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  The interaction of Ras with GTPase-activating proteins

Wittinghofer, A., Scheffzek, K., & Ahmadian, M. R. (1997). The interaction of Ras with GTPase-activating proteins. FEBS Letters, 410(1), 63-67. doi:10.1016/S0014-5793(97)00321-9.

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Genre: Journal Article
Alternative Title : The interaction of Ras with GTPase-activating proteins

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FEBSLett_410_1997_63.pdf (Any fulltext), 612KB
 
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 Creators:
Wittinghofer, Alfred1, Author           
Scheffzek, Klaus1, Author           
Ahmadian, Mohammad Reza, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: Ras; Ras-GTPase-activating protein; GTPase; Transition state; signal transduction; cell growth; guanosine triphosphatase; ras protein; guanosine triphosphatase activating protein
 Abstract: Ras plays a major role as a molecular switch in many signal transduction pathways which lead to cell growth and differentiation. The GTPase reaction of Ras is of central importance in the function of the switch since it terminates Ras-effector interactions. GTPase-activating proteins (GAPs) accelerate the very slow intrinsic hydrolysis reaction of the GTP-bound Ras by several orders of magnitude and thereby act as presumably negative regulators of Ras action. The GTP hydrolysis of oncogenic mutants of Ras remains unaltered. In this review we discuss recent biochemical and structural findings relating to the mechanism of GAP action, which strengthen the hypothesis that GAP accelerates the actual cleavage step by stabilizing the transition state of the phosphoryl transfer reaction

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Language(s): eng - English
 Dates: 1997-03-1119971997-06-23
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 410 (1) Sequence Number: - Start / End Page: 63 - 67 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501