Andrew D. Mesecar
Affiliations: | Molecular Biosciences | Purdue University, West Lafayette, IN, United States |
Area:
molecular mechanisms and function of therapeutic enzymes and proteinsWebsite:
http://www.chem.purdue.edu/people/faculty/faculty.asp?itemID=91Google:
"Andrew D. Mesecar"Bio:
http://www.bio.purdue.edu/molecular_biosciences/directory.php?refID=770
Mean distance: 7.83 | S | N | B | C | P |
Parents
Sign in to add mentor| Thomas L. Nowak | grad student | 1995 | Notre Dame | |
| (Kinetic responses and conformational changes required for yeast pyruvate kinase activation and catalysis) | ||||
| Daniel E. Koshland | post-doc | 1995-1998 | UC Berkeley | |
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Publications
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| Ghosh AK, Shahabi D, Imhoff MEC, et al. (2023) SARS-CoV-2 papain-like protease (PLpro) inhibitory and antiviral activity of small molecule derivatives for drug leads. Bioorganic & Medicinal Chemistry Letters. 96: 129489 |
| Bose S, Steussy CN, López-Pérez D, et al. (2023) Targeting Enterococcus faecalis HMG-CoA reductase with a non-statin inhibitor. Communications Biology. 6: 360 |
| Ghosh AK, Shahabi D, Yadav M, et al. (2021) Chloropyridinyl Esters of Nonsteroidal Anti-Inflammatory Agents and Related Derivatives as Potent SARS-CoV-2 3CL Protease Inhibitors. Molecules (Basel, Switzerland). 26 |
| Ghosh AK, Raghavaiah J, Shahabi D, et al. (2021) Indole Chloropyridinyl Ester-Derived SARS-CoV-2 3CLpro Inhibitors: Enzyme Inhibition, Antiviral Efficacy, Structure-Activity Relationship, and X-ray Structural Studies. Journal of Medicinal Chemistry |
| Yen YC, Kammeyer A, Jensen KC, et al. (2019) Development of an efficient enzyme production and structure-based discovery platform for BACE1 inhibitors. Biochemistry |
| Hjortland NM, Mesecar AD. (2016) Steady-state kinetic studies reveal that the anti-cancer target Ubiquitin-Specific Protease 17 (USP17) is a highly efficient deubiquitinating enzyme. Archives of Biochemistry and Biophysics. 612: 35-45 |
| St John SE, Tomar S, Stauffer SR, et al. (2015) Targeting zoonotic viruses: Structure-based inhibition of the 3C-like protease from bat coronavirus HKU4--The likely reservoir host to the human coronavirus that causes Middle East Respiratory Syndrome (MERS). Bioorganic & Medicinal Chemistry. 23: 6036-48 |
| Báez-Santos YM, St John SE, Mesecar AD. (2015) The SARS-coronavirus papain-like protease: structure, function and inhibition by designed antiviral compounds. Antiviral Research. 115: 21-38 |
| Zhai X, Go MK, O'Donoghue AC, et al. (2014) Enzyme architecture: the effect of replacement and deletion mutations of loop 6 on catalysis by triosephosphate isomerase. Biochemistry. 53: 3486-501 |
| Báez-Santos YM, Barraza SJ, Wilson MW, et al. (2014) X-ray structural and biological evaluation of a series of potent and highly selective inhibitors of human coronavirus papain-like proteases. Journal of Medicinal Chemistry. 57: 2393-412 |