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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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).
The implication is if we can elevate the levels of this molecular chaperone, we may be able to handle the situation a little better," Cashikar said.
Orphazyme was formed in 2009 to develop molecular chaperone therapies to treat rare genetic lysosomal diseases.
We have attracted significant interest from several pharmaceutical companies as potential partners to advance development of our molecular chaperone programs, and we view clearance to resume arimoclomol clinical testing as a key step in moving these negotiations forward.
This opens new blockbuster opportunities for our molecular chaperone technology beyond the large neurodegenerative disease, stroke recovery and neuropathy markets that we have been investigating," said CytRx's President and CEO Steven A.
Above all, he wants to determine precisely how incorrect folding contributes to the origin of neurodegenerative diseases and why the molecular chaperones perform less well with increasing age.
By interacting with periplasmic molecular chaperones it is achieved that the assembly of pili is prevented or inhibited and thereby the infectivity of the bacteria is diminished.
The heat stress response entails the rapid production of heat stress proteins, which act as molecular chaperones to ensure that newly formed proteins are folded properly and misfolded proteins are removed from the cell.
Although intrinsically disordered protein are considered to be a crucial part of the proteome, most experimental and computational studies have focused on the contribution of intrinsic disorder to signaling and assembly of multi-domain complexes, leaving molecular chaperones as an unexplored niche.
Their topics include Varicella zoster virus transcriptional regulation and the roles of its immediate-early proteins, the role of the ICPO protein in counter-acting intrinsic cellular resistance to virus infection, translational control in Herpes simplex virus-infected cells, structure-function profiles of nine Varicella-zoster virus glycoproteins, nuclear egress and development of Herpes simplex virus, molecular chaperones and alphaherpesvirus infection, Varicella-zoster virus pathogenesis and latency, vaccines and new antiviral strategies against Herpes simplex virus, immunity and immune evasion strategies induced by Varicella zoster virus, the expression and functions of human alphaherpesvirus microRNAs, and oncolytic Herpes simplex virus vectors for cancer therapy.

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