Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 10, Issue 1, Pages 26-33Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/S0959-440X(99)00044-5
Keywords
-
Categories
Ask authors/readers for more resources
The contribution of the two major cytosolic chaperone systems. Hsp70 and the cylindrical chaperonins, to cellular protein folding has been clarified by a number of recent papers. These studies found that, in vivo, a significant fraction of newly synthesized polypeptides transit through these chaperone systems in both prokaryotic and eukaryotic cells. The identification and characterization of the cellular substrates of chaperones will be instrumental in understanding how proteins fold in vivo.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available