Zobrazeno 1 - 10
of 25
pro vyhledávání: '"David R. Wing"'
Autor:
David R. Wing, David Harvey, Melitta Schachner, Raymond A. Dwek, Susanne Zamze, Taj S. Mattu, Penka Pesheva
Publikováno v:
Glycobiology, 9 (8)
Glycobiology, 9 (8)
ISSN:0959-6658
ISSN:0959-6658
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29aa4590a566e579e7e21ed6d6d586e8
http://doc.rero.ch/record/304438/files/9-8-823.pdf
http://doc.rero.ch/record/304438/files/9-8-823.pdf
Autor:
T D Butters, Frances M. Platt, Gabriele Reinkensmeier, David Harvey, Ulrika Andersson, V Hunnam, David R. Wing, Brett Garner, Raymond A. Dwek
The functional importance of glycolipids has emphasized the need for more sensitive methods of detection, characterization, and quantification than has often been possible using traditional thin-layer chromatographic techniques. We describe the use o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5682e50dc8f9dfe75fe32117e36f446
https://ora.ox.ac.uk/objects/uuid:1c51f2c8-b6b5-45d3-b988-c1646963b2f9
https://ora.ox.ac.uk/objects/uuid:1c51f2c8-b6b5-45d3-b988-c1646963b2f9
Autor:
Maren von der Ohe, Susan F. Wheeler, Melitta Schachner, David R. Wing, Steffen Liedtke, Manfred Wuhrer, Hildegard Geyer, Martina Mühlenhoff, Rudolf Geyer, Raymond A. Dwek, David Harvey, Rita Gerardy-Schahn
Publikováno v:
Scopus-Elsevier
The neural cell adhesion molecule (NCAM) plays important roles during development, plasticity, and regeneration in the adult nervous system. Its function is strongly influenced by attachment of the unusual alpha 2-8-linked polysialic acid (PSA). Here
Publikováno v:
European Journal of Biochemistry. 268:4063-4078
A family of about 20 novel acidic bi- and tri-antennary N-glycans, amounting to almost half those expressed on Bowes melanoma tissue-plasminogen activator (t-PA) were found to possess Galbeta1-->4GlcNAcbeta1-->, sulfated and sialylated GalNAcbeta1-->
Publikováno v:
Journal of the American Society for Mass Spectrometry. 11:564-571
Analysis of commercial samples of chicken ovalbumin by reversed-phase high performance liquid chromatography and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) showed the presence of several other co-purifying glycoproteins.
Autor:
David Harvey, Richard A.C. Clark, Beatrice M. Anner, Mounja Benallal, Raymond A. Dwek, Bernhard Kuster, David R. Wing
Publikováno v:
Glycoconjugate Journal. 16:437-456
The organ-specific nature of the glycosylation of Na+,K+-ATPase-enriched preparations from kidney and brain tissues has earlier been indicated by the use of lectin-staining techniques. Na+,K+-ATPase is ubiquitous and abundant, and subject to upregula
Publikováno v:
European Journal of Biochemistry. 258:243-270
This paper extends our earlier work on the analysis of neutral N-glycans from adult rat brain to glycans carrying NeuAc residues as their sole charged groups. These structures comprised at least 40% of the total (acidic and neutral) N-glycan pool. Co
Autor:
R.B. Parekh, R. Dwek, Alan F. Williams, A N Barclay, R. Dalchau, Antony C. Willis, T W Rademacher, David R. Wing, J.W. Fabre
Publikováno v:
Glycobiology. 3:339-348
Protein structure and tissue type are known to influence glycosylation of proteins. We have previously investigated the N-glycans at each of the three glycosylation sites of the cell surface glycoprotein Thy-1 when isolated from rat brain and thymocy
Autor:
T W Rademacher, G Thor, B. Schmitz, Melitta Schachner, Mark C. Field, David R. Wing, Raymond A. Dwek
Publikováno v:
Glycoconjugate Journal. 9:293-301
In this report, we describe the preparation of a library of N-linked glycans from whole murine brain obtained by the large-scale hydrazinolysis of an acetone powder of the tissue followed by chromatographic procedures. 84% of the characterized oligos
Publikováno v:
Biochemistry. 40(13)
The prion protein contains two N-linked glycosylation sites and a glycosylphosphatidylinositol (GPI) anchor. The large size of the N-linked sugars, together with their dynamic properties, enables them to shield two orthogonal faces of the protein alm