Wentao Fu
University of Illinois at Chicago
9 Papers
49 Citations
Wentao Fu is an academic researcher from University of Illinois at Chicago. The author has contributed to research in topics: Oxyanion hole & Protease. The author has an hindex of 7, co-authored 9 publications.
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Papers
A noncovalent class of papain-like protease/deubiquitinase inhibitors blocks SARS virus replication
Kiira Ratia,Scott D. Pegan,Jun Takayama,Katrina Sleeman,Melissa M. Coughlin,Surendranath Baliji,Rima Chaudhuri,Wentao Fu,Bellur S. Prabhakar,Michael E. Johnson,Susan C. Baker,Arun K. Ghosh,Andrew D. Mesecar +12 more
TL;DR: Findings provide proof-of-principle that PLpro is a viable target for development of antivirals directed against SARS-CoV, and that potent noncovalent cysteine protease inhibitors can be developed with specificity directed toward pathogenic deubiquitinating enzymes without inhibiting host DUBs.
497
Design and Synthesis of Peptidomimetic Severe Acute Respiratory Syndrome Chymotrypsin-like Protease Inhibitors
Arun K. Ghosh,Kai Xi,Kiira Ratia,Bernard D. Santarsiero,Wentao Fu,Brian H. Harcourt,Paul A. Rota,Susan C. Baker,Michael E. Johnson,Andrew D. Mesecar +9 more
TL;DR: These inhibitors exhibited antiviral activity against SARS-CoV in infected cells in the micromolar range and provided important drug-design templates for the design of small-molecule inhibitors.
132
Structure-based design, synthesis, and biological evaluation of peptidomimetic SARS-CoV 3CLpro inhibitors.
Arun K. Ghosh,Kai Xi,Valerie Grum-Tokars,Xiao Ming Xu,Kiira Ratia,Wentao Fu,Katherine V. Houser,Susan C. Baker,Michael E. Johnson,Andrew D. Mesecar +9 more
TL;DR: In this article, a series of peptidomimetic severe acute respiratory syndrome-coronavirus chymotrypsin-like protease inhibitors were designed and synthesized based upon X-ray crystal structure of inhibitor 1 bound to SARS-CoV 3CLpro.
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An oxyanion-hole selective serine protease inhibitor in complex with trypsin.
TL;DR: p-amidinophenylmethylphosphinic acid was designed, synthesized and crystallized in complex with trypsin to study interactions with the oxyanion hole at the S1 site and shows improved activity.
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Glutamate racemase dimerization inhibits dynamic conformational flexibility and reduces catalytic rates.
Shahila Mehboob,Liang Guo,Wentao Fu,Anuradha Mittal,Tiffany Yau,Kent Truong,Mary G. Johlfs,Fei Long,Leslie W.-M. Fung,Michael E. Johnson +9 more
TL;DR: The authors' steered molecular dynamics simulations and normal-mode analysis results indicate that the monomeric form of the enzyme is more flexible than the native dimeric form, and suggest that increased flexibility may accelerate catalysis.
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