Guanosine triphosphatase stimulation of oncogenic Ras mutants (Q27618496)

1

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T Zor

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D Vogt

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W Kabsch

4

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Z Selinger

5

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A Wittinghofer

6

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K Scheffzek

Proceedings of the National Academy of Sciences of the United States of America

7

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language of work or name

English

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publication date

8 June 1999

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published in

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volume

96

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issue

12

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page(s)

7065-70

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cites work

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A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants

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Three-dimensional structures of H-ras p21 mutants: molecular basis for their inability to function as signal switch molecules

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Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis

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Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteins.

2 June 2018

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Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

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Crystallization and preliminary X-ray analysis of the human c-H-ras-oncogene product p21 complexed with GTP analogues

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Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis

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GTP analogue hydrolysis by the Gs protein: implication for the role of catalytic glutamine in the GTPase reaction

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12 December 2020

Kinetics of interaction of nucleotides with nucleotide-free H-ras p21

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12 December 2020

Substrate and Product Structural Requirements for Binding of Nucleotides to H-ras p21: The Mechanism of Discrimination between Guanosine and Adenosine Nucleotides

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12 December 2020

Formation of a Transition-State Analog of the Ras GTPase Reaction by Ras GDP, Tetrafluoroaluminate, and GTPase-Activating Proteins

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12 December 2020

Rescue of a mutant G-protein by substrate-assisted catalysis

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12 December 2020