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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
12                          SYNGAP1, a synaptic Ras GTPase activating protein, and SHANK3, a synaptic sc
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
16 d Ras on the plasma membrane by means of the Ras GTPase-activating protein CAPRI.
17              Finally, we showed that Carabin Ras-GTPase-activating protein domain and calcineurin-int
18 completely rescued by expression of the GAP (RAS-GTPase activating protein) domain of neurofibromin.
19                               Elimination of Ras GTPase-activating protein enhanced E-CD4 but decreas
20  (AIP1), a recently identified member of the Ras GTPase-activating protein family, is highly expresse
21 DAB2 interactive protein) is a member of the RAS-GTPase-activating protein family.
22                  synGAP is a neuron-specific Ras GTPase-activating protein found in high concentratio
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
26                       Moreover, the synaptic Ras GTPase activating protein (GAP) SynGAP is selectivel
27 la mutation on the interaction of H-Ras with Ras GTPase activating protein (GAP), neurofibromin 1 (NF
28 Ras signalling pathway through its intrinsic Ras GTPase-activating protein (GAP) activity.
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
31 ut not GAPex-5DeltaGAP, a mutant lacking the Ras GTPase-activating protein (GAP) domain.
32                  One domain is homologous to Ras GTPase-activating protein (GAP) domains.
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
35                                          The Ras GTPase-activating protein (GAP) p120RasGAP inhibits
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
38 kDa by SDS-PAGE and associates with the p120 ras GTPase-activating protein (GAP).
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
42                       In addition to the two Ras GTPase activating proteins (GAPs; p120- and NF1-GAP)
43    GAP1(m) is a member of the GAP1 family of Ras GTPase-activating proteins (GAPs) [1].
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
46                                  SynGAP is a Ras-GTPase activating protein highly enriched at excitat
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
49                                      RasGAP (Ras GTPase-activating protein) is a negative regulator a
50       One insertion was in the gene encoding Ras GTPase-activating protein; its overexpression phenot
51 mutations in the NF1 gene, which encodes the RAS GTPase-activating protein neurofibromin.
52 ith PLCgamma, phosphatidylinositol 3-kinase, Ras GTPase-activating protein, or protein tyrosine phosp
53                                The mammalian Ras GTPase-activating protein (p120Ras-GAP) interacts wi
54             Here, we report a novel synaptic Ras-GTPase activating protein (p135 SynGAP) that is a ma
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
59                       Neurofibromin exhibits Ras GTPase activating protein (Ras-GAP) activity that is
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
63 s that contains a 216-amino acid domain with Ras-GTPase-activating protein (Ras-GAP) activity.
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
66       Yeast 2-hybrid analyses identified the Ras GTPase-activating protein Rasa1, a known regulator o
67  effect found in our previous studies of the Ras GTPase activating protein (RasGAP) and the elongatio
68                                              ras GTPase activating protein (rasGAP) is highly conserv
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
71                 The NF1-encoded protein is a Ras GTPase-activating protein (RasGAP) [2].
72                                NF1 encodes a Ras GTPase-activating protein (RasGAP) and its loss driv
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
76       Specifically, we show that loss of the Ras GTPase-activating protein (RasGAP) gene DAB2IP induc
77             We have previously reported that Ras GTPase-activating protein (RasGAP) is involved in a
78 otifs in the C terminus and does not bind to Ras GTPase-activating protein (RasGAP) upon phosphorylat
79                 p62(dok) associates with the Ras GTPase-activating protein (RasGAP), but only when p6
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
82                                Dok, a 62-kDa Ras GTPase-activating protein (rasGAP)-associated phosph
83                                     A 62-kDa Ras GTPase-activating protein (RasGAP)-associated protei
84  docking platform for the SH2 domains of the Ras GTPase-activating protein (RasGAP).
85 the process of Ras inactivation catalyzed by Ras GTPase-activating protein (RasGAP).
86 coded protein, neurofibromin, functions as a Ras-GTPase activating protein (RasGAP).
87                 However, it is unknown which Ras GTPase-activating proteins (RasGAPs) inactivate Ras
88                                              Ras GTPase-activating proteins (RasGAPs) inhibit signal
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
92                                    Here, 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
98       RASA1 (also known as p120 RasGAP) is a Ras GTPase-activating protein that functions as a regula
99                   SynGAP is a brain-specific ras GTPase-activating protein that is an abundant compon
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
104                                              Ras GTPase-activating protein was found to be a caspase
105           We discovered that DAB2IP, a novel Ras-GTPase-activating protein, was frequently epigenetic

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