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Molecular chaperones and the cytoskeleton
Journal of Cell Science, 1997ABSTRACT Heat shock proteins, first observed because they are preferentially synthesized by organisms exposed to heat or other physiological stress, are also synthesized constitutively. These proteins are divided into several families, namely, HSP100, 90, 70, 60 (chaperonin), and the small heat shock/α-crystallin proteins.
P, Liang, T H, MacRae
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Molecular chaperones and disease
Inflammation Research, 1996Molecular 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, 2003Chaperone 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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Dynamism in Molecular Chaperones
Journal of Molecular Biology, 2011John A. Carver ; http://www.journals.elsevier.com/journal-of-molecular-biology/
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Prions and molecular chaperones
1993Molecular chaperones are proteins involved in the folding of other proteins. Among these chaperones, some are involved in their own folding (auto-chaperones). A question arises: what is the mechanism of the chaperone folding catalysis? A model for protein folding that uses the thermodynamics of irreversible processes and statistical mechanics to ...
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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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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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Molecular Chaperones: Panning for chaperone-binding peptides
Current Biology, 1994Experiments designed to define the substrate-binding preferences of the molecular chaperone BiP show that bound peptides are characterized by a heptameric motif with alternating hydrophobic residues.
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