R. Andrew Byrd
Structural Biophysics Laboratory
The Center for Cancer Research
United States of America
Biography
Dr. Byrd received his Ph.D. from the University of South Carolina in 1977, specializing in high-resolution biomolecular NMR. He was a postdoctoral fellow and subsequently a research officer in the Molecular Biophysics Laboratory of the National Research Council of Canada, where he investigated biological membranes by solid-state NMR. Following a period as a senior investigator at the Center for Drugs and Biologics/FDA, he established the Macromolecular NMR Section of the ABL-Basic Research Program at the NCI-Frederick in 1992. He chaired the Experimental NMR Conference in 1992 and co-chaired the International Conference on Magnetic Resonance in Biological Systems in 1996. Dr. Byrd has been the Chief of the Structural Biophysics Laboratory in the Center for Cancer Research, NCI since 1999. He has served on multiple drug discovery panels for NCI and served as the Director of the Molecular Discovery Program from 2009-2011.
Research Interest
Biomedical Engineering and Biophysics, Molecular Biology and Biochemistry, Structural Biology
Publications
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Zwahlen C, Gardner KH, Sarma SP, Horita DA, Byrd RA, et al. (1998) An NMR experiment for measuring methyl-methyl NOEs in 13C-labeled proteins with high resolution. J. Am. Chem. Soc. 120: 7617-25.
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Gaponenko V, Sarma SP, Altieri AS, Horita DA, Li J, et al. (2004) Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints. J. Biomol. NMR. 28: 205-12.
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Cecchi F, Pajalunga D, Fowler CA, Uren A, Rabe DC, et al. (2012) Targeted disruption of heparan sulfate interaction with hepatocyte and vascular endothelial growth factors blocks normal and oncogenic signaling. Cancer Cell. 22: 250-62.
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Das R, Liang YH, Mariano J, Li J, Huang T, et al. (2013) Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine. EMBO J. 32: 2504-16.
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Das R, Mariano J, Tsai YC, Kalathur RC, Kostova Z, et al. (2009) Allosteric activation of E2-RING finger-mediated ubiquitylation by a structurally defined specific E2-binding region of gp78. Mol. Cell. 34: 674-85.
