Glycoprotein Structural Genomics: Solving the Glycosylation Problem

[1]  R. Owens,et al.  Analysis of variable N-glycosylation site occupancy in glycoproteins by liquid chromatography electrospray ionization mass spectrometry. , 2007, Analytical biochemistry.

[2]  Weixian Lu,et al.  A time- and cost-efficient system for high-level protein production in mammalian cells. , 2006, Acta crystallographica. Section D, Biological crystallography.

[3]  L. Gustafsson,et al.  Eukaryotic expression: developments for structural proteomics , 2006, Acta crystallographica. Section D, Biological crystallography.

[4]  R. Dwek,et al.  Inhibition of hybrid- and complex-type glycosylation reveals the presence of the GlcNAc transferase I-independent fucosylation pathway. , 2006, Glycobiology.

[5]  Christian Siebold,et al.  Molecular analysis of receptor protein tyrosine phosphatase μ‐mediated cell adhesion , 2006, The EMBO journal.

[6]  Steven E Brenner,et al.  The Impact of Structural Genomics: Expectations and Outcomes , 2005, Science.

[7]  Janet Newman,et al.  Towards rationalization of crystallization screening for small- to medium-sized academic laboratories: the PACT/JCSG+ strategy. , 2005, Acta crystallographica. Section D, Biological crystallography.

[8]  Zheng Rong Yang,et al.  RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins , 2005, Bioinform..

[9]  I. Wilson,et al.  Crystal Structure of Human Toll-Like Receptor 3 (TLR3) Ectodomain , 2005, Science.

[10]  W. M. Abbott,et al.  Optimisation and evaluation of a high-throughput mammalian protein expression system. , 2005, Protein expression and purification.

[11]  Arnon Chait,et al.  Protein crystallization: virtual screening and optimization. , 2005, Progress in biophysics and molecular biology.

[12]  Lester G. Carter,et al.  A procedure for setting up high‐throughput nanolitre crystallization experiments. Crystallization workflow for initial screening, automated storage, imaging and optimization , 2005, Acta crystallographica. Section D, Biological crystallography.

[13]  J. Andersen,et al.  Prolonged and increased expression of soluble Fc receptors, IgG and a TCR-Ig fusion protein by transiently transfected adherent 293E cells. , 2005, Journal of immunological methods.

[14]  S. Brunak,et al.  Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites. , 2005, Glycobiology.

[15]  David J Harvey,et al.  Proteomic analysis of glycosylation: structural determination of N- and O-linked glycans by mass spectrometry , 2005, Expert review of proteomics.

[16]  J. Rose,et al.  Structure of Mouse Golgi α-Mannosidase IA Reveals the Molecular Basis for Substrate Specificity among Class 1 (Family 47 Glycosylhydrolase) α1,2-Mannosidases* , 2004, Journal of Biological Chemistry.

[17]  Thomas C Terwilliger,et al.  Structures and technology for biologists , 2004, Nature Structural &Molecular Biology.

[18]  A. Kichler Gene transfer with modified polyethylenimines , 2004, The journal of gene medicine.

[19]  Raymond A Dwek,et al.  Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding. , 2003, Glycobiology.

[20]  David I. Stuart,et al.  A procedure for setting up high-throughput nanolitre crystallization experiments. II. Crystallization results , 2003 .

[21]  T. Koide,et al.  N-linked oligosaccharide processing, but not association with calnexin/calreticulin is highly correlated with endoplasmic reticulum-associated degradation of antithrombin Glu313-deleted mutant. , 2003, Archives of biochemistry and biophysics.

[22]  Roland Contreras,et al.  Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[23]  J. Norton,et al.  A novel immunoglobulin superfamily receptor (19A) related to CD2 is expressed on activated lymphocytes and promotes homotypic B-cell adhesion. , 2002, The Biochemical journal.

[24]  Y. Durocher,et al.  High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. , 2002, Nucleic acids research.

[25]  D. Kuntz,et al.  Structure of Golgi α‐mannosidase II: a target for inhibition of growth and metastasis of cancer cells , 2001, The EMBO journal.

[26]  A. Herscovics,et al.  N-Glycan processing by a lepidopteran insect α1,2-mannosidase , 2000 .

[27]  A. Varki,et al.  Evolutionary considerations in relating oligosaccharide diversity to biological function. , 1999, Glycobiology.

[28]  J. Sodroski,et al.  Probability Analysis of Variational Crystallization and Its Application to gp120, The Exterior Envelope Glycoprotein of Type 1 Human Immunodeficiency Virus (HIV-1)* , 1999, The Journal of Biological Chemistry.

[29]  R. Parekh,et al.  Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. , 1995, Analytical biochemistry.

[30]  D I Stuart,et al.  Ligand Binding by the Immunoglobulin Superfamily Recognition Molecule CD2 Is Glycosylation-independent (*) , 1995, The Journal of Biological Chemistry.

[31]  R. Beijersbergen,et al.  Cell-cell adhesion mediated by a receptor-like protein tyrosine phosphatase. , 1993, The Journal of biological chemistry.

[32]  R. Spiro,et al.  Characterization of endomannosidase inhibitors and evaluation of their effect on N-linked oligosaccharide processing during glycoprotein biosynthesis. , 1993, The Journal of biological chemistry.

[33]  D. Stuart,et al.  Expression of soluble recombinant glycoproteins with predefined glycosylation: application to the crystallization of the T-cell glycoprotein CD2. , 1993, Protein engineering.

[34]  R. Spiro,et al.  Characterization of the endomannosidase pathway for the processing of N-linked oligosaccharides in glucosidase II-deficient and parent mouse lymphoma cells. , 1992, The Journal of biological chemistry.

[35]  Richard Axel,et al.  Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 Å resolution , 1992, Cell.

[36]  M. Amiot,et al.  Expression of the Blast-1 activation/adhesion molecule and its identification as CD48. , 1991, Journal of immunology.

[37]  G. Kaushal,et al.  Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I. , 1990, The Journal of biological chemistry.

[38]  R. Spiro,et al.  Demonstration that Golgi endo-alpha-D-mannosidase provides a glucosidase-independent pathway for the formation of complex N-linked oligosaccharides of glycoproteins. , 1990, The Journal of biological chemistry.

[39]  A. Barclay,et al.  High level expression in Chinese hamster ovary cells of soluble forms of CD4 T lymphocyte glycoprotein including glycosylation variants. , 1990, The Journal of biological chemistry.

[40]  P. Heinrich,et al.  Effect of swainsonine on the processing of the asparagine-linked carbohydrate chains of alpha 1-antitrypsin in rat hepatocytes. Evidence for the formation of hybrid oligosaccharides. , 1983, The Journal of biological chemistry.

[41]  J. Behr,et al.  Polyethylenimine (PEI). , 2005, Advances in genetics.

[42]  S. Geisse,et al.  Large-scale Transient Transfection of Mammalian Cells: A Newly Emerging Attractive Option for Recombinant Protein Production , 2005, Journal of Structural and Functional Genomics.

[43]  A. Herscovics,et al.  N-Glycan processing by a lepidopteran insect alpha1,2-mannosidase. , 2000, Glycobiology.

[44]  D. Stuart,et al.  Effects of N‐butyldeoxynojirimycin and the Lec3.2.8.1 mutant phenotype on N‐glycan processing in Chinese hamster ovary cells: Application to glycoprotein crystallization , 1999, Protein science : a publication of the Protein Society.