FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1570063124> ?p ?o ?g. }

• W1570063124 endingPage "12115" @default.
• W1570063124 startingPage "12104" @default.
• W1570063124 abstract "Abstract Alg3 yeast mutants synthesize endoglycosidase H-resistant oligosaccharides whose precursor for elongation is Man1 alpha-->2Man1 alpha-->2Man1 alpha-->3(Man1 alpha-->6)Man1 beta-->4GlcNAc2 (Verostek, M.F., Atkinson, P.H., and Trimble, R. B. (1991) J. Biol. Chem. 266, 5547-5551). To characterize alg3 glycan elongation in vivo, oligosaccharides on alg3,sec18 invertase synthesized and secreted at 26 degrees C were released with peptide-N4-N-acetyl-beta-glucosaminyl asparagine amidase and purified by Bio-Gel P-4 chromatography. Large (Man > 30GlcNAc2) and intermediate (Man5-10GlcNAc2) sized oligosaccharides were pooled separately, and the smaller ones were exchanged with 2H2O for one- and two-dimensional DQF-COSY 1H NMR analyses at 500 MHz. Although there was no detectable substitution of the terminal alpha 1,6-core-linked mannose, addition of alpha 1,6-, alpha 1,2-, and alpha 1,3-mannoses to the alpha 1,3-linked core branch of a majority of the Man5 precursor was analogous to core-filling reactions seen on wild type invertase glycans (Trimble, R.B., and Atkinson, P.H. (1986) J. Biol. Chem. 261, 9815-9824). Two additional types of oligosaccharide structures were found; those which retained glucose and those consistent with mannan elongation. Glucose retention appeared to be due to inefficient trimming from minor glucosylated intermediates, while mannan elongation was by extension of a new alpha 1,6-linked branch from the alpha 1,3-core-linked residue as seen in wild-type core oligosaccharides (Hernandez, L.M., Ballou, L., Alvarado, E., Gillece-Castro, B.L., Burlingame, A.L., and Ballou, C. E. (1989) J. Biol. Chem. 264, 11849-11856) or mnn1,mnn2,mnn10 processing intermediates (Ballou, L., Alvarado, E., Tsai, P-k., Dell, A., and Ballou, C.E. (1989) J. Biol. Chem. 264, 11857-11864). Thus, the alpha 1,6-linked branch additions which form Man9GlcNAc2-PP-dolichol from Man5GlcNAc2-PP-dolichol appear to provide important structural information enabling efficient recognition by the endoplasmic reticulum-glucosyltransferases forming oligosaccharide-lipid as well as the glucosidases involved in early trimming reactions, but the alg3 mutant documents that they are unnecessary for normal yeast mannan elongation." @default.
• W1570063124 created "2016-06-24" @default.
• W1570063124 creator A5008755693 @default.
• W1570063124 creator A5027915409 @default.
• W1570063124 creator A5058305680 @default.
• W1570063124 date "1993-06-01" @default.
• W1570063124 modified "2023-10-10" @default.
• W1570063124 title "Glycoprotein biosynthesis in the alg3 Saccharomyces cerevisiae mutant. II. Structure of novel Man6-10GlcNAc2 processing intermediates on secreted invertase" @default.
• W1570063124 doi "https://doi.org/10.1016/s0021-9258(19)50314-3" @default.
• W1570063124 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8505334" @default.
• W1570063124 hasPublicationYear "1993" @default.
• W1570063124 type Work @default.
• W1570063124 sameAs 1570063124 @default.
• W1570063124 citedByCount "34" @default.
• W1570063124 countsByYear W15700631242012 @default.
• W1570063124 countsByYear W15700631242014 @default.
• W1570063124 countsByYear W15700631242022 @default.
• W1570063124 countsByYear W15700631242023 @default.
• W1570063124 crossrefType "journal-article" @default.
• W1570063124 hasAuthorship W1570063124A5008755693 @default.
• W1570063124 hasAuthorship W1570063124A5027915409 @default.
• W1570063124 hasAuthorship W1570063124A5058305680 @default.
• W1570063124 hasBestOaLocation W15700631241 @default.
• W1570063124 hasConcept C104317684 @default.
• W1570063124 hasConcept C108625454 @default.
• W1570063124 hasConcept C143065580 @default.
• W1570063124 hasConcept C181199279 @default.
• W1570063124 hasConcept C185592680 @default.
• W1570063124 hasConcept C2777576037 @default.
• W1570063124 hasConcept C2778252681 @default.
• W1570063124 hasConcept C2779222958 @default.
• W1570063124 hasConcept C553450214 @default.
• W1570063124 hasConcept C55493867 @default.
• W1570063124 hasConcept C86803240 @default.
• W1570063124 hasConcept C95444343 @default.
• W1570063124 hasConceptScore W1570063124C104317684 @default.
• W1570063124 hasConceptScore W1570063124C108625454 @default.
• W1570063124 hasConceptScore W1570063124C143065580 @default.
• W1570063124 hasConceptScore W1570063124C181199279 @default.
• W1570063124 hasConceptScore W1570063124C185592680 @default.
• W1570063124 hasConceptScore W1570063124C2777576037 @default.
• W1570063124 hasConceptScore W1570063124C2778252681 @default.
• W1570063124 hasConceptScore W1570063124C2779222958 @default.
• W1570063124 hasConceptScore W1570063124C553450214 @default.
• W1570063124 hasConceptScore W1570063124C55493867 @default.
• W1570063124 hasConceptScore W1570063124C86803240 @default.
• W1570063124 hasConceptScore W1570063124C95444343 @default.
• W1570063124 hasIssue "16" @default.
• W1570063124 hasLocation W15700631241 @default.
• W1570063124 hasOpenAccess W1570063124 @default.
• W1570063124 hasPrimaryLocation W15700631241 @default.
• W1570063124 hasRelatedWork W1976802801 @default.
• W1570063124 hasRelatedWork W1990240964 @default.
• W1570063124 hasRelatedWork W2072731694 @default.
• W1570063124 hasRelatedWork W2073938168 @default.
• W1570063124 hasRelatedWork W2079034519 @default.
• W1570063124 hasRelatedWork W2327550610 @default.
• W1570063124 hasRelatedWork W2364482154 @default.
• W1570063124 hasRelatedWork W2725521960 @default.
• W1570063124 hasRelatedWork W4248869635 @default.
• W1570063124 hasRelatedWork W4312925230 @default.
• W1570063124 hasVolume "268" @default.
• W1570063124 isParatext "false" @default.
• W1570063124 isRetracted "false" @default.
• W1570063124 magId "1570063124" @default.
• W1570063124 workType "article" @default.