chaperone

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Related to Molecular chaperone: Chaperone molecule
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Synonyms for chaperone

one who accompanies and supervises a young woman or gatherings of young people

accompany as a chaperone

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References in periodicals archive ?
Thus, molecular chaperones transiently associate with newly synthesized polypeptides, suppress inappropriate interactions between sticky hydrophobic amino acids, help them fold according to the Anfinsen's dogma, and then dissociate from the now correctly folded proteins, allowing them to function.
The major Hsp90 function is to serve as molecular chaperone interacting with multiple proteins (Mayer and Bukau 1999; Pearl and Prodromou 2000; Pearl et al.
Structural analysis of substrate binding by the molecular chaperone DnaK.
Small heat-shock proteins (sHSPs) represent an abundant and ubiquitous family of molecular chaperones.
One physiological adaptation to living in a stressful habitat like the intertidal is the synthesis of molecular chaperones (Feder and Hofmann, 1999; Hochachka and Somero, 2002).
Molecular chaperones, like their human counterparts, prevent inappropriate liaisons between their charges and tempters that would lead them astray.
Hsp90 is a molecular chaperone protein that was recently identified as essential for the proper expression and function of the ALK protein.
Editors Machajewski and Gao present students, academics, researchers, and professionals working in a wide variety of contexts with a collection of academic papers and scholarly articles that together provide a comprehensive examination of the field of molecular chaperone inhibition and its applications in pharmaceutical research.
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.
Then molecular chaperone appeared as an endogenous protein for proper folding and/or assembly of another protein or protein complex, (32) followed by chemical chaperone (33) and chaperone therapy.
Ganetespib, an investigational drug candidate, is a selective inhibitor of heat shock protein 90 (Hsp90), a molecular chaperone which controls the folding and activation of a number of client proteins that drive tumor development and progression, added the company.
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 present study has implicated participation of the molecular chaperone p26, and I focus on that possibility next.
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