[Chaperone proteins--essential proteins for cellular activity].
Molecular chaperones are an ubiquitous, abundant and highly conserved group of proteins which bind and stabilize proteins at intermediate stages of folding, assembly, translocation across membranes and degradation. They first came to attention because of their specific induction during the cellular response of all organisms to heat shock, but are now known to be constitutively and abundantly expressed in the absence of any stress. Despite the obvious importance of stress responses, only recently has scrutiny focused on the role of heat shock proteins in the control of disease pathology. Knowledge about Hsp functions in bacteria is much further advanced than in eukaryotes, but already some hints of Hsp involvement in mammalian diseases have emerged.
Sandovici
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Disciplina de Genetică umană, Facultatea de Medicină, Universitatea de Medicină şi Farmacie Gr. T. Popa, Iaşi.
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D000818:Animals; D002318:Cardiovascular Diseases / Q000503:physiopathology; D002468:Cell Physiological Phenomena; D003593:Cytoplasm / Q000502:physiology; D006801:Humans; D018832:Molecular Chaperones / Q000145:classification / Q000494:pharmacology / Q000502:physiology*; D010455:Peptides / Q000502:physiology
D018832:Molecular Chaperones; D010455:Peptides