molecular chaperone


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Related to molecular chaperone: Chaperone molecule

molecular chaperone

[mə′lək·yə·lər ′shap·ə‚rän]
(cell and molecular biology)
Any of a class of cellular proteins involved in correct folding of certain polypeptide chains and their assembage into an oligomer.
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Heat shock protein 70 (HSP70) are the molecular chaperones that assist in folding of newly synthesized polypeptides, refolding of misfolded proteins and translocation of proteins through biological membranes, and in addition have regulatory functions in signal transduction, cell cycle and apoptosis.
Chaperonins form a sub-group of molecular chaperones and 10-kDa antigen has homology with the GroES or chaperonin-10 (Cpn l0) family of heat shock proteins (17-19).
Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones.
Since molecular chaperones have multiple cellular functions (Lindquist, 1986; Parsell and Lindquist, 1993), the process of molting could potentially elicit an increase in Hsp levels and either confound or interact with the effects of temperature.
Protein chaperone (endogenous) = molecular chaperone induced by small molecules Target diseases: Neurodegenerative diseases (polyQ diseases, tauopathies) Myopathies (myosin chaperone) Wilson disease (copper chaperone)
An alternative interpretation would be that p26 undergoes self-aggregation and is then chaperoned back to its native state by itself or by some other molecular chaperone, such as hsp70.
It was known that the molecular chaperone, HspB1, was present in the hallmark plaque of Alzheimer's patients but its role remained a mystery.
Our results demonstrate that, for Homarus americanus, (1) exposure to 50% or 150% seawater significantly alters hemolymph osmolarity, (2) hypo- and hyper-osmotic stress both can significantly elevate molecular chaperone gene expression, (3) osmotic effects on molecular chaperone mRNA levels may differ depending on duration of stress and tissue, and (4) polyubiquitin gene expression is also significantly increased by osmotic stress and similarly can differ on the basis of exposure duration and tissue.
Opportunity to develop molecular chaperone therapy for the treatment of lysosomal storage diseases -
The original finding that lens [Alpha]-crystallin could function as a molecular chaperone, protecting many proteins against heat denaturation, was made by Horwitz (1).
Heat Shock Protein 90 (Hsp90) is a molecular chaperone that mediates the post-translational stability of its protein substrates, many of which are validated oncogenes.
In addition, CytRx is developing two drug candidates based on its industry-leading molecular chaperone technology, which aims to repair or degrade misfolded proteins associated with disease.

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