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Structural Dynamics (Melville, N.Y.)|March 15, 2019
Time-resolved x-ray crystallography capture of a slow reaction tetrahydrofolate intermediateHongnan Cao, Jeffrey Skolnick
Journal of Chemical Information and Modeling|March 16, 2021
FRAGSITE: A Fragment-Based Approach for Virtual Ligand ScreeningHongyi Zhou, Hongnan Cao, Jeffrey Skolnick
Journal of the American Chemical Society|July 19, 2011
X-ray crystal structure of arsenite-inhibited xanthine oxidase: μ-sulfido,μ-oxo double bridge between molybdenum and arsenic in the active siteHongnan Cao, James Hall, Russ Hille
Biochemistry|January 9, 2014
Substrate orientation and specificity in xanthine oxidase: crystal structures of the enzyme in complex with indole-3-acetaldehyde and guanineHongnan Cao, James Hall, Russ Hille
Journal of Chemical Information and Modeling|October 3, 2018
FINDSITE<sup>comb2.0</sup>: A New Approach for Virtual Ligand Screening of Proteins and Virtual Target Screening of BiomoleculesHongyi Zhou, Hongnan Cao, Jeffrey Skolnick
The Journal of Biological Chemistry|July 10, 2010
Substrate orientation and catalytic specificity in the action of xanthine oxidase: the sequential hydroxylation of hypoxanthine to uric acidHongnan Cao, James M Pauff, Russ Hille
The Journal of Biological Chemistry|December 26, 2008
Substrate Orientation and Catalysis at the Molybdenum Site in Xanthine Oxidase: CRYSTAL STRUCTURES IN COMPLEX WITH XANTHINE AND LUMAZINEJames M Pauff, Hongnan Cao, Russ Hille
Journal of Natural Products|July 26, 2014
X-ray crystal structure of a xanthine oxidase complex with the flavonoid inhibitor quercetinHongnan Cao, James M Pauff, Russ Hille
Communications Biology|December 20, 2018
The crystal structure of a tetrahydrofolate-bound dihydrofolate reductase reveals the origin of slow product releaseHongnan Cao, Mu Gao, Hongyi Zhou, et al.
The Journal of Biological Chemistry|September 27, 2014
The reductive half-reaction of xanthine dehydrogenase from Rhodobacter capsulatus: the role of Glu232 in catalysisJames Hall, Stefan Reschke, Hongnan Cao, et al.
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