Ontology highlight
ABSTRACT:
SUBMITTER: Craig TA
PROVIDER: S-EPMC2992958 | biostudies-literature | 2010 Nov
REPOSITORIES: biostudies-literature
Craig Theodore A TA Kumar Rajiv R
Biochemical and biophysical research communications 20101014 2
To gain insights into the mechanism of action of sclerostin, a protein that regulates bone mass, we performed yeast two-hybrid analyses using human SOST (sclerostin) cDNA cloned into pGBKT7 DNA-binding domain vector as a bait, and a normalized, high-complexity, universal cDNA library in a GAL4 activating domain vector. We identified an interaction between sclerostin and the carboxyl-terminal portion of the receptor tyrosine-protein kinase erbB-3. To determine the biological relevance of this int ...[more]