Harvard Catalyst Profiles
Contact, publication, and social network information about Harvard faculty and fellows.
Open Source Software
to edit your profile (add a photo, awards, links to other websites, etc.)
Edit My Profile
My Person List (
Return to Top
Search Result Details
Back to Search Results
This page shows the details of why an item matched the keywords from your search.
One or more keywords matched the following items that are connected to
LARGE can functionally bypass alpha-dystroglycan glycosylation defects in distinct congenital muscular dystrophies.
Molecular recognition by LARGE is essential for expression of functional dystroglycan.
O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.
Opposing roles of integrin alpha6Abeta1 and dystroglycan in laminin-mediated extracellular signal-regulated kinase activation.
Loss of basement membrane, receptor and cytoskeletal lattices in a laminin-deficient muscular dystrophy.
Disruption of perlecan binding and matrix assembly by post-translational or genetic disruption of dystroglycan function.
Like-acetylglucosaminyltransferase (LARGE)-dependent modification of dystroglycan at Thr-317/319 is required for laminin binding and arenavirus infection.
Basal lamina strengthens cell membrane integrity via the laminin G domain-binding motif of alpha-dystroglycan.
Dystroglycan controls signaling of multiple hormones through modulation of STAT5 activity.
Residual laminin-binding activity and enhanced dystroglycan glycosylation by LARGE in novel model mice to dystroglycanopathy.
Laminin-6 assembles into multimolecular fibrillar complexes with perlecan and participates in mechanical-signal transduction via a dystroglycan-dependent, integrin-independent mechanism.
Unique role of dystroglycan in peripheral nerve myelination, nodal structure, and sodium channel stabilization.
Old World arenavirus infection interferes with the expression of functional alpha-dystroglycan in the host cell.
Endogenous glucuronyltransferase activity of LARGE or LARGE2 required for functional modification of a-dystroglycan in cells and tissues.