John P. Richard
Affiliations: | Chemistry | State University of New York, Buffalo, Buffalo, NY, United States |
Website:
https://www.acsu.buffalo.edu/~jrichard/richard.html#educationGoogle:
"John P. Richard"Bio:
http://rave.ohiolink.edu/etdc/view?acc_num=osu1487088320404038
Parents
Sign in to add mentor| Perry A. Frey | grad student | 1979 | Ohio State (Chemistry Tree) | |
| (Studies on the stereochemical course of enzyme catalyzed thiophosphoryl group transfer.) | ||||
| William P. Jencks | post-doc | 1979-1982 | Brandeis (Chemistry Tree) | |
| Irwin A. Rose | research scientist | 1982-1984 | Fox Chase Cancer Center (Chemistry Tree) | |
Children
Sign in to add trainee| Tiago A.S. Brandão | grad student | SUNY Buffalo (Chemistry Tree) | |
| Swetansu B. Pattnaik | grad student | 2007 | SUNY Buffalo |
| Maybelle Go | grad student | 2004-2009 | SUNY Buffalo (Chemistry Tree) |
| Shonoi A. Barnett | grad student | 2010 | SUNY Buffalo |
| Maria Merced Malabanan | grad student | 2012 | SUNY Buffalo |
| Xiang Zhai | grad student | 2015 | SUNY Buffalo |
| Bogdana Goryanova | grad student | 2008-2015 | SUNY Buffalo |
| Archie C. Reyes | grad student | 2011-2016 | SUNY Buffalo |
| Patrick Lista Fernandez | post-doc | 2020- | SUNY Buffalo (Chemistry Tree) |
BETA: Related publications
See more...
Publications
|
You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect. |
| Yeary PE, Richard JP. (2024) Changes in Mechanism and Transition State Structure for Solvolysis Reactions of Ring Substituted Benzyl Chlorides in Aqueous Solution. Journal of Physical Organic Chemistry. 37 |
| Cristobal JR, Hegazy R, Richard JP. (2024) Glycerol 3-Phosphate Dehydrogenase: Role of the Protein Conformational Change in Activation of a Readily Reversible Enzyme-Catalyzed Hydride Transfer Reaction. Biochemistry |
| Hegazy R, Richard JP. (2023) Triosephosphate Isomerase: The Crippling Effect of the P168A/I172A Substitution at the Heart of an Enzyme Active Site. Biochemistry |
| Cristobal JR, Nagorski RW, Richard JP. (2023) Utilization of Cofactor Binding Energy for Enzyme Catalysis: Formate Dehydrogenase-Catalyzed Reactions of the Whole NAD Cofactor and Cofactor Pieces. Biochemistry |
| Cristobal JR, Richard JP. (2023) Kinetics and mechanism for enzyme-catalyzed reactions of substrate pieces. Methods in Enzymology. 685: 95-126 |
| Hegazy R, Cordara G, Wierenga RK, et al. (2023) The Role of Asn11 in Catalysis by Triosephosphate Isomerase. Biochemistry |
| Fernandez PL, Richard JP. (2022) Adenylate Kinase-Catalyzed Reactions of AMP in Pieces: Specificity for Catalysis at the Nucleoside Activator and Dianion Catalytic Sites. Biochemistry |
| Richard JP. (2022) Enabling Role of Ligand-Driven Conformational Changes in Enzyme Evolution. Biochemistry. 61: 1533-1542 |
| Cristobal JR, Richard JP. (2022) Glycerol-3-Phosphate Dehydrogenase: The K120 and K204 Side Chains Define an Oxyanion Hole at the Enzyme Active Site. Biochemistry |
| Pereira MS, de Araújo SS, Nagem RAP, et al. (2022) The role of remote flavin adenine dinucleotide pieces in the oxidative decarboxylation catalyzed by salicylate hydroxylase. Bioorganic Chemistry. 119: 105561 |