Gene expression in wild type and Mgat3 mouse embryos

ABSTRACT: Dr. Stanley's laboratory is interested in 1) understanding the biological roles of specific classes of N-glycan in development and immunity through studies of glycosyltransferase mutant mice, 2) identifying complex binding specificities of galectins using a panel of CHO glycosylation mutants, and 3) determining how O-fucose glycans function in Notch receptor signaling and in modulating the interaction of Notch receptors with their ligands. The bisecting GlcNAc on N-glycans inhibits ricin binding and enhances E-PHA binding. It is expected that mammalian CBP's, including galectins, may have their binding affected positively or negatively by the presence of the bisecting GlcNAc. In fact unpublished experiments have identified reduced binding of at least one galectin to LEC10 CHO cells that ex

ORGANISM(S): Mus musculus

SUBMITTER: Steven Head 

PROVIDER: E-GEOD-27055 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress