NMR-based design and evaluation of novel bidentate inhibitors of the protein tyrosine phosphatase YopH(548 views) Leone M, Barile E, Vazquez J, Mei A, Guiney D, Dahl R, Pellecchia M
Chem Biol Drug Des (ISSN: 1747-0277, 1747-0285), 2010 Jul; 76(1): 10-16.
Keywords: Nmr Screening, Protein Tyrosine Phosphatase, Spin Label, Yersinia, Yoph, Antibiotic Agent, Bacterial Protein, Bidentate Derivative, Furanyl Salicylate Derivative, Protein Tyrosine Phosphatase Inhibitor, Protein Yoph, Unclassified Drug, Antibacterial Activity, Article, Cell Membrane Permeability, Controlled Study, Drug Binding Site, Drug Design, Drug Screening, Drug Structure, Drug Synthesis, Drug Targeting, Human, Human Cell, Molecular Docking, Molecular Probe, Nuclear Magnetic Resonance Spectroscopy, Priority Journal, Spin Labeling, Structure Activity Relation, Yersinia Pestis, Yersinia Pseudotuberculosis, Bacterial Outer Membrane Proteins, Hela Cells, Models, Biomolecular, Small Molecule Libraries, Yersinia Infections,
Affiliations: *** IBB - CNR ***
Infectious and Inflammatory Disease Center and Cancer Center, Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Rd, San Diego, CA 92037, United States
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Naples, Italy
Department of Medicine, University of California at San Diego, 9500 Gilman Drive, San Diego, CA 92093, United States
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Cornelis, G. R., Type III secretion: A bacterial device for close combat with cells of their eukaryotic host (2000) Philos Trans R Soc Lond B Biol Sci, 355, pp. 681-693
Cornelis, G. R., Molecular and cell biology aspects of plague (2000) Proc Natl Acad Sci USA, 97, pp. 8778-8783
Black, D. S., Marie-Cardine, A., Schraven, B., Bliska, J. B., The Yersinia tyrosine phosphatase YopH targets a novel adhesion-regulated signalling complex in macrophages (2000) Cell Microbiol, 2, pp. 401-414
Black, D. S., Montagna, L. G., Zitsmann, S., Bliska, J. B., Identification of an amino-terminal substrate-binding domain in the Yersinia tyrosine phosphatase that is required for efficient recognition of focal adhesion targets (1998) Mol Microbiol, 29, pp. 1263-1274
Guan, K. L., Dixon, J. E., Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia (1990) Science, 249, pp. 553-556
Bubeck, S. S., Dube, P. H., Yersinia pestis CO92 delta yopH is a potent live, attenuated plague vaccine (2007) Clin Vaccine Immunol, 14, pp. 1235-1238
Eldridge, M. D., Murray, C. W., Auton, T. R., Paolini, G. V., Mee, R. P., Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes (1997) J Comput Aided Mol des, 11, pp. 425-445
Wu, B., Rega, M. F., Wei, J., Yuan, H., Dahl, R., Zhang, Z., Discovery and binding studies on a series of novel Pin1 ligands (2009) Chem Biol Drug des, 73, pp. 369-379
Browne, S. H., Lesnick, M. L., Guiney, D. G., Genetic requirements for salmonella-induced cytopathology in human monocyte-derived macrophages (2002) Infect Immun, 70, pp. 7126-7135
Hajduk, P. J., Dinges, J., Miknis, G. F., Merlock, M., Middleton, T., Kempf, D. J., NMR-based discovery of lead inhibitors that block DNA binding of the human papillomavirus E2 protein (1997) J Med Chem, 40, pp. 3144-3150
Hajduk, P. J., SAR by NMR: Putting the pieces together (2006) Mol Interv, 6, pp. 266-272
NMR-based design and evaluation of novel bidentate inhibitors of the protein tyrosine phosphatase YopH