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The molecular chaperone (hsp70) and its potential roles during dormancy and germination of Dictyostelium discoideum spores; correlation with action tyrosine phosphorylation.

, 2000
David Cervi
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Molecular Chaperones

Encyclopedia of Molecular Pharmacology, 2021
J. Valpuesta
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Mimicking Molecular Chaperones to Regulate Protein Folding

Advances in Materials, 2019
Folding and unfolding are essential ways for a protein to regulate its biological activity. The misfolding of proteins usually reduces or completely compromises their biological functions, which eventually causes a wide range of diseases including ...
Feihe Ma, C. Li, Yang Liu, Linqi Shi
semanticscholar   +1 more source

[Molecular chaperones].

Bioorganicheskaia khimiia, 2010
Chaperones are unique remodeling proteins that participate in a great number of intracellular processes and are involved in the correction of protein structure, the prevention of the aggregation of misfolded proteins, the destruction of protein aggregates, and also the unfolding of native protein targets for their translocation across a membrane.
E E, Mel'nikov, T V, Rotanova
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Microbial molecular chaperones

2001
Protein folding in the cell, long thought to be a spontaneous process, in fact often requires the assistance of molecular chaperones. This is thought to be largely because of the danger of incorrect folding and aggregation of proteins, which is a particular problem in the crowded environment of the cell.
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MOLECULAR CHAPERONES

Annual Review of Biochemistry, 1991
R J, Ellis, S M, van der Vies
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Molecular chaperones and disease

Inflammation Research, 1996
Molecular chaperones are intracellular protein-folding proteins which form part of an ancient cellular response to stress called the heat shock response. They have been the focus for attention during the last decade because of the discovery of their vital role in cell functioning.
B, Henderson, S P, Nair, A R, Coates
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Aging and molecular chaperones

Experimental Gerontology, 2003
Chaperone function plays a key role in sequestering damaged proteins and in repairing proteotoxic damage. Chaperones are induced by environmental stress and are called as stress or heat shock proteins. Here, we summarize the current knowledge about protein damage in aged organisms, about changes in proteolytic degradation, chaperone expression and ...
Csaba, Soti, Péter, Csermely
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Molecular Chaperones ☆

2013
J.L. Camberg, S.M. Doyle, D.M. Johnston, S. Wickner   +3 more
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Dynamism in Molecular Chaperones

Journal of Molecular Biology, 2011
John A. Carver ; http://www.journals.elsevier.com/journal-of-molecular-biology/
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