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Expression of small heat shock proteins after parasitization Small heat shock protein (sHSP) as molecular chaperones, protect proteins from being denatured during extreme conditions (Li et al.
9) Furthermore, BiP/GRP78 was found to be a member of the heat shock protein 70 family, whose emerging role at that time was as a molecular chaperone.
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.
Nevertheless, sHSPs have been added to the catalogue of molecular chaperones because they bind to denatured proteins as holding chaperones and thereby suppress the unintended interactions that may lead to the precipitation of aggregates.
Molecular Chaperones inhibit c-JNK pathway(Jun N terminal kinase pathway)--Inhibition of Neuronal cell death.
Molecular chaperones are a diverse set of proteins that mediate the correct folding, assembly, transport and degradation of other proteins.
Molecular chaperones such as heat-shock proteins (Hsps) act to rescue damaged proteins and prevent them from aggregating, thereby helping conserve the pool of existing proteins from irreversible damage (Parsell and Lindquist, 1993; Buchner, 1996; Fink, 1999).
Molecular chaperones, like their human counterparts, prevent inappropriate liaisons between their charges and tempters that would lead them astray.
We are pleased that the management team and Board of Directors of Orphazyme share our vision that molecular chaperones have the potential to improve the lives of patients worldwide.
Inhibitors of Molecular Chaperones as Therapeutic Agents
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.

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