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Title: Fluorescence approaches to the study of the p21ras GTPase mechanism. Author: Eccleston JF, Moore KJ, Brownbridge GG, Webb MR, Lowe PN. Journal: Biochem Soc Trans; 1991 Apr; 19(2):432-7. PubMed ID: 1889625. Abstract: The use of ribose-modified guanine nucleotides and tryptophan mutants of p21ras, neither of which have significant effect on the kinetic mechanism of the p21ras GTPase and the GAP-activated p21ras GTPase, will now allow a detailed kinetic study of how GAP and other regulatory proteins interact with p21ras. This will lead to a better understanding of how the relative concentrations of 'active' p21ras. GTP and 'inactive' p21ras. GDP are regulated in the cell.[Abstract] [Full Text] [Related] [New Search]