Publications

Consolidation of glycosyl hydrolase family 30: a dual domain 4/7 hydrolase family consisting of two structurally distinct groups.
St John FJ, González JM, Pozharski E. 2010. Consolidation of glycosyl hydrolase family 30: a dual domain 4/7 hydrolase family consisting of two structurally distinct groups. FEBS letters 584(21): 4435-41. DOI: 10.1016/j.febslet.2010.09.051
Performance of ZDOCK and ZRANK in CAPRI rounds 13-19.
Hwang H, Vreven T, Pierce BG, Hung JH, Weng Z. 2010. Performance of ZDOCK and ZRANK in CAPRI rounds 13-19. Proteins 78(15): 3104-10. DOI: 10.1002/prot.22764
Chitosan: an integrative biomaterial for lab-on-a-chip devices.
Koev ST, Dykstra PH, Luo X, Rubloff GW, Bentley WE, Payne GF, Ghodssi R. 2010. Chitosan: an integrative biomaterial for lab-on-a-chip devices. Lab on a chip 10(22): 3026-42. DOI: 10.1039/c0lc00047g
Elicitation of structure-specific antibodies by epitope scaffolds.
Ofek G, Guenaga FJ, Schief WR, Skinner J, Baker D, Wyatt R, Kwong PD. 2010. Elicitation of structure-specific antibodies by epitope scaffolds. Proceedings of the National Academy of Sciences of the United States of America 107(42): 17880-7. DOI: 10.1073/pnas.1004728107
Accurate and adequate spatiotemporal expression and localization of RPW8.2 is key to activation of resistance at the host-pathogen interface.
Wang W, Berkey R, Wen Y, Xiao S. 2010. Accurate and adequate spatiotemporal expression and localization of RPW8.2 is key to activation of resistance at the host-pathogen interface. Plant signaling & behavior 5(8): 1002-5.
Holo-Ni(II)HpNikR is an asymmetric tetramer containing two different nickel-binding sites.
West AL, St John F, Lopes PE, MacKerell AD, Pozharski E, Michel SL. 2010. Holo-Ni(II)HpNikR is an asymmetric tetramer containing two different nickel-binding sites. Journal of the American Chemical Society 132(41): 14447-56. DOI: 10.1021/ja104118r
Biotemplated aqueous-phase palladium crystallization in the absence of external reducing agents.
Lim JS, Kim SM, Lee SY, Stach EA, Culver JN, Harris MT. 2010. Biotemplated aqueous-phase palladium crystallization in the absence of external reducing agents. Nano letters 10(10): 3863-7. DOI: 10.1021/nl101375f
Assessing energetic contributions to binding from a disordered region in a protein-protein interaction .
Cho S, Swaminathan CP, Bonsor DA, Kerzic MC, Guan R, Yang J, Kieke MC, Andersen PS, Kranz DM, Mariuzza RA, et al. 2010. Assessing energetic contributions to binding from a disordered region in a protein-protein interaction . Biochemistry 49(43): 9256-68. DOI: 10.1021/bi1008968
The Calcium-Dependent Interaction of S100B with Its Protein Targets.
Zimmer DB, Weber DJ. 2010. The Calcium-Dependent Interaction of S100B with Its Protein Targets. Cardiovascular psychiatry and neurology 2010: . DOI: 10.1155/2010/728052
Percentile-based spread: a more accurate way to compare crystallographic models.
Pozharski E. 2010. Percentile-based spread: a more accurate way to compare crystallographic models. Acta crystallographica. Section D, Biological crystallography 66(Pt 9): 970-8. DOI: 10.1107/S0907444910027927
A structural hinge in eukaryotic MutY homologues mediates catalytic activity and Rad9-Rad1-Hus1 checkpoint complex interactions.
Luncsford PJ, Chang DY, Shi G, Bernstein J, Madabushi A, Patterson DN, Lu AL, Toth EA. 2010. A structural hinge in eukaryotic MutY homologues mediates catalytic activity and Rad9-Rad1-Hus1 checkpoint complex interactions. Journal of molecular biology 403(3): 351-70. DOI: 10.1016/j.jmb.2010.08.045
Biofabrication to build the biology-device interface.
Liu Y, Kim E, Ghodssi R, Rubloff GW, Culver JN, Bentley WE, Payne GF. 2010. Biofabrication to build the biology-device interface. Biofabrication 2(2): 022002. DOI: 10.1088/1758-5082/2/2/022002
Diffusion of interleukin-2 from cells overlaid with cytocompatible enzyme-crosslinked gelatin hydrogels.
Yung CW, Bentley WE, Barbari TA. 2010. Diffusion of interleukin-2 from cells overlaid with cytocompatible enzyme-crosslinked gelatin hydrogels. Journal of biomedical materials research. Part A 95(1): 25-32. DOI: 10.1002/jbm.a.32740
Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering.
Schwieters CD, Suh JY, Grishaev A, Ghirlando R, Takayama Y, Clore GM. 2010. Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering. Journal of the American Chemical Society 132(37): 13026-45. DOI: 10.1021/ja105485b
Studies on ligand binding to histidine triad nucleotide binding protein 1.
Bai G, Feng B, Wang JB, Pozharski E, Shapiro M. 2010. Studies on ligand binding to histidine triad nucleotide binding protein 1. Bioorganic & medicinal chemistry 18(18): 6756-62. DOI: 10.1016/j.bmc.2010.07.051