Other Free Encyclopedias » Medicine Encyclopedia » Genetics in Medicine - Part 1 » Chaperones - Discovery Of Chaperones, Recognizing And Correcting Mistakes, Two Common Chaperone Systems: Hsp70 And Hsp60

Chaperones - Chaperones And Human Disease

molecular proteins http folding

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.

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>.

[back] Chaperones - Other Chaperone Systems

User Comments

The following comments are not guaranteed to be that of a trained medical professional. Please consult your physician for advice.

Your email address will be altered so spam harvesting bots can't read it easily.
Hide my email completely instead?

Cancel or