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April 29, 1992Philosophical Transactions of the Royal Society B Biological Sciences

Studies on the structure and mechanism of H-ras p21

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RGRoger S. GoodyMax Planck Institute of Molecular PhysiologyEPE.F. PaiOntario Institute for Cancer ResearchISIlme SchlichtingMax Planck Institute for Medical Research

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Goody et al. (1992) studied this question.

synapsesocial.com/papers/6aa018c1bca7bdefa1b573achttps://doi.org/10.1098/rstb.1992.0037
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  1. 1Use of the Glu-Glu-Phe C-terminal epitope for rapid purification of the catalytic domain of normal and mutant ras GTPase-activating proteins1991 · 56 citations
  2. 2p21 with a phenylalanine 28—-leucine mutation reacts normally with the GTPase activating protein GAP but nevertheless has transforming properties.1991 · 106 citations
  3. 3Characterisation of the metal‐ion–GDP complex at the active sites of transforming and nontransforming p21 proteins by observation of the <sup>17</sup>O‐Mn superhyperfine coupling and by kinetic methods1987 · 73 citations
  4. 4Is there a rate-limiting step before GTP cleavage by H-ras p21?1991 · 84 citations
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