FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2080958887> ?p ?o ?g. }

• W2080958887 endingPage "14430" @default.
• W2080958887 startingPage "14418" @default.
• W2080958887 abstract "Aberrant glycosylation of α-dystroglycan (α-DG) results in loss of interactions with the extracellular matrix and is central to the pathogenesis of several disorders. To examine protein glycosylation of α-DG, a facile synthetic approach has been developed for the preparation of unusual phosphorylated O-mannosyl glycopeptides derived from α-DG by a strategy in which properly protected phospho-mannosides are coupled with a Fmoc protected threonine derivative, followed by the use of the resulting derivatives in automated solid-phase glycopeptide synthesis using hyper-acid-sensitive Sieber amide resin. Synthetic efforts also provided a reduced phospho-trisaccharide, and the NMR data of this derivative confirmed the proper structural assignment of the unusual phospho-glycan structure. The glycopeptides made it possible to explore factors that regulate the elaboration of critical glycans. It was established that a glycopeptide having a 6-phospho-O-mannosyl residue is not an acceptor for action by the enzyme POMGnT1, which attaches β(1,2)-GlcNAc to O-mannosyl moietes, whereas the unphosphorylated derivate was readily extended by the enzyme. This finding implies a specific sequence of events in determining the structural fate of the O-glycan. It has also been found that the activity of POMGnT1 is dependent on the location of the acceptor site in the context of the underlying polypeptide/glycopeptide sequence. Conformational analysis by NMR has shown that the O-mannosyl modification does not exert major conformational effect on the peptide backbone. It is, however, proposed that these residues, introduced at the early stages of glycoprotein glycosylation, have an ability to regulate the loci of subsequent O-GalNAc additions, which do exert conformational effects. The studies show that through access to discrete glycopeptide structures, it is possible to reveal complex regulation of O-glycan processing on α-DG that has significant implications both for its normal post-translational maturation, and the mechanisms of the pathologies associated with hypoglycosylated α-DG." @default.
• W2080958887 created "2016-06-24" @default.
• W2080958887 creator A5003918300 @default.
• W2080958887 creator A5006418968 @default.
• W2080958887 creator A5019975195 @default.
• W2080958887 creator A5030157703 @default.
• W2080958887 creator A5047989158 @default.
• W2080958887 creator A5055188575 @default.
• W2080958887 creator A5055980813 @default.
• W2080958887 creator A5073108061 @default.
• W2080958887 creator A5087911344 @default.
• W2080958887 date "2011-08-22" @default.
• W2080958887 modified "2023-09-26" @default.
• W2080958887 title "Synthetic, Structural, and Biosynthetic Studies of an Unusual Phospho-Glycopeptide Derived from α-Dystroglycan" @default.
• W2080958887 cites W1496611805 @default.
• W2080958887 cites W1963757547 @default.
• W2080958887 cites W1968072780 @default.
• W2080958887 cites W1968666078 @default.
• W2080958887 cites W1968896304 @default.
• W2080958887 cites W1979452378 @default.
• W2080958887 cites W1981004520 @default.
• W2080958887 cites W1981447099 @default.
• W2080958887 cites W1983066280 @default.
• W2080958887 cites W1986082861 @default.
• W2080958887 cites W1988184759 @default.
• W2080958887 cites W1992834754 @default.
• W2080958887 cites W1995992973 @default.
• W2080958887 cites W2000699613 @default.
• W2080958887 cites W2004228578 @default.
• W2080958887 cites W2004785920 @default.
• W2080958887 cites W2008741744 @default.
• W2080958887 cites W2009118884 @default.
• W2080958887 cites W2010834344 @default.
• W2080958887 cites W2013661031 @default.
• W2080958887 cites W2018105404 @default.
• W2080958887 cites W2020140161 @default.
• W2080958887 cites W2040718007 @default.
• W2080958887 cites W2042334899 @default.
• W2080958887 cites W2054971943 @default.
• W2080958887 cites W2062628051 @default.
• W2080958887 cites W2065551216 @default.
• W2080958887 cites W2067254197 @default.
• W2080958887 cites W2075590217 @default.
• W2080958887 cites W2077463658 @default.
• W2080958887 cites W2081042973 @default.
• W2080958887 cites W2084198615 @default.
• W2080958887 cites W2087238905 @default.
• W2080958887 cites W2093217904 @default.
• W2080958887 cites W2109678537 @default.
• W2080958887 cites W2126256628 @default.
• W2080958887 cites W2133843400 @default.
• W2080958887 cites W2137815739 @default.
• W2080958887 cites W2138827544 @default.
• W2080958887 cites W2143133768 @default.
• W2080958887 cites W2146966424 @default.
• W2080958887 cites W2165170270 @default.
• W2080958887 cites W2168889822 @default.
• W2080958887 cites W2950976733 @default.
• W2080958887 doi "https://doi.org/10.1021/ja205473q" @default.
• W2080958887 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3176502" @default.
• W2080958887 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21812486" @default.
• W2080958887 hasPublicationYear "2011" @default.
• W2080958887 type Work @default.
• W2080958887 sameAs 2080958887 @default.
• W2080958887 citedByCount "39" @default.
• W2080958887 countsByYear W20809588872012 @default.
• W2080958887 countsByYear W20809588872013 @default.
• W2080958887 countsByYear W20809588872014 @default.
• W2080958887 countsByYear W20809588872015 @default.
• W2080958887 countsByYear W20809588872016 @default.
• W2080958887 countsByYear W20809588872017 @default.
• W2080958887 countsByYear W20809588872018 @default.
• W2080958887 countsByYear W20809588872019 @default.
• W2080958887 countsByYear W20809588872020 @default.
• W2080958887 countsByYear W20809588872022 @default.
• W2080958887 crossrefType "journal-article" @default.
• W2080958887 hasAuthorship W2080958887A5003918300 @default.
• W2080958887 hasAuthorship W2080958887A5006418968 @default.
• W2080958887 hasAuthorship W2080958887A5019975195 @default.
• W2080958887 hasAuthorship W2080958887A5030157703 @default.
• W2080958887 hasAuthorship W2080958887A5047989158 @default.
• W2080958887 hasAuthorship W2080958887A5055188575 @default.
• W2080958887 hasAuthorship W2080958887A5055980813 @default.
• W2080958887 hasAuthorship W2080958887A5073108061 @default.
• W2080958887 hasAuthorship W2080958887A5087911344 @default.
• W2080958887 hasBestOaLocation W20809588872 @default.
• W2080958887 hasConcept C108625454 @default.
• W2080958887 hasConcept C137610392 @default.
• W2080958887 hasConcept C181199279 @default.
• W2080958887 hasConcept C185592680 @default.
• W2080958887 hasConcept C206212055 @default.
• W2080958887 hasConcept C2775880066 @default.
• W2080958887 hasConcept C2776414213 @default.
• W2080958887 hasConcept C2777313579 @default.
• W2080958887 hasConcept C2778312041 @default.
• W2080958887 hasConcept C2779281246 @default.
• W2080958887 hasConcept C2781338088 @default.
• W2080958887 hasConcept C501593827 @default.

• next