Affiliation: Virginia Commonwealth University
- 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...
- Biochemical and Biophysical Analysis of Angiopoietin SignalingWilliam A Barton; Fiscal Year: 2010....