NMR-based design and evaluation of novel bidentate inhibitors of the protein tyrosine phosphatase YopH(901 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
References: Not available.
NMR-based design and evaluation of novel bidentate inhibitors of the protein tyrosine phosphatase YopH