The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding.

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Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules.

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Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm.

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Elucidation of binding determinants and functional consequences of Ras/Raf-cysteine-rich domain interactions.

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Molecular role for the Rab binding platform of guanine nucleotide dissociation inhibitor in endoplasmic reticulum to Golgi transport.

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PA112414

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The kinetic mechanism of the GAP-activated GTPase of p21 ras.

Citations & References

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  • Journal: Philos Trans R Soc Lond B Biol Sci (1992) 336:49-53; discussion 53-4
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Lot # 1683714

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The role of Mg2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins.

Citations & References

  • Authors: Zhang B, Zhang Y, Wang Z, Zheng Y
  • Journal: J Biol Chem (2000) 275:25299-25307
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Transient kinetic studies on the interaction of Ras and the Ras-binding domain of c-Raf-1 reveal rapid equilibration of the complex.

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  • Journal: Biochemistry (1998) 37:14292-14299
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