life. They prevent irreversible aggregation of unfolded proteins and maintain proteostasis by stabilizing promiscuously a variety of non-native proteins in an ATP-independent manner. In the cellular chaperone network, sHsps act as the first line of defence and keep their substrates in a folding-competent state until they are refolded by downstream ATP-dependent chaperone systems. Besides this interaction with unfolding substrates upon stress, sHsps show a different mode of binding for specific clients which are also recognized under physiological conditions. In vertebrates, sHsps are especially needed to maintain the refractive index of the eye lens. Additionally, sHsps are linked to a broad variety of diseases such as myopathies and neuropathies. The most striking feature of sHsps is their ability to form dynamic ensembles of higher oligomers. The activity of sHsps is regulated by changes in the composition of the ensembles.

In Vitro Holdase Activity of E. coli Small Heat-Shock Proteins IbpA, IbpB and IbpAB: A Biophysical Study with Some Unconventional Techniques

2014 ◽  
Vol 21 (6) ◽  
pp. 564-571 ◽  
Author(s):  
Sourav Roy ◽  
Monobesh Patra ◽  
Suman Nandy ◽  
Milon Banik ◽  
Rakhi Dasgupta ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
E Coli ◽  
Biophysical Study ◽  
Shock Proteins

The Small Heat-shock Proteins IbpA and IbpB in E. coli: The Small Ones With a Big Role

2016 ◽  
Vol 9 (2) ◽  
pp. 84-96
Author(s):  
Sanchari Bhattacharjee ◽  
Rakhi Dasgupta ◽  
Angshuman Bagchi
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
E Coli ◽  
Shock Proteins
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