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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Supervising the fold: functional principles of molecular chaperones. FASEB J 1996:10(1): 10-19.
Outside of their primary function of protein refolding, molecular chaperones also play important roles in cellular processes such as guiding misfolded proteins for degradation through the ubiquitin-proteasome system (UPS) or autophagy-lysosome pathway (ALP), disaggregating protein aggregates, suppressing cell death pathways, and promoting mitochondrial health (Figure 1).
Secretory and transmembrane proteins accounting for one-third of total cellular proteins are synthesized on ribosomes bound to the endoplasmic reticulum (ER) membrane, translocated into the lumen of the ER, and then folded with the assistance of molecular chaperones and folding enzymes (protein disulfide isomerase etc.) abundantly expressed in the ER (ER chaperones hereafter).
The assay was initiated by adding 0.72 [micro]M MDH and the molecular chaperone proteins to assay buffer (50 mM Tris-HCl, 100 mM NaCl; pH7.4) heated to 48[degrees]C.
These HSPs, are commonly referred to as "molecular chaperones".
1 Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions 2 Necessary for efficient RNA polymerase transcription elongation past template- encoded arresting sites 3 A molecular chaperone, thought to be involved in the initiation step of translation at high temperature.
The company owns three clinical-stage compounds based on its small molecule "molecular chaperone" co-induction technology.
The UPR induces the expression of 78-kDa glucose-regulated protein [Grp78; also known as immunoglobulin heavy-chain-binding protein (BiP)], an ER-resident molecular chaperone that prevents the aggregation of unfolded or misfolded proteins so that they can be properly refolded (Brostrom and Brostrom 2003; Lee 2001; Schroder and Kaufman 2005).
In mammals, alpha crystallin functions as a molecular chaperone. Whereas alpha crystallin has been extensively studied in the endothermic mammals, little is known about this protein in ectothermic vertebrates.
This discovery is the first scientific evidence of a heat shock-like molecular chaperone protein that appears to protect the bacteria from the cow's immune system.
Like an overprotective human caretaker, the molecular chaperone needs a nudge before it lets go.
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.

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