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Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor.
Metallo beta-lactamase enzymes confer antibiotic resistance to bacteria by catalyzing the hydrolysis of beta-lactam antibiotics. This relatively new form of resistance is spreading unchallenged asExpand
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Discovery of RG7388, a potent and selective p53-MDM2 inhibitor in clinical development.
Restoration of p53 activity by inhibition of the p53-MDM2 interaction has been considered an attractive approach for cancer treatment. However, the hydrophobic protein-protein interaction surfaceExpand
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Activation of the p53 pathway by small-molecule-induced MDM2 and MDMX dimerization
Activation of p53 tumor suppressor by antagonizing its negative regulator murine double minute (MDM)2 has been considered an attractive strategy for cancer therapy and several classes of p53-MDM2Expand
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  • Open Access
Identification of 1,5-naphthyridine derivatives as a novel series of potent and selective TGF-beta type I receptor inhibitors.
Optimization of the screening hit 1 led to the identification of novel 1,5-naphthyridine aminothiazole and pyrazole derivatives, which are potent and selective inhibitors of the transforming growthExpand
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  • Open Access
Refined structures of beta-ketoacyl-acyl carrier protein synthase III.
beta-Ketoacyl-acyl carrier protein synthase III (FabH) is a condensing enzyme that plays central roles in fatty acid biosynthesis. Three-dimensional structures of E. coli FabH in the presence andExpand
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Crystal structure and substrate specificity of the β‐ketoacyl‐acyl carrier protein synthase III (FabH) from Staphylococcus aureus
β‐Ketoacyl‐ACP synthase III (FabH), an essential enzyme for bacterial viability, catalyzes the initiation of fatty acid elongation by condensing malonyl‐ACP with acetyl‐CoA. We have determined theExpand
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Novel subunit—subunit interactions in the structure of glutamine synthetase
We present an atomic model for glutamine synthetase, an enzyme of central importance in bacterial nitrogen metabolism, from X–ray crystallography. The 12 identical subunits are arranged as the carbonExpand
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Structure of the C-terminally truncated human ProMMP9, a gelatin-binding matrix metalloproteinase.
The X-ray crystal structure of the proform of human matrix metalloproteinase MMP9 has been solved to 2.5 A resolution. The construct includes the prodomain, the catalytic domain and three FnIIExpand
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  • Open Access
Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK.
Bacterial enoyl-ACP reductase (FabI) is responsible for catalyzing the final step of bacterial fatty acid biosynthesis and is an attractive target for the development of novel antibacterial agents.Expand
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Stereochemical mechanism of action for thymidylate synthase based on the X-ray structure of the covalent inhibitory ternary complex with 5-fluoro-2'-deoxyuridylate and 5,10-methylenetetrahydrofolate.
The structure of the Escherichia coli thymidylate synthase (TS) covalent inhibitory ternary complex consisting of enzyme, 5-fluoro-2'-deoxyuridylate (FdUMP) and 5,10-methylene tetrahydrofolateExpand
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