William BartonSummaryAffiliation: Virginia Commonwealth University Country: USA Publications
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Publications
Highly efficient selenomethionine labeling of recombinant proteins produced in mammalian cellsWilliam A Barton
Department of Biochemistry, Virginia Commonwealth University, Richmond, 23298, USA
Protein Sci 15:2008-13. 2006..We therefore evaluated several variables that play roles in determining incorporation levels and report here a simple protocol for selenomethionine modification of proteins in mammalian cells routinely yielding >90% labeling efficiency...
Tie1-Tie2 interactions mediate functional differences between angiopoietin ligandsTom C M Seegar
Department of Biochemistry and Molecular Biology, Virginia Commonwealth University, 1101 East Marshall Street, Richmond, VA 23298, USA
Mol Cell 37:643-55. 2010..We further demonstrate that the Tie1-Tie2 interactions are dynamic, inhibitory, and differentially modulated by angiopoietin-1 and -2. Based on the available data, we propose a unified model for angiopoietin-induced Tie2 signaling...
Expanding pyrimidine diphosphosugar libraries via structure-based nucleotidylyltransferase engineeringWilliam A Barton
Cellular Biochemistry and Biophysics Program, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA
Proc Natl Acad Sci U S A 99:13397-402. 2002..In aggregate, our results provide valuable blueprints for altering nucleotidylyltransferase specificity by design, which is the first step toward in vitro glycorandomization...
Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmCJacob Lesniak
Joan and Sanford I Weill Graduate School of Medical Sciences of Cornell University, New York, New York 10021, USA
Protein Sci 12:2838-43. 2003....
Structure-based enzyme engineering and its impact on in vitro glycorandomizationJon S Thorson
Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, University of Wisconsin - Madison, Madison, WI 53705, USA
Chembiochem 5:16-25. 2004
Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteinsWilliam A Barton
Cellular Biochemistry and Biophysics Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA
EMBO J 22:3291-302. 2003..The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex...
Crystal structure of the ephrin-B1 ectodomain: implications for receptor recognition and signalingDimitar B Nikolov
Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA
Biochemistry 44:10947-53. 2005..The implications of the ephrin-B1 structure, in context of available ephrin-B1 mutagenesis data, for the mechanism of Eph-ephrin recognition and signaling initiation are discussed...
Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in transPeter W Janes
Department of Biochemistry and Molecular Biology, PO Box 13D, Monash University, Victoria 3800, Australia
Cell 123:291-304. 2005..Our data suggest a simple mechanism for regulating ADAM10-mediated ephrin proteolysis, which ensures that only Eph bound ephrins are recognized and cleaved...
Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complexWilliam A Barton
Structural Biology Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, New York 10021, USA
Nat Struct Mol Biol 13:524-32. 2006..Analysis of the structures and structure-based mutagenesis provide insight into the mechanism of receptor activation and support the hypothesis that all angiopoietins interact with Tie2 in a structurally similar manner...
Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein OhrJacob Lesniak
Joan and Sanford I Weill Graduate School of Medical Sciences of Cornell University, New York City, NY 10021, USA
EMBO J 21:6649-59. 2002..We propose that the Ohr catalytic mechanism is similar to that of the structurally unrelated peroxiredoxins, directly utilizing highly reactive cysteine thiol groups to elicit hydroperoxide reduction...
Structure of the angiopoietin-2 receptor binding domain and identification of surfaces involved in Tie2 recognitionWilliam A Barton
Structural Biology Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, New York 10021, USA
Structure 13:825-32. 2005..The structure reveals a fibrinogen fold with a unique C-terminal P domain. Conservation analysis and structure-based mutagenesis identify a groove on the Ang2 molecular surface that mediates receptor recognition...
Research Grants
- Biochemical and Biophysical Analysis of Angiopoietin SignalingWilliam A Barton; Fiscal Year: 2010....
