(Q24300229)

GOA release 2020-03-11

GTPase activity

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Why does the Ras switch "break" by oncogenic mutations?

GOA release 2020-03-11

author

Jacqueline Cherfils

series ordinal

2

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Sebastiano Pasqualato

series ordinal

1

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language of work or name

English

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publication date

April 2005

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published in

Structure

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volume

13

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issue

4

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page(s)

533-40

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cites work

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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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GTPase-activating proteins: helping hands to complement an active site

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Structural and biochemical properties show ARL3-GDP as a distinct GTP binding protein

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The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins

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Structure of the GDP-Pi complex of Gly203-->Ala gialpha1: a mimic of the ternary product complex of galpha-catalyzed GTP hydrolysis

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Structural basis of activation and GTP hydrolysis in Rab proteins

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MgF(3)(-) as a transition state analog of phosphoryl transfer

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Understanding the rates of certain enzyme-catalyzed reactions: proton abstraction from carbon acids, acyl-transfer reactions, and displacement reactions of phosphodiesters

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GTP hydrolysis mechanisms in ras p21 and in the ras-GAP complex studied by fluorescence measurements on tryptophan mutants

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Ras catalyzes GTP hydrolysis by shifting negative charges from gamma- to beta-phosphate as revealed by time-resolved FTIR difference spectroscopy

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Role of glutamine-61 in the hydrolysis of GTP by p21H-ras: an experimental and theoretical study.

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The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants

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Small GTP-binding proteins

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