chaperone

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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.
Immediate response of the DnaK molecular chaperone system to heat shock.
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.
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).
Hsp90 is a molecular chaperone required for the proper folding and activation of many cancer-promoting proteins, and is recognized as a key facilitator of cancer cell growth and survival.
Inhibitors of Molecular Chaperones as Therapeutic Agents
It is expected that blood-brain-barrier-permeable molecular chaperone inducers become available as new drugs for neurodegenerative diseases in the near future.
Translocated p26 is believed to function as a molecular chaperone for nuclear proteins, including lamins--major nuclear proteins--probably in association with hsp70 (Willsie and Clegg, 2002).
The Hsp90 molecular chaperone controls the folding of key signaling molecules required to maintain normal cell function in many organs, including the retina.
Washington, June 21 (ANI): Scientists have shown a molecular chaperone is working like a waste management company to collect and detoxify high levels of toxic amyloid beta peptide found in Alzheimer's disease.

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