molecular chaperone


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Related to molecular chaperone: Chaperone molecule

molecular chaperone

n.
References in periodicals archive ?
The host laboratory has purified full-length BRCA2 protein and shown that it facilitates RAD51-mediated HR by acting as a molecular chaperone for RAD51 filament formation.
Hsp90 is an abundant and highly specialized molecular chaperone that plays many important roles in human biology and medicine.
Ahmed Chadli, a researcher in the Molecular Chaperone Program at the GRU Cancer Center and senior author of the study.
A molecular chaperone briefly accompanies its substrate protein and makes sure that the substrate makes no inappropriate inter- and intramolecular interactions," writes Witt (biochemistry and molecular biology, Louisiana State University Health Sciences Center) in his introduction.
They are believed to be involved in the initiation step of translation at high temperature and possibly a molecular chaperone.
In the future the experiments will also explore the molecular method of action of ionomycin, whether it is a pore or a molecular chaperone, and measure the change metabolic activity of the cells once exposed to ionomycin.
Like an overprotective human caretaker, the molecular chaperone needs a nudge before it lets go.
Hsp90 is a molecular chaperone protein that was recently identified as essential for the proper expression and function of the ALK protein.
The research in the Fisher lab is focused on taking the vast knowledge describing molecular chaperone function and applying this data to establish broad based research tools and approaches to eventually aid in the identification and design of the next generation of small molecule protein drugs to ameliorate Protein Folding Diseases.
Topics addressed in the 14 included presentations are the history of the understanding of cell stress; systems biology of molecular chaperone networks; unusual cellular disposition of the mitochondrial chaperones Hsp60, Hsp70, and Hsp10; cell surface molecular chaperones as endogenous modulators of innate immune response; cell stress proteins in extracellular fluids; Hsp60 and the immune system; novel immunotherapies from cell stress proteins; cell stress proteins as modulators of bacteria-host interactions; chaperonin 60 and microphage activation; extracellular functions of thioredoxin; Hsp27 as an anti-inflammatory and immunomodulatory stress protein acting to dampen immune function; and binding immunoglobulin protein as a potential new therapy for the treatment of rheumatoid arthritis.
The Hsp90 molecular chaperone controls the folding of key signaling molecules required to maintain normal cell function in many organs, including the retina.

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