Chaperones
Chaperones And Human Disease
It is clear that molecular chaperones assist with the folding of newly synthesized proteins and correct protein misfolding. Recent studies now suggest that defects in molecular chaperone/substrate interactions may also play a substantial role in human disease. For example, mutations linked to Alzheimer's disease have been shown to disrupt the expression of chaperones in the endoplasmic reticulum. In addition, several genes linked to eye degeneration diseases have recently been identified as putative molecular chaperones.
SEE ALSO CELL, EUKARYOTIC; POST-TRANSLATIONAL CONTROL; PROTEINS; RIBOSOME; TRANSLATION.
Patricia L. Clark
Bibliography
Frydman, Judith. "Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones." Annual Review of Biochemistry 70 (2001): 603-647.
Wickner, Sue, Michael R. Maurizi, and Susan Gottesman. "Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins." Science 286 (1999): 1888-1893.
Internet Resources
"Chaperone." Nurse Minerva. <http://www.nurseminerva.co.uk/chaperon.htm>.
"Innovations." Environmental Health Perspectives. National Institutes of Health. <http://ehpnet1.niehs.nih.gov/docs/1994/102-6-7/innovations.html>.
"Molecular Chaperones." Federation of American Societies for Experimental Biology. <http://www.faseb.org/opar/protfold/molechap.html>.
Additional topics
Medicine EncyclopediaGenetics in Medicine - Part 1Chaperones - Discovery Of Chaperones, Recognizing And Correcting Mistakes, Two Common Chaperone Systems: Hsp70 And Hsp60