Virtual International Authority File


Petsko, Gregory A. Sudoc [ABES], France National Diet Library, Japan NII (Japan) National Library of the Netherlands National Library of Catalonia National Library of France BIBSYS Library of Congress/NACO National Library of Israel ISNI

Gregory Petsko American academic Wikidata

Petsko, Gregory A., 1948- National Library of the Czech Republic NUKAT Center of Warsaw University Library

VIAF ID: 39628851 (Personal)


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Title Sources
Funky, not junky Wikidata
Galileo's stepchildren Wikidata
Good chemistry Wikidata
The grail problem. Wikidata
Grain of truth Wikidata
Gregory Petsko dự đoán về đại dịch các căn bệnh thần kinh sắp đến Wikidata
Gregory Petsko ile yaklaşan nörolojik salgın üzerine Wikidata
Gregory Petsko:将要到来的神经流感 Wikidata
The guards themselves Wikidata
H5N1. Wikidata
Half right Wikidata
Homologuephobia Wikidata
How may you help me? Wikidata
The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase Wikidata
Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms" Wikidata
Interaction of a peptidomimetic aminimide inhibitor with elastase Wikidata
Intrinsic motions along an enzymatic reaction trajectory Wikidata
Ira Wikidata
Judgement call Wikidata
Karā zusetsu tanpakushitsu no kōzō to kinō : Genomu jidai no apurōchi National Diet Library, Japan
L'epidemia neurologica in arrivo: Gregory Petsko Wikidata
The life aquatic. Wikidata
Live and let diet Wikidata
Location, location, location. Wikidata
Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate modeling and active site mutations Wikidata
Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant Wikidata
Metal-Dependent Function of a Mammalian Acireductone Dioxygenase Wikidata
Model behavior. Wikidata
Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability Wikidata
No place like Ome Wikidata
no98014393 National Diet Library, Japan
Our own petards. Wikidata
Perpetual motion of the worst kind. Wikidata
Pharmacogenomics arrives Wikidata
Photolysis and deacylation of inhibited chymotrypsin Wikidata
Probing the Active Center of Benzaldehyde Lyase with Substitutions and the Pseudosubstrate Analogue Benzoylphosphonic Acid Methyl Ester † Wikidata
Protein structure and function Sudoc [ABES], France National Diet Library, Japan National Library of the Netherlands Wikidata National Library of Catalonia National Library of France NUKAT Center of Warsaw University Library BIBSYS Library of Congress/NACO
The refined crystal structure of subtilisin Carlsberg at 2.5 A resolution Wikidata
Rising in the East Wikidata
The road worrier Wikidata
The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: mechanistic and crystallographic evidence for stereospecific alkylation by (R)-alpha-phenylglycidate Wikidata
The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase Wikidata
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 Wikidata
The role of water in the catalytic efficiency of triosephosphate isomerase Wikidata
The Rosetta stone. Wikidata
Seek and ye shall maybe find. Wikidata
Size doesn't matter. Wikidata
Sleeping dogs Wikidata
The slide rule and the calculator. Wikidata
Snapshot of a Reaction Intermediate: Analysis of Benzoylformate Decarboxylase in Complex with a Benzoylphosphonate Inhibitor † Wikidata
Solving crystal structures, 1997: National Library of Israel Library of Congress/NACO
Still no flying cars Wikidata
Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors Wikidata
The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase Wikidata
Structural Consequences of Cysteinylation of Cu/Zn-Superoxide Dismutase Wikidata
Structural mechanism of enoyl-CoA hydratase: three atoms from a single water are added in either an E1cb stepwise or concerted fashion Wikidata
Structure and activity of two photoreversible cinnamates bound to chymotrypsin Wikidata
Structure and specificity of a quorum-quenching lactonase (AiiB) from Agrobacterium tumefaciens Wikidata
Structure of a eukaryotic thiaminase I Wikidata
Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase Wikidata
Structure of acid beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease Wikidata
Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis Wikidata
Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis Wikidata
Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway Wikidata
Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae Wikidata
Testing Geometrical Discrimination within an Enzyme Active Site: Constrained Hydrogen Bonding in the Ketosteroid Isomerase Oxyanion Hole Wikidata
Trinity. Wikidata
Tsunami Wikidata
Twilight of a hero Wikidata
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme Wikidata
The usual suspects Wikidata
War and peace Wikidata
What's in a name? Wikidata
Who owns the data? Wikidata
Winter, plague and pestilence. Wikidata
Zinc Coordination Geometry and Ligand Binding Affinity: The Structural and Kinetic Analysis of the Second-Shell Serine 228 Residue and the Methionine 180 Residue of the Aminopeptidase from Vibrio proteolyticus † Wikidata
Грегори Петско о грядущей неврологической эпидемии Wikidata
گریگوری پتسکو در مورد اپیدمی عصبی جدید صحبت میکند. Wikidata
그레고리 페츠코, 다가오는 신경학적 질병의 창궐에 대하여 Wikidata
カラー図説タンパク質の構造と機能 : ゲノム時代のアプローチ National Diet Library, Japan NII (Japan)
グレゴリー・ペトスコの来るべき神経疾患の流行における考え Wikidata

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