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1 tion by Y. pseudotuberculosis YopE, a potent Rho GTPase activating protein.
2 1, a kinesin-6 motor, and CYK-4/MgcRacGAP, a Rho GTPase-activating protein.
3 ssociation of intronic variants in ARHGAP15 (Rho GTPase-activating protein 15; rs4662344-T: P=1.9 x 1
4 that the cortical development gene Slit-Robo Rho GTPase-activating protein 2 (SRGAP2) duplicated thre
6 e 12 (MMP12)/MMP13, catenin alpha3 (CTNNA3), rho GTPase-activating protein 24 (ARHGAP24), angiopoieti
7 ll spreading through its interaction partner Rho GTPase-activating protein 29 (ArhGAP29), a GTPase ac
8 cating mutations in the terminal exon of the Rho GTPase-activating protein 31 gene, ARHGAP31, which e
10 circ_0003258 could elevate the expression of Rho GTPase activating protein 5 (ARHGAP5) via sponging m
14 on, migration, and proliferation through its Rho GTPase-activating protein activity and focal adhesio
16 f Pseudomonas aeruginosa that possesses both Rho GTPase-activating protein and ADP-ribosyltransferase
17 Deleted in Liver Cancer 1 (DLC1) encodes a Rho-GTPase activating protein and is a candidate 8p tumo
18 comprising the Cdc42-interactor IQGAP1, the Rho GTPase-activating protein ARHGAP10, and the integrin
19 3D spheroids of human cells, we identify the Rho GTPase activating protein ARHGAP18 as an effector of
20 emonstrated that selective expression of the Rho GTPase-activating protein ARHGAP42 in smooth muscle
21 (CaV2.2) were induced by TNF, whereas Vav2, Rho GTPase-activating protein, calcium channel voltage-d
22 hat through its domain structure, SRGAP2A, a Rho-GTPase-activating protein, can co-regulate excitator
25 duces formation of the AKT kinase (AKT)/DLC1 Rho-GTPase-activating protein (DLC1) complex and thereby
27 uronal diacylglycerol-binding protein with a Rho GTPase-activating protein domain that inactivates Ra
29 ion of the actin cytoskeleton independent of Rho GTPase-activating protein function, and ExoT was sub
32 ends on interactions with CYK-4/MgcRacGAP, a Rho GTPase-activating protein (GAP) domain containing pr
33 we show that, contrary to expectations, the Rho GTPase-activating protein (GAP) domain of CYK-4 prom
40 two-hybrid method, we identified a family of Rho GTPase-activating proteins (GAP) from Arabidopsis, t
43 otypically enriched Cadherin2 sequesters the Rho GTPase-activating protein, Gap21/23, to homotypic ju
47 ding proteins are subjected to regulation by Rho GTPase-activating proteins (GAPs) in the course of t
49 r with its binding partner ARHGAP35/P190A, a RHO GTPase-activating protein, in the radial glia-like n
53 with exception of the Crossveinless-c (Cv-c) Rho GTPase-activating protein, most effectors exert litt
55 d that the Rho GTPase and its regulator p190 Rho-GTPase-activating protein (p190 RhoGAP) also play an
56 anism involves p120 catenin interaction with Rho GTPase activating protein (p190RhoGAP), leading to p
59 t-Robo pathway component EVA-1/EVA1C and the Rho GTPase-activating protein RGA-9b/ARHGAP, which are r
62 (deleted in liver cancer 1), which encodes a Rho GTPase-activating protein (Rho-GAP), is a potent tum
63 AP3, a member of the Slit-Robo sub-family of Rho GTPase-activating proteins (Rho GAPs), controls acti
64 ends on its presence at focal adhesions, its Rho-GTPase activating protein (Rho-GAP) function, and it
67 neurons require Crossveinless-c, a specific Rho-GTPase-activating protein (Rho-Gap), to alter their
69 nine nucleotide exchange factor (RhoGEF) and Rho GTPase activating protein (RhoGAP) pair required for
70 in of Pseudomonas aeruginosa with N-terminal Rho GTPase-activating protein (RhoGAP) and C-terminal AD
72 9, and S567) in the DLC1 tumor suppressor, a Rho GTPase-activating protein (RhoGAP) associated with f
80 rmed cells, ERK5 induced the expression of a Rho GTPase-activating protein (RhoGAP), RhoGAP7/DLC-1, v
81 binding to Mg(2+), and k(cat) values of the Rho GTPase-activating protein (RhoGAP)-catalyzed reactio
82 cell, which might install platforms allowing Rho-GTPase-activating protein (RhoGAP) activity to be fo
87 eleted in liver cancer genes (DLC1-3) encode Rho-GTPase-activating proteins (RhoGAPs) whose expressio
88 e in vitro and in vivo, whereas mutations in rho-GTPase-activating protein showed the same phenotype
89 et genes, including Arhgap1, which encodes a RHO GTPase activating protein that was required for tumo
91 at target the tumor suppressor gene DLC-1 (a Rho GTPase-activating protein), which is frequently dele
92 e have demonstrated that MEKK1 binds to p115 Rho GTPase-activating protein, which has GTPase-activati