Publications
330 results found
Dell A, Morris H, Haslam S, 2010, Functional Glycomics: The Pivotal Role of Mass Spectrometry, Annual Conference of the Society-for-Glycobiology, Publisher: OXFORD UNIV PRESS INC, Pages: 1450-1450, ISSN: 0959-6658
Clark G, Pang P-C, Grassi P, et al., 2010, Tumor Biomarker Glycoproteins Present in the Seminal Plasma of Healthy Human Males Are Novel Endogenous Ligands for DC-Sign, Annual Conference of the Society-for-Glycobiology, Publisher: OXFORD UNIV PRESS INC, Pages: 1522-1522, ISSN: 0959-6658
Kaminski L, Abu-Qarn M, Guan Z, et al., 2010, AglJ Adds the First Sugar of the N-Linked Pentasaccharide Decorating the <i>Haloferax volcanii</i> S-Layer Glycoprotein, JOURNAL OF BACTERIOLOGY, Vol: 192, Pages: 5572-5579, ISSN: 0021-9193
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- Citations: 55
Bateman AC, Karamanska R, Busch MG, et al., 2010, Glycan Analysis and Influenza A Virus Infection of Primary Swine Respiratory Epithelial Cells <i>THE IMPORTANCE OF NeuAc</i>α<i>2-6</i> <i>GLYCANS</i>, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 285, Pages: 34016-34026
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- Citations: 79
Lo W-Y, Lagrange AH, Hernandez CC, et al., 2010, Glycosylation of β2 Subunits Regulates GABA<sub>A</sub> Receptor Biogenesis and Channel Gating, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 285, Pages: 31348-31361
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- Citations: 32
Jervis AJ, Langdon R, Hitchen P, et al., 2010, Characterization of N-Linked Protein Glycosylation in <i>Helicobacter pullorum</i>, JOURNAL OF BACTERIOLOGY, Vol: 192, Pages: 5228-5236, ISSN: 0021-9193
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- Citations: 53
Hitchen PG, Twigger K, Valiente E, et al., 2010, Glycoproteomics: a powerful tool for characterizing the diverse glycoforms of bacterial pilins and flagellins, BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 38, Pages: 1307-1313, ISSN: 0300-5127
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- Citations: 21
Picco G, Julien S, Brockhausen I, et al., 2010, Over-expression of ST3Gal-I promotes mammary tumorigenesis, GLYCOBIOLOGY, Vol: 20, Pages: 1241-1250, ISSN: 0959-6658
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- Citations: 100
Kay E, Lesk VI, Tamaddoni-Nezhad A, et al., 2010, Systems analysis of bacterial glycomes, BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 38, Pages: 1290-1293, ISSN: 0300-5127
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- Citations: 10
Fang M, Dewaele S, Zhao Y-P, et al., 2010, Serum N-glycome biomarker for monitoring development of DENA-induced hepatocellular carcinoma in rat, MOLECULAR CANCER, Vol: 9, ISSN: 1476-4598
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- Citations: 22
Harris EN, Parry S, Sutton-Smith M, et al., 2010, <i>N-</i>Glycans on the link domain of human HARE/Stabilin-2 are needed for hyaluronan binding to purified ecto-domain, but not for cellular endocytosis of hyaluronan, GLYCOBIOLOGY, Vol: 20, Pages: 991-1001, ISSN: 0959-6658
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- Citations: 14
Hitchen P, Brzostek J, Panico M, et al., 2010, Modification of the <i>Campylobacter jejuni</i> flagellin glycan by the product of the Cj1295 homopolymeric-tract-containing gene, MICROBIOLOGY-SGM, Vol: 156, Pages: 1953-1962, ISSN: 1350-0872
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- Citations: 42
Garner OB, Aguilar HC, Fulcher JA, et al., 2010, Endothelial Galectin-1 Binds to Specific Glycans on Nipah Virus Fusion Protein and Inhibits Maturation, Mobility, and Function to Block Syncytia Formation, PLOS PATHOGENS, Vol: 6, ISSN: 1553-7366
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- Citations: 52
Chavele K-M, Martinez-Pomares L, Domin J, et al., 2010, Mannose receptor interacts with Fc receptors and is critical for the development of crescentic glomerulonephritis in mice, JOURNAL OF CLINICAL INVESTIGATION, Vol: 120, Pages: 1469-1478, ISSN: 0021-9738
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- Citations: 40
Magidovich H, Yurist-Doutsch S, Konrad Z, et al., 2010, AglP is a S-adenosyl-L-methionine-dependent methyltransferase that participates in the N-glycosylation pathway of <i>Haloferax volcanii</i>, MOLECULAR MICROBIOLOGY, Vol: 76, Pages: 190-199, ISSN: 0950-382X
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- Citations: 53
Charlier E, Conde C, Zhang J, et al., 2010, SHIP-1 inhibits CD95/APO-1/Fas-induced apoptosis in primary T lymphocytes and T leukemic cells by promoting CD95 glycosylation independently of its phosphatase activity, Leukemia, Vol: 24, Pages: 821-832, ISSN: 0887-6924
Takamatsu S, Antonopoulos A, Ohtsubo K, et al., 2010, Physiological and glycomic characterization of <i>N</i>-acetylglucosaminyltransferase-IVa and -IVb double deficient mice, GLYCOBIOLOGY, Vol: 20, Pages: 485-497, ISSN: 0959-6658
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- Citations: 46
Wada Y, Dell A, Haslam SM, et al., 2010, Comparison of Methods for Profiling <i>O</i>-Glycosylation HUMAN PROTEOME ORGANISATION HUMAN DISEASE GLYCOMICS/PROTEOME INITIATIVE MULTI-INSTITUTIONAL STUDY OF IgA1, MOLECULAR & CELLULAR PROTEOMICS, Vol: 9, Pages: 719-727, ISSN: 1535-9476
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- Citations: 119
Coombs PJ, Harrison R, Pemberton S, et al., 2010, Identification of Novel Contributions to High-affinity Glycoprotein-Receptor Interactions using Engineered Ligands, JOURNAL OF MOLECULAR BIOLOGY, Vol: 396, Pages: 685-696, ISSN: 0022-2836
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- Citations: 22
North SJ, Huang H-H, Sundaram S, et al., 2010, Glycomics Profiling of Chinese Hamster Ovary Cell Glycosylation Mutants Reveals <i>N</i>-Glycans of a Novel Size and Complexity, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 285, Pages: 5759-5775
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- Citations: 163
Yurist-Doutsch S, Magidovich H, Ventura VV, et al., 2010, N-glycosylation in Archaea: on the coordinated actions of <i>Haloferax volcanii</i> AglF and AglM, MOLECULAR MICROBIOLOGY, Vol: 75, Pages: 1047-1058, ISSN: 0950-382X
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- Citations: 55
Yurist-Doutsch S, Magidovich H, Ventura VV, et al., 2010, N-glycosylation in Archaea: On the coordinated actions of Haloferax volcanii AglF and AglM., Mol Microbiol
ABSTRACT Like Eukarya and Bacteria, Archaea are also capable of performing N-glycosylation. In the halophilic archaeon Haloferax volcanii, N-glycosylation is mediated by the products of the agl gene cluster. In the present report, this gene cluster was expanded to include an additional sequence, aglM, shown to participate in the biosynthesis of hexuronic acids contained within a pentasaccharide decorating the S-layer glycoprotein, a reporter Hfx. volcanii glycoprotein. In response to different growth conditions, changes in the transcription profile of aglM mirrored changes in the transcription profiles of aglF, aglG and aglI, genes encoding confirmed participants in the Hfx. volcanii N-glycosylation pathway, thus offering support to the hypothesis that in Hfx. volcanii, N-glycosylation serves an adaptive role. Following purification, biochemical analysis revealed AglM to function as a UDP-glucose dehydrogenase. In a coupled reaction with AglF, a previously identified glucose-1-phosphate uridyltransferase, UDP-glucuronic acid was generated from glucose-1-phosphate and UTP in a NAD(+)-dependent manner. These experiments thus represent the first step toward in vitro reconstitution of the archaeal N-glycosylation process.
Yoon S-J, Park S-Y, Pang P-C, et al., 2010, N-glycosylation status of beta-haptoglobin in sera of patients with prostate cancer vs. benign prostate diseases, International Journal of Oncology, Vol: 36, Pages: 193-203, ISSN: 1019-6439
N-glycosylation status of purified β-haptoglobin separated from sera of patients with prostate cancer was studied in comparison to that of sera from patients with benign prostate diseases, or normal subjects. Two different approaches, as summarized below, one based on binding of lectins and antibodies to β-haptoglobin, the other on mass spectrometry of released N-linked glycans from β-haptoglobin, were performed. Some of the results were useful for distinction of prostate cancer vs. benign prostate diseases. i) Binding of Phaseolus vulgaris-L lectin (PHA-L), defining the GlcNAcβ6Manα6Man side chain present in tri- or tetra-antennary N-linked glycans, to β-haptoglobin was higher for cases of prostate cancer and high-grade prostate intraepithelial neoplasia than for benign diseases. Binding of Aleuria aurantia lectin (AAL) defining Fucα3-, α4-, or α6-GlcNAc, or monoclonal antibody directed to sialyl-Lex, to β-haptoglobin was also higher for some of the cancer cases than for benign diseases. Many other lectins and antibodies showed no binding to β-haptoglobin, or showed no significant difference between cancer vs. benign diseases. ii) Mass spectrometric analysis of N-linked glycans of β-haptoglobin released by Peptide N-glycosidase-F showed enhanced expression of monosialyl tri-antennary structures in prostate cancer cases. Thus, binding of PHA-L to affinity-purified β-haptoglobin from sera of patients could lead to development of useful tools for differential diagnosis of prostate cancer vs. benign prostate diseases.
Canis K, McKinnon TAJ, Nowak A, et al., 2010, The plasma von Willebrand factor <i>O</i>-glycome comprises a surprising variety of structures including ABH antigens and disialosyl motifs, JOURNAL OF THROMBOSIS AND HAEMOSTASIS, Vol: 8, Pages: 137-145, ISSN: 1538-7933
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- Citations: 58
North SJ, Jang-Lee J, Harrison R, et al., 2010, Chapter Two - Mass Spectrometric Analysis of Mutant Mice, Pages: 27-77, ISSN: 0076-6879
Abstract Mass spectrometry (MS) has proven to be the preeminent tool for the rapid, high-sensitivity analysis of the primary structure of glycans derived from diverse biological sources including cells, fluids, secretions, tissues, and organs. These analyses are anchored by matrix-assisted laser desorption ionization time of flight (MALDI-TOF) analysis of permethylated derivatives of glycan pools released from the samples, to produce glycomic mass fingerprints. The application of complimentary techniques, such as chemical and enzymatic digestions, GC–MS linkage analysis, and tandem mass spectrometry (MS/MS) utilizing both electrospray (ES) and MALDI-TOF/TOF, together with bioinformatic tools allows the elucidation of incrementally more detailed structural information from the sample(s) of interest. The mouse as a model organism offers many advantages in the study of human biology, health, and disease; it is a mammal, shares 99% genetic homology with humans and its genome supports targeted mutagenesis in specific genes to produce knockouts efficiently and precisely. Glycomic analyses of tissues and organs from mice genetically deficient in one or more glycosylation gene and comparison with data collected from wild-type samples enables the facile identification of changes and perturbations within the glycome. The Consortium for Functional Glycomics (CFG) has been applying such MS-based glycomic analyses to a range of murine tissues from both wild-type and glycosylation-knockout mice in order to provide a repository of structural data for the glycobiology community. In this chapter, we describe in detail the methodologies used to prepare, derivatize, purify, and analyze glycan pools from mouse organs and tissues by MS. We also present a summary of data produced from the CFG systematic structural analysis of wild-type and knockout mouse tissues, together with a detailed example of a glycomic analysis of the Mgat4a knockout mouse.
Dell A, Galadari A, Sastre F, et al., 2010, Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes., Int J Microbiol, Vol: 2010
Recent years have witnessed a rapid growth in the number and diversity of prokaryotic proteins shown to carry N- and/or O-glycans, with protein glycosylation now considered as fundamental to the biology of these organisms as it is in eukaryotic systems. This article overviews the major glycosylation pathways that are known to exist in eukarya, bacteria and archaea. These are (i) oligosaccharyltransferase (OST)-mediated N-glycosylation which is abundant in eukarya and archaea, but is restricted to a limited range of bacteria; (ii) stepwise cytoplasmic N-glycosylation that has so far only been confirmed in the bacterial domain; (iii) OST-mediated O-glycosylation which appears to be characteristic of bacteria; and (iv) stepwise O-glycosylation which is common in eukarya and bacteria. A key aim of the review is to integrate information from the three domains of life in order to highlight commonalities in glycosylation processes. We show how the OST-mediated N- and O-glycosylation pathways share cytoplasmic assembly of lipid-linked oligosaccharides, flipping across the ER/periplasmic/cytoplasmic membranes, and transferring "en bloc" to the protein acceptor. Moreover these hallmarks are mirrored in lipopolysaccharide biosynthesis. Like in eukaryotes, stepwise O-glycosylation occurs on diverse bacterial proteins including flagellins, adhesins, autotransporters and lipoproteins, with O-glycosylation chain extension often coupled with secretory mechanisms.
Peyfoon E, Meyer B, Hitchen PG, et al., 2010, The <i>S</i>-Layer Glycoprotein of the Crenarchaeote <i>Sulfolobus acidocaldarius</i> Is Glycosylated at Multiple Sites with Chitobiose-Linked <i>N</i>-Glycans, ARCHAEA-AN INTERNATIONAL MICROBIOLOGICAL JOURNAL, Vol: 2010, ISSN: 1472-3646
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- Citations: 64
Magalhaes A, Gomes J, Ismail MN, et al., 2009, Fut2-null mice display an altered glycosylation profile and impaired BabA-mediated <i>Helicobacter pylori</i> adhesion to gastric mucosa, GLYCOBIOLOGY, Vol: 19, Pages: 1525-1536, ISSN: 0959-6658
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- Citations: 82
Rogers DW, Baldini F, Battaglia F, et al., 2009, Transglutaminase-Mediated Semen Coagulation Controls Sperm Storage in the Malaria Mosquito, PLOS BIOLOGY, Vol: 7, ISSN: 1545-7885
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- Citations: 96
Xu K, Antonopoulos A, Spanoudakis E, et al., 2009, Glucose Ceramide Synthase Inhibitors Inhibit Osteoclast Activation Induced by Myeloma-Derived and De Novo Synthesized Glycosphingolipids, 51st Annual Meeting of the American-Society-of-Hematology, Publisher: AMER SOC HEMATOLOGY, Pages: 176-176, ISSN: 0006-4971
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