Ontology highlight
ABSTRACT:
SUBMITTER: Cyr DM
PROVIDER: S-EPMC4445657 | biostudies-literature | 2008 Jun
REPOSITORIES: biostudies-literature
Molecular chaperones such as heat shock protein 70 (Hsp70) are crucial for protein folding. Crystal structures of Hsp70 in a complex with the nucleotide exchange factor (NEF) Hsp110 reported in this issue of Cell (Polier et al., 2008) and in Molecular Cell (Schuermann et al., 2008) provide new insights into how NEF action specifies Hsp70 cellular function. ...[more]