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Subject cui: C0018296 Name: Guanosine Triphosphate Phosphohydrolases Sem. type: aapp Novel: true

Predicate: STIMULATES

Object cui: C1366537|998 Name: CDC42|CDC42 gene Sem. type: gngm|gngm Novel: true

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Guanosine Triphosphate Phosphohydrolases STIMULATES CDC42|CDC42 gene Correct? #Y/N
In fibroblasts, TrioD1 triggers the formation of particular cell structures, similar to those elicited by RhoG, a GTPase known to activate both Rac1 and Cdc42Hs . (PMID: 10652265) 0/0
RhoG is a member of the Rho family of GTPases that activates Rac1 and Cdc42 through a microtubule-dependent pathway. (PMID: 11689693) 0/0
Employing biochemical activity assays for Rho-like GTPases we found that hPEM-2 specifically activates Cdc42 and not Rac or RhoA. (PMID: 10559246) 0/0
RhoG GTPase controls a pathway that independently activates Rac1 and Cdc42Hs . (PMID: 9614181) 0/0
Activated mutants of each GTPase increased susceptibility to apoptosis, and activation of Cdc42 increased within 5 min of Fas stimulation. (PMID: 10734125) 0/0
Activation of Cdc42, a member of the Rho family of monomeric GTPases, is an essential signal regulating reannealing of AJs and reversal of the increase in endothelial permeability. (PMID: 17574122) 0/0
GTPases of the Rho subfamily are required for Brucella abortus internalization in nonprofessional phagocytes: direct activation of Cdc42 . (PMID: 11579087) 0/0
The specific GTPase-activating protein for Cdc42Hs, the Cdc42Hs-GAP, strongly stimulates the rate of reversal of the fluorescence enhancement at 545 nm, consistent with its ability to fully catalyze the GTPase reaction of Cdc42Hs. (PMID: 8605211) 0/0
We conclude that IpaC leads to activation of Cdc42 which in turn, causes activation of Rac, both GTPases being required for Shigella entry. (PMID: 10369666) 0/0
Activation of the small GTPases Rac1 and Cdc42, shown by immunoprecipitation, as well as inhibition of tyrosine kinases, GTPases, or Rac1 provided further support for the role of the FcgammaII-R. (PMID: 18390832) 0/0
In contrast to Rac, Cdc42 activation was independent of phospholipase C activation, indicating that the two GTPases are differently regulated. (PMID: 11696351) 0/0