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Molecular chaperones: Pathways and networks
Some proteins synthesized by growing eukaryotic cells are transferred along unidirectional pathways of molecular chaperones until the risk of aggregation has decreased and they can be released safely.
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Impact of ovariectomy on neurotransmitter receptors BDNF/TrkB and endoplasmic reticulum molecular chaperones in rat hypoglossal nucleus. [PDF]
Sleep Biol RhythmsLu H, Wu Q, Liu Z, Li S.
europepmc +1 more source
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.
Peter A. Lund +3 more
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Molecular chaperones and photoreceptor function [PDF]
Progress in Retinal and Eye Research, 2008 Molecular chaperones facilitate and regulate protein conformational change within cells. This encompasses many fundamental cellular processes: including the correct folding of nascent chains; protein transport and translocation; signal transduction and ...
Michael E. Cheetham, Nele Schwarz
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Molecular Chaperones in the Kidney
Annual Review of Physiology, 2002▪ Abstract The normal milieu of the kidney includes hypoxia, large osmotic fluxes, and an enormous amount of fluid/solute reabsorption. Renal adaptation to these conditions requires a host of molecular chaperones that stabilize protein conformation, target nascent proteins to their final intracellular destination, and prevent protein aggregation ...
Steven C, Borkan, Steven R, Gullans
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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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