Search Results - (Author, Cooperation:M. C. Field)

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  1. 1
    S. Alsford ; S. Eckert ; N. Baker ; L. Glover ; A. Sanchez-Flores ; K. F. Leung ; D. J. Turner ; M. C. Field ; M. Berriman ; D. Horn
    Nature Publishing Group (NPG)
    Published 2012
    Staff View
    Publication Date:
    2012-01-27
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Aquaglyceroporins/deficiency/metabolism ; Drug Resistance/*genetics ; Eflornithine/pharmacology ; Endocytosis/drug effects ; Glycosylation/drug effects ; High-Throughput Screening Assays ; Humans ; Lysosomes/drug effects/metabolism ; Melarsoprol/pharmacology ; Nifurtimox/pharmacology ; Pentamidine/pharmacology ; RNA Interference ; Suramin/pharmacology ; Trypanocidal Agents/*pharmacology/therapeutic use ; Trypanosoma brucei brucei/cytology/*drug effects/enzymology/metabolism ; Trypanosomiasis, African/*drug therapy/genetics
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  2. 2
    P. A. Nguyen ; A. C. Groen ; M. Loose ; K. Ishihara ; M. Wuhr ; C. M. Field ; T. J. Mitchison
    American Association for the Advancement of Science (AAAS)
    Published 2014
    Staff View
    Publication Date:
    2014-10-11
    Publisher:
    American Association for the Advancement of Science (AAAS)
    Print ISSN:
    0036-8075
    Electronic ISSN:
    1095-9203
    Topics:
    Biology
    Chemistry and Pharmacology
    Computer Science
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Animals ; Cell Membrane/chemistry/*physiology ; *Cell-Free System ; Centrosome/physiology ; *Cytokinesis ; DNA-Binding Proteins/genetics/metabolism ; Guanosine Triphosphate/metabolism ; Kinesin/genetics/metabolism ; Lipid Bilayers ; Microtubules/physiology ; Models, Biological ; Nuclear Proteins/genetics/metabolism ; *Signal Transduction ; Xenopus laevis ; rhoA GTP-Binding Protein/metabolism
    Published by:
    http://www.aaas.org/

    Latest Papers from Table of Contents or Articles in Press
  3. 3
    Field, M. C. ; Wing, D. R. ; Dwek, R. A. ; Rademacher, T. W. ; Schmitz, B. ; Bollensen, E. ; Schachner, M.

    Oxford, UK : Blackwell Publishing Ltd
    Published 1992
    Staff View
    ISSN:
    1471-4159
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Medicine
    Notes:
    Abstract: P0, the most abundant glycoprotein of PNS myelin, is a homophilic and heterophilic adhesion molecule. P0 is known to contain a glycofonn population that expresses the L2/HNK-1 carbohydrate epitope found on other neural adhesion molecules, and to be functionally implicated centrally in neural cell adhesion and neurite outgrowth. This carbohydrate epitope has been characterized previously from glycolipid structures and contains a sulphated glucuronic acid residue. However, the L2/HNK-1 carbohydrate epitope has not been characterized in glycoproteins. Because P0 possesses only one glycosylation sequon, the number of P0 glycoforms is equal to the heterogeneity of the glycan species. Here we report that the carbohydrate analysis of L2/HNK-1-reactive P0 showed the presence of anionic structures containing sialic acid and sulphate in various combinations. At least one sulphate residue was present in 80% of the monosaccharide sequences, and 20% contained three sulphates. High-resolution P4 gel chromatography of the desialylated and desulphated oligosaccharides showed substantial heterogeneity of monosaccharide sequences. Sequential exoglycosidase digestions indicated that the majority of the structures were of the hybrid class, although the sulphated structures were found to be en-doglycosidase H-resistant.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1111/j.1471-4159.1992.tb09353.x

    Articles: DFG German National Licenses
  4. 4
    Staff View
    ISSN:
    1573-4986
    Keywords:
    N-linked ; oligosaccharide library ; L2/HNK-1 epitope ; anionicity ; murine brain ; large scale hydrazinolysis
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Chemistry and Pharmacology
    Notes:
    Abstract In this report, we describe the preparation of a library ofN-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 oligosaccharides were found to be anionic, the remainder neutral. The anionic species were successively neutralized by neuraminidase (29%), aq. hydrofluoric acid (30%), and methanolysis (26%), indicating that approximately equal portions were sensitive to desialylation, dephosphorylation and desulfation, respectively. The presence of the sulfated fraction was confirmed by direct35SO4 metabolic labelling. A residual partially characterized fraction was found to be anionic through possession of carboxylic acid groups, unrelated to sialic acid. The purified oligosaccharides, in the absence of their original protein conjugates, were shown to retain those immunological characteristics essential for recognition by a specific monoclonal antibody, LS (412), that is known to recognize a carbohydrate epitope present on a number of neural adhesion molecules and functional in neural cell adhesion. These properties confirm the viability of scaling up the size of the hydrazinolysis procedure and adapting it to whole tissue for the production of glycan libraries and for the probing of structures of interest.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF00731089

    Articles: DFG German National Licenses