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1 th high levels of RAS-GTP had loss of NF1, a RAS GTPase activating protein.
2 f the neurofibromatosis type 1 (NF1) gene, a Ras GTPase activating protein.
3 the NF1 gene, which encodes neurofibromin, a RAS GTPase-activating protein.
4 hoprotein reported to bind the SH3 domain of Ras GTPase-activating protein.
5 that binds to the pleckstrin domain of p120 Ras GTPase-activating protein.
6 ppressor postulated to function in part as a Ras GTPase-activating protein.
7 directed against either pp60(src), RhoA, or Ras GTPase-activating protein.
8 nositol 3'-kinase, phospholipase Cgamma, and Ras-GTPase activating protein.
9 ed CAPRI and RASAL as related Ca2+-triggered Ras GTPase-activating proteins.
10 otein (CREB) phosphorylation via RASA1 (p120 Ras GTPase-activating protein 1) down-regulation, wherea
11 al known properties and functions, including Ras GTPase-activating protein activity, adenylyl cyclase
13 gene product, neurofibromin, functions as a Ras GTPase-activating protein, and has been proposed to
14 F receptors including phospholipase C gamma, Ras GTPase-activating protein, and phosphotyrosine phosp
15 The NF1 gene encodes for neurofibromin, a RAS GTPase-activating protein, and thus negatively regul
18 completely rescued by expression of the GAP (RAS-GTPase activating protein) domain of neurofibromin.
20 (AIP1), a recently identified member of the Ras GTPase-activating protein family, is highly expresse
23 emonstrates that the loss of DAB2IP, a novel Ras-GTPase activating protein frequently found in many c
24 calcium-promoted Ras inactivator (CAPRI), a Ras GTPase-activating protein, functions as an adaptor f
25 sential for signaling and contains a R-Ras/M-Ras GTPase activating protein (GAP) domain that is divid
27 la mutation on the interaction of H-Ras with Ras GTPase activating protein (GAP), neurofibromin 1 (NF
29 The NF1-encoded protein neurofibromin is a Ras GTPase-activating protein (GAP) and can directly lim
30 t their effects via an intracellular R-Ras/M-Ras GTPase-activating protein (GAP) domain or by activat
33 DAB2 interacting protein) is a member of the Ras GTPase-activating protein (GAP) family that has been
34 at Ras, through an effector-like function of Ras GTPase-activating protein (GAP) in neonatal cardiac
36 romoted Ras inactivator), a Ca(2+)-dependent Ras GTPase-activating protein (GAP) that switches off th
37 To distinguish between inhibition of Ras by Ras GTPase-activating protein (GAP) versus a potential e
39 ere we report that sphingosine can stimulate Ras-GTPase activating protein (GAP) activity in vitro, a
40 coded protein, neurofibromin, functions as a Ras-GTPase activating protein (GAP), nothing is known ab
41 ity of, Bruton's tyrosine kinase (Btk) and a Ras GTPase-activating protein, Gap1m, in vitro and in vi
44 he tyrosine phosphorylation of two important Ras GTPase-activating proteins (GAPs), p120 Ras-GAP and
45 ced wild-type TC21 activity in vivo and that Ras GTPase-activating proteins (GAPs; p120-GAP and NF1-G
47 novel GTPase-activating protein containing a Ras GTPase-activating protein homology domain (N terminu
48 Ras-GRF mutant containing the PH domain from Ras-GTPase-activating protein in place of its own N-term
52 ith PLCgamma, phosphatidylinositol 3-kinase, Ras GTPase-activating protein, or protein tyrosine phosp
55 -back' mutants in which association with the Ras GTPase-activating protein, phosphatidylinositol 3-ki
56 992 receptors were associated with more SOS, Ras-GTPase activating protein, phosphatidylinositol 3-ki
57 n as DAB2IP), a novel member of the Ras-GAP (Ras-GTPase-activating protein) protein family, opens its
58 ells while the phosphorylation/activation of Ras GTPase activating protein (Ras GAP) and mitogen acti
60 In the present study, we identified a novel Ras GTPase-activating protein (Ras-GAP) as an ASK1-inter
61 l abolished the association of PDGFalphar to Ras GTPase-activating protein (Ras-GAP), but it did not
62 ongly reduced by silencing expression of the Ras-GTPase activating protein (Ras-GAP) neurofibromin, a
64 we demonstrate that RASAL2, which encodes a RAS-GTPase-activating protein (RAS-GAP), is a functional
65 an include functional alteration of GTPases, Ras GTPase-activating proteins, Ras guanine exchange fac
67 effect found in our previous studies of the Ras GTPase activating protein (RasGAP) and the elongatio
69 n (G125V) in the scat Rasa3 gene, encoding a Ras GTPase activating protein (RasGAP), and elucidate th
70 One key regulator of this cascade is the Nf1 Ras GTPase activating protein (RasGAP), which attenuates
73 aptor Grb2-associated binder-1 (GAB1) on its RAS GTPase-activating protein (RASGAP) binding sites and
74 orylation of Dok-1, augmented recruitment of Ras GTPase-activating protein (RasGAP) by Dok-1, and inh
75 AP1 as a human protein related to a putative Ras GTPase-activating protein (RasGAP) from the fission
78 otifs in the C terminus and does not bind to Ras GTPase-activating protein (RasGAP) upon phosphorylat
80 predicted, growth-related targets, including Ras GTPase-activating protein (RasGAP), cyclin-dependent
81 peptide derived from the N2 fragment of p120 Ras GTPase-activating protein (RasGAP), sensitizes tumor
89 Rasal, belonging to the GAP1 subfamily of Ras GTPase-activating proteins (RasGAPs) with dual RasGA
90 Nf1, a tumor suppressor gene that encodes a Ras-GTPase-activating protein, results in hyperactivity
91 tors (HERs), induced expression of G3BP, the Ras GTPase-activating protein SH3 domain-binding protein
93 resis and identified by mass spectrometry as Ras-GTPase-activating protein SH3 domain-binding protein
94 teins (p85 (phosphoinositide 3-kinase), Vav, Ras-GTPase-activating protein SH3 domain-binding protein
95 that members of the Ras network of proteins, Ras-GTPase activating protein-SH3-domain-binding protein
96 Here, we describe the isolation of a novel Ras-GTPase activating protein, SynGAP, that interacts wi
97 to citron, p135 SynGAP, an abundant synaptic Ras GTPase-activating protein that can bind to all three
100 e we report the characterisation of RASAL, a Ras GTPase-activating protein that senses the frequency
101 ating protein (SynGAP) is a neuronal RasGAP (Ras GTPase-activating protein) that is selectively expre
102 as, suggesting that it may also compete with Ras GTPase-activating protein, thus contributing to the
103 alyzed GTP hydrolysis in water, Ras, and Ras.Ras-GTPase-activating protein using quantum mechanics/mo
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