2018 - Fellow of the Royal Society, United Kingdom
Biochemistry, GTPase, Rab, GTP' and Nucleotide are his primary areas of study. His biological study deals with issues like Biophysics, which deal with fields such as Nuclear magnetic resonance spectroscopy. His studies in GTPase integrate themes in fields like Protein structure and Guanosine.
His Rab study combines topics from a wide range of disciplines, such as Transport protein, Ras superfamily, Guanine Nucleotide Dissociation Inhibitors and Prenylation. The study incorporates disciplines such as Magnesium ion, Crystallography, RHO protein GDP dissociation inhibitor, Active site and Molecule in addition to GTP'. His research integrates issues of Ran, Affinities, Stereochemistry and Weak binding in his study of Nucleotide.
His scientific interests lie mostly in Biochemistry, GTPase, Rab, Stereochemistry and Cell biology. The study of Biochemistry is intertwined with the study of Biophysics in a number of ways. In his study, which falls under the umbrella issue of GTPase, Crystallography is strongly linked to GTP'.
His research investigates the connection between Rab and topics such as Prenylation that intersect with issues in C-terminus. Roger S. Goody works mostly in the field of Stereochemistry, limiting it down to topics relating to Nucleotide and, in certain cases, Reaction rate constant and Adenylate kinase. His Enzyme research is multidisciplinary, incorporating elements of Molecular biology and Reverse transcriptase.
Roger S. Goody focuses on Rab, Cell biology, GTPase, Biochemistry and Effector. His work carried out in the field of Rab brings together such families of science as Legionella pneumophila, Vesicular transport protein, Adenylylation and Prenylation. Roger S. Goody combines topics linked to Membrane with his work on Cell biology.
His GTPase study incorporates themes from GTP-binding protein regulators, Plasma protein binding, Biophysics, Signal transduction and GTP'. His Function research extends to Biochemistry, which is thematically connected. His study in Effector is interdisciplinary in nature, drawing from both Gene duplication, Genetics, Bivalent and Endocytosis.
His primary areas of investigation include GTPase, Cell biology, Rab, Biochemistry and Vesicular transport protein. His GTPase research is multidisciplinary, incorporating perspectives in GTP-binding protein regulators, Plasma protein binding, Mutation, Adenylylation and Protein structure. His work deals with themes such as Endosome, Guanosine triphosphate, GTPase-activating protein and Prenylation, which intersect with Rab.
His study looks at the relationship between Biochemistry and topics such as Biophysics, which overlap with Enzyme catalysis. His GTP' research incorporates themes from Function and Protein–protein interaction. His Guanine nucleotide exchange factor study combines topics in areas such as Nucleotide, Guanine and Ternary complex.
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Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution : implications for the mechanism of GTP hydrolysis
Emil F. Pai;Ute Krengel;Gregory A. Petsko;Roger S. Goody.
The EMBO Journal (1990)
The Original Michaelis Constant: Translation of the 1913 Michaelis–Menten Paper
Kenneth A. Johnson;Roger S. Goody.
Time−resolved X−ray crystallographic study of the conformational change in Ha−ras p21 protein on GTP hydrolysis
Ilme Schlichting;Steven C. Almo;Gert Rapp;Keith Wilson.
Kinetics of interaction of nucleotides with nucleotide-free H-ras p21.
Jacob John;Roland Sohmen;Juergen Feuerstein;Rosita Linke.
The Legionella Effector Protein DrrA AMPylates the Membrane Traffic Regulator Rab1b
Matthias P. Müller;Heide Peters;Julia Blümer;Wulf Blankenfeldt.
GTPase activity of Rab5 acts as a timer for endocytic membrane fusion
Vladimir Rybin;Oliver Ullrich;Mariantonietta Rubino;Kirill A. Alexandrov.
A toolkit and benchmark study for FRET-restrained high-precision structural modeling
Stanislav Kalinin;Thomas Peulen;Simon Sindbert;Paul J Rothwell.
Nature Methods (2012)
Expression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide‐binding site
Jane Tucker;Georg Sczakiel;Jürgen Feuerstein;Jacob John.
The EMBO Journal (1986)
The magnesium ion-dependent adenosine triphosphatase of myosin. Two-step processes of adenosine triphosphate association and adenosine diphosphate dissociation.
Clive R. Bagshaw;John F. Eccleston;Fritz Eckstein;Roger S. Goody.
Biochemical Journal (1974)
The kinetic mechanism of Ran--nucleotide exchange catalyzed by RCC1.
Christian Klebe;Heino Prinz;Alfred Wittinghofer;Roger S. Goody.
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