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1 f the neurofibromatosis type 1 (NF1) gene, a Ras GTPase activating protein.
2 th high levels of RAS-GTP had loss of NF1, a RAS GTPase activating protein.
3  directed against either pp60(src), RhoA, or Ras GTPase-activating protein.
4 n the NF1 gene that encodes neurofibromin, a RAS GTPase-activating protein.
5        The DAB2IP tumor suppressor encodes a RAS GTPase-activating protein.
6 the NF1 gene, which encodes neurofibromin, a RAS GTPase-activating protein.
7 hoprotein reported to bind the SH3 domain of Ras GTPase-activating protein.
8  that binds to the pleckstrin domain of p120 Ras GTPase-activating protein.
9 ppressor postulated to function in part as a Ras GTPase-activating protein.
10 nositol 3'-kinase, phospholipase Cgamma, and Ras-GTPase activating protein.
11 ed CAPRI and RASAL as related Ca2+-triggered Ras GTPase-activating proteins.
12                   We identified the synaptic Ras GTPase activating protein 1 (Syngap1), encoded by a
13 otein (CREB) phosphorylation via RASA1 (p120 Ras GTPase-activating protein 1) down-regulation, wherea
14 rat homolog, but not its mutant defective in Ras GTPase activating protein activity, reverses miR-431
15 al known properties and functions, including Ras GTPase-activating protein activity, adenylyl cyclase
16                          SYNGAP1, a synaptic Ras GTPase activating protein, and SHANK3, a synaptic sc
17  gene product, neurofibromin, functions as a Ras GTPase-activating protein, and has been proposed to
18 F receptors including phospholipase C gamma, Ras GTPase-activating protein, and phosphotyrosine phosp
19    The NF1 gene encodes for neurofibromin, a RAS GTPase-activating protein, and thus negatively regul
20 HB4 (ephrin receptor B4) and the RASA1 (p120 Ras GTPase-activating protein) are necessary for the dev
21 rategy and demonstrate its implementation on Ras GTPase-activating protein-binding protein 1 (G3BP1)
22    Stress granule (SG) formation mediated by Ras GTPase-activating protein-binding protein 1 (G3BP1)
23 ss granules are formed through the switch of Ras GTPase-activating protein-binding protein 1 (G3BP1)
24 s were enriched, including the SG-nucleating Ras GTPase-activating protein-binding protein 1 (G3BP1).
25                                          The Ras GTPase-activating protein-binding protein G3BP1 is a
26                                              Ras GTPase-activating protein-binding proteins 1 and 2 (
27 d Ras on the plasma membrane by means of the Ras GTPase-activating protein CAPRI.
28              Finally, we showed that Carabin Ras-GTPase-activating protein domain and calcineurin-int
29 completely rescued by expression of the GAP (RAS-GTPase activating protein) domain of neurofibromin.
30                               Elimination of Ras GTPase-activating protein enhanced E-CD4 but decreas
31  (AIP1), a recently identified member of the Ras GTPase-activating protein family, is highly expresse
32 DAB2 interactive protein) is a member of the RAS-GTPase-activating protein family.
33                  synGAP is a neuron-specific Ras GTPase-activating protein found in high concentratio
34 emonstrates that the loss of DAB2IP, a novel Ras-GTPase activating protein frequently found in many c
35  calcium-promoted Ras inactivator (CAPRI), a Ras GTPase-activating protein, functions as an adaptor f
36 sential for signaling and contains a R-Ras/M-Ras GTPase activating protein (GAP) domain that is divid
37                       Moreover, the synaptic Ras GTPase activating protein (GAP) SynGAP is selectivel
38 la mutation on the interaction of H-Ras with Ras GTPase activating protein (GAP), neurofibromin 1 (NF
39 Ras signalling pathway through its intrinsic Ras GTPase-activating protein (GAP) activity.
40   The NF1-encoded protein neurofibromin is a Ras GTPase-activating protein (GAP) and can directly lim
41 t their effects via an intracellular R-Ras/M-Ras GTPase-activating protein (GAP) domain or by activat
42 ut not GAPex-5DeltaGAP, a mutant lacking the Ras GTPase-activating protein (GAP) domain.
43                  One domain is homologous to Ras GTPase-activating protein (GAP) domains.
44 DAB2 interacting protein) is a member of the Ras GTPase-activating protein (GAP) family that has been
45 at Ras, through an effector-like function of Ras GTPase-activating protein (GAP) in neonatal cardiac
46                                          The Ras GTPase-activating protein (GAP) p120RasGAP inhibits
47                                  RASAL2 is a RAS GTPase-activating protein (GAP) that has been associ
48 romoted Ras inactivator), a Ca(2+)-dependent Ras GTPase-activating protein (GAP) that switches off th
49  To distinguish between inhibition of Ras by Ras GTPase-activating protein (GAP) versus a potential e
50                         SynGAP is a synaptic Ras GTPase-activating protein (GAP) with four C-terminal
51 kDa by SDS-PAGE and associates with the p120 ras GTPase-activating protein (GAP).
52 ere we report that sphingosine can stimulate Ras-GTPase activating protein (GAP) activity in vitro, a
53 coded protein, neurofibromin, functions as a Ras-GTPase activating protein (GAP), nothing is known ab
54 ity of, Bruton's tyrosine kinase (Btk) and a Ras GTPase-activating protein, Gap1m, in vitro and in vi
55                       In addition to the two Ras GTPase activating proteins (GAPs; p120- and NF1-GAP)
56    GAP1(m) is a member of the GAP1 family of Ras GTPase-activating proteins (GAPs) [1].
57 he tyrosine phosphorylation of two important Ras GTPase-activating proteins (GAPs), p120 Ras-GAP and
58 ced wild-type TC21 activity in vivo and that Ras GTPase-activating proteins (GAPs; p120-GAP and NF1-G
59                                  SynGAP is a Ras-GTPase activating protein highly enriched at excitat
60                                 SYNGAP1 is a Ras-GTPase-activating protein highly enriched at excitat
61 novel GTPase-activating protein containing a Ras GTPase-activating protein homology domain (N terminu
62 Ras-GRF mutant containing the PH domain from Ras-GTPase-activating protein in place of its own N-term
63                                      RasGAP (Ras GTPase-activating protein) is a negative regulator a
64       One insertion was in the gene encoding Ras GTPase-activating protein; its overexpression phenot
65 in signaling and prevent inactivation by the RAS GTPase-activating protein neurofibromin 1.
66 mutations in the NF1 gene, which encodes the RAS GTPase-activating protein neurofibromin.
67 ith PLCgamma, phosphatidylinositol 3-kinase, Ras GTPase-activating protein, or protein tyrosine phosp
68                                The mammalian Ras GTPase-activating protein (p120Ras-GAP) interacts wi
69             Here, we report a novel synaptic Ras-GTPase activating protein (p135 SynGAP) that is a ma
70 -back' mutants in which association with the Ras GTPase-activating protein, phosphatidylinositol 3-ki
71 992 receptors were associated with more SOS, Ras-GTPase activating protein, phosphatidylinositol 3-ki
72 n as DAB2IP), a novel member of the Ras-GAP (Ras-GTPase-activating protein) protein family, opens its
73 ells while the phosphorylation/activation of Ras GTPase activating protein (Ras GAP) and mitogen acti
74                       Neurofibromin exhibits Ras GTPase activating protein (Ras-GAP) activity that is
75  In the present study, we identified a novel Ras GTPase-activating protein (Ras-GAP) as an ASK1-inter
76                                  Loss of the RAS GTPase-activating protein (RAS-GAP) NF1 drives aberr
77 l abolished the association of PDGFalphar to Ras GTPase-activating protein (Ras-GAP), but it did not
78 ongly reduced by silencing expression of the Ras-GTPase activating protein (Ras-GAP) neurofibromin, a
79 s that contains a 216-amino acid domain with Ras-GTPase-activating protein (Ras-GAP) activity.
80  we demonstrate that RASAL2, which encodes a RAS-GTPase-activating protein (RAS-GAP), is a functional
81 an include functional alteration of GTPases, Ras GTPase-activating proteins, Ras guanine exchange fac
82       Yeast 2-hybrid analyses identified the Ras GTPase-activating protein Rasa1, a known regulator o
83 g of LFA-1 to ICAM-1, including the Rap1 and Ras GTPase-activating protein RASA3.
84  effect found in our previous studies of the Ras GTPase activating protein (RasGAP) and the elongatio
85                                              ras GTPase activating protein (rasGAP) is highly conserv
86 n (G125V) in the scat Rasa3 gene, encoding a Ras GTPase activating protein (RasGAP), and elucidate th
87 One key regulator of this cascade is the Nf1 Ras GTPase activating protein (RasGAP), which attenuates
88                 The NF1-encoded protein is a Ras GTPase-activating protein (RasGAP) [2].
89                                NF1 encodes a Ras GTPase-activating protein (RasGAP) and its loss driv
90 acted with the SH3 domain and phosphorylated Ras GTPase-activating protein (RasGAP) and upregulated R
91 aptor Grb2-associated binder-1 (GAB1) on its RAS GTPase-activating protein (RASGAP) binding sites and
92 orylation of Dok-1, augmented recruitment of Ras GTPase-activating protein (RasGAP) by Dok-1, and inh
93 AP1 as a human protein related to a putative Ras GTPase-activating protein (RasGAP) from the fission
94       Specifically, we show that loss of the Ras GTPase-activating protein (RasGAP) gene DAB2IP induc
95             We have previously reported that Ras GTPase-activating protein (RasGAP) is involved in a
96          These screens converged on RASA2, a RAS GTPase-activating protein (RasGAP) that we identify
97  of activated Ras by blocking recruitment of Ras GTPase-activating protein (RasGAP) to the plasma mem
98 otifs in the C terminus and does not bind to Ras GTPase-activating protein (RasGAP) upon phosphorylat
99 y, including Nck adaptor protein (Nck), p120-Ras GTPase-activating protein (RasGAP), and the alpha- a
100                 p62(dok) associates with the Ras GTPase-activating protein (RasGAP), but only when p6
101 predicted, growth-related targets, including Ras GTPase-activating protein (RasGAP), cyclin-dependent
102 peptide derived from the N2 fragment of p120 Ras GTPase-activating protein (RasGAP), sensitizes tumor
103                                Dok, a 62-kDa Ras GTPase-activating protein (rasGAP)-associated phosph
104                                     A 62-kDa Ras GTPase-activating protein (RasGAP)-associated protei
105  docking platform for the SH2 domains of the Ras GTPase-activating protein (RasGAP).
106 the process of Ras inactivation catalyzed by Ras GTPase-activating protein (RasGAP).
107 coded protein, neurofibromin, functions as a Ras-GTPase activating protein (RasGAP).
108 precisely controlled by mechanisms involving Ras GTPase activating proteins (RasGAPs) responsible for
109                 However, it is unknown which Ras GTPase-activating proteins (RasGAPs) inactivate Ras
110                                              Ras GTPase-activating proteins (RasGAPs) inhibit signal
111    Rasal, belonging to the GAP1 subfamily of Ras GTPase-activating proteins (RasGAPs) with dual RasGA
112  Nf1, a tumor suppressor gene that encodes a Ras-GTPase-activating protein, results in hyperactivity
113     We further show that nsp1 interacts with Ras GTPase-activating protein SH3 domain-binding protein
114 tors (HERs), induced expression of G3BP, the Ras GTPase-activating protein SH3 domain-binding protein
115                                          The Ras-GTPase activating protein SH3 domain-binding protein
116                                    Here, the Ras-GTPase-activating protein SH3 domain-binding protein
117 resis and identified by mass spectrometry as Ras-GTPase-activating protein SH3 domain-binding protein
118 teins (p85 (phosphoinositide 3-kinase), Vav, Ras-GTPase-activating protein SH3 domain-binding protein
119 that members of the Ras network of proteins, Ras-GTPase activating protein-SH3-domain-binding protein
120   Here, we describe the isolation of a novel Ras-GTPase activating protein, SynGAP, that interacts wi
121                                          The Ras GTPase-activating protein SYNGAP1 plays a central ro
122 to citron, p135 SynGAP, an abundant synaptic Ras GTPase-activating protein that can bind to all three
123       RASA1 (also known as p120 RasGAP) is a Ras GTPase-activating protein that functions as a regula
124                   SynGAP is a brain-specific ras GTPase-activating protein that is an abundant compon
125 e we report the characterisation of RASAL, a Ras GTPase-activating protein that senses the frequency
126                                 SYNGAP1 is a Ras GTPase-activating protein that underlies the formati
127 ating protein (SynGAP) is a neuronal RasGAP (Ras GTPase-activating protein) that is selectively expre
128 as, suggesting that it may also compete with Ras GTPase-activating protein, thus contributing to the
129                                            A Ras GTPase activating protein tumor suppressor (RasGAP),
130 alyzed GTP hydrolysis in water, Ras, and Ras.Ras-GTPase-activating protein using quantum mechanics/mo
131                                              Ras GTPase-activating protein was found to be a caspase
132           We discovered that DAB2IP, a novel Ras-GTPase-activating protein, was frequently epigenetic
133 ing protein homologous to mammalian synaptic Ras GTPase-activating protein, which modify daf-7 expres

 
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