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Microbial molecular chaperones
2001Protein 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 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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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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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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