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David Live

Researcher at University of Georgia

Publications -  34
Citations -  1150

David Live is an academic researcher from University of Georgia. The author has contributed to research in topics: Glycopeptide & Mannose. The author has an hindex of 19, co-authored 34 publications receiving 1064 citations. Previous affiliations of David Live include University of Minnesota & Cornell University.

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Principles of Mucin Architecture: Structural Studies on Synthetic Glycopeptides Bearing Clustered Mono-, Di-, Tri-, and Hexasaccharide Glycodomains

TL;DR: The similarity of the NMR data for each of the alpha-O-linked glycopeptides demonstrates that this structure persists for each construct and that the mode of attachment of the first sugar and the peptide is paramount in establishing the organization of the core.
Journal ArticleDOI

Bulk susceptibility corrections in nuclear magnetic resonance experiments using superconducting solenoids

David Live, +1 more
- 01 Jun 1970 - 
TL;DR: In this article, the problem of correcting the observed chemical shift for the difference in the bulk susceptibilities of the sample and the reference compound was treated for the Varian A-60 or HA-100 spectrometer.
Journal ArticleDOI

B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycan

TL;DR: The results indicate that B4GAT1 is involved in the initiation of the LARGE-dependent repeating disaccharide that is necessary for extracellular matrix protein binding to O-mannosylated α-dystroglycan that is lacking in secondary dystroglcanopathies.
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Glycomic analyses of mouse models of congenital muscular dystrophy.

TL;DR: The findings illustrate that classicalβ1,2-elongation and β1,6-GlcNAc branching of O-mannose glycan structures are dependent upon the POMGnT1 enzyme and that O- Mannosylation is not limited solely to α-DG in the mammalian brain.
Journal ArticleDOI

The Catalytic and Lectin Domains of UDP-GalNAc:Polypeptide α-N-Acetylgalactosaminyltransferase Function in Concert to Direct Glycosylation Site Selection

TL;DR: Results highlight the existence of two modes of site selection used by these ppGalNAcTs: local sequence recognition by the catalytic domain and the concerted recognition of distal sites of prior glycosylation together with local sequence binding mediated, respectively, by the lectin and catalytic domains.