Literature DB >> 2122258

The GTPase superfamily: a conserved switch for diverse cell functions.

H R Bourne1, D A Sanders, F McCormick.   

Abstract

Proteins that bind and hydrolyse GTP are being discovered at a rapidly increasing rate. Each of these many GTPases acts as a molecular switch whose 'on' and 'off' states are triggered by binding and hydrolysis of GTP. Conserved structure and mechanism in myriad versions of the switch--in bacteria, yeast, flies and vertebrates--suggest that all derive from a single primordial protein, repeatedly modified in the course of evolution to perform a dazzling variety of functions.

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Year:  1990        PMID: 2122258     DOI: 10.1038/348125a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  615 in total

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Authors:  I P Whitehead; Q T Lambert; J A Glaven; K Abe; K L Rossman; G M Mahon; J M Trzaskos; R Kay; S L Campbell; C J Der
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Journal:  Mol Cell Biol       Date:  2001-04       Impact factor: 4.272

5.  Galpha(14) links a variety of G(i)- and G(s)-coupled receptors to the stimulation of phospholipase C.

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Authors:  R H Cool; G Schmidt; C U Lenzen; H Prinz; D Vogt; A Wittinghofer
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8.  Rem2, a new member of the Rem/Rad/Gem/Kir family of Ras-related GTPases.

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Journal:  Biochem J       Date:  2000-04-01       Impact factor: 3.857

9.  Involvement of a small GTP-binding protein (G protein) regulator, small G protein GDP dissociation stimulator, in antiapoptotic cell survival signaling.

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Journal:  Mol Biol Cell       Date:  2000-05       Impact factor: 4.138

10.  Loss of Rhb1, a Rheb-related GTPase in fission yeast, causes growth arrest with a terminal phenotype similar to that caused by nitrogen starvation.

Authors:  K E Mach; K A Furge; C F Albright
Journal:  Genetics       Date:  2000-06       Impact factor: 4.562

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