Gregory A. Petsko - Concepedia

Author

Gregory A. Petsko

Brandeis University

Also Known As

Gregory A. Petsko, Gregory A.Petsko, Gregory A. Petsko, John A. Gerlt

Publications

2.3K

Citations

H-Index

Concepts

All Affiliations

Brandeis University University of California, San Francisco Harvard University Massachusetts Institute of Technology University of Maryland, College Park

About

Gregory A. Petsko is an author at Brandeis University specializing in natural sciences, molecular biology, and biochemistry.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Natural Sciences	5	5	492
2	Biochemistry	3	3	236
3	Engineering	1	1	68
4	Health Sciences	1	1	41
5	Medicine	1	1	164

Gregory A. Petsko

Publications

921

Citations

H-Index

Page 1

	Year	Citations
Crystal Cryocooling Distorts Conformational Heterogeneity in a Model Michaelis Complex of DHFR D.A. Keedy, Henry van den Bedem, David A. Sivak, Structure Crystal StructureNatural SciencesProtein X-ray CrystallographyConformational StudyStructural Biology	2014	164
Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism Elliott Nickbarg, R. Davenport, Gregory A. Petsko, Biochemistry	1988	128
Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous David J. Neidhart, George L. Kenyon, John A. Gerlt, Nature Cellular EnzymologyBiochemistryNatural SciencesBiocatalysisMandelate Racemase	1990	127
Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95 Elizabeth A. Komives, Louise Chang, Elias Lolis, Biochemistry	1991	123
Analogous inhibitors of elastase do not always bind analogously Carla Mattos, Bjarne Rasmussen, Xiaochun Ding, Nature Structural & Molecular Biology Natural SciencesMechanism Of ActionMolecular BiologyProtein EngineeringAnalogous Inhibitors	1994	92
Role of the Divalent Metal Ion in Sugar Binding, Ring Opening, and Isomerization by D-Xylose Isomerase: Replacement of a Catalytic Metal by an Amino Acid Karen N. Allen, Arnon Lavie, Arthur Glasfeld, Biochemistry	1994	77
Mechanism of the Reaction Catalyzed by Mandelate Racemase: Importance of Electrophilic Catalysis by Glutamic Acid 317 Bharati Mitra, Abraham T. Kallarakal, John W. Kozarich, Biochemistry EngineeringAldo-keto ReductaseMandelate RacemaseMolecular BiologyElectrophilic Catalysis	1995	68
Crystal Structure of the K12M/G15A Triosephosphate Isomerase Double Mutant and Electrostatic Analysis of the Active Site Diane Joseph‐McCarthy, Elias Lolis, Elizabeth A. Komives, Biochemistry	1994	42
Photolysis and deacylation of inhibited chymotrypsin Barry Stoddard, John D. Bruhnke, Paula M. Koenigs, Biochemistry Inhibited ChymotrypsinPhotochemistryBiochemistryX-ray Diffraction StudiesNatural Sciences	1990	41
The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase Constance J. Jeffery, Lisa M. Gloss, Gregory A. Petsko, Protein Engineering Design and Selection	2000	31

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