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1 in (a guanine nucleotide-exchange factor for Ran-GTPase).
2 guanine nucleotide exchange factor (GEF) for Ran GTPase.
3 s the mechanism of substrate displacement by Ran GTPase.
4 hat it was a CRM-1-dependent event driven by Ran GTPase.
5 RanGAP1 is the activating protein for the Ran GTPase.
6 y-dependent process, but may not involve the RAN GTPase.
7 o the guanine nucleotide exchange factor for Ran GTPase.
8 nsitive to the nucleotide-bound state of the Ran GTPase.
9 nd by a dominant-negative mutant form of the Ran GTPase.
10 lly interact with both the NES motif and the Ran GTPase.
11 o leptomycin B and nucleotide-bound state of Ran-GTPase.
12 tinal cyclophilin-related protein that binds Ran-GTPase.
15 us (EMCV) binds and inhibits the activity of Ran-GTPase, a key regulator of nucleocytoplasmic transpo
17 GTP.RBH complex stimulated GTP hydrolysis by Ran GTPase activating protein 1 both in vitro and in per
21 for distortion, encodes a truncated RanGAP (Ran GTPase activating protein), a key nuclear transport
22 r import were used together with cytoplasmic Ran GTPase-activating factors to demonstrate that import
23 DP, established by the spatial separation of Ran GTPase-activating protein (RanGAP) and the Ran guani
25 -purification strategy, we have identified a Ran GTPase-activating protein (RanGAP2) as an Rx-interac
26 (gsp1), and essential Ran regulatory factors Ran GTPase-activating protein (rna1), Ran guanine nucleo
27 Cdc25C (Chk1, Chk2, and H2AX), as well as on Ran GTPase-activating protein 1 conjugated to small ubiq
28 sentrin-2 could covalently modify RanGAP1, a Ran GTPase-activating protein critically involved in nuc
29 GDP enabled by the specific locations of the Ran GTPase-activating protein RanGAP and the nucleotide
30 sequestering of its accessory proteins, the Ran GTPase-activating protein RanGAP and the nucleotide
36 n vitro, this interaction can accelerate the Ran GTPase-activating protein-mediated hydrolysis of GTP
40 This trafficking was dependent on the high Ran GTPase activity resulting from oncogenic transformat
41 ng nuclear localization signals requires the Ran GTPase and a complex of proteins assembled at the nu
42 the nuclear/cytoplasmic concentration of the Ran GTPase and inhibits the nuclear localization of Ubc9
44 been defined by their ability to bind to the Ran GTPase and the presence of a common region of approx
46 ntrosome independent, operates downstream of Ran GTPase, and depends upon BRCA1/BARD1 E3 ubiquitin li
49 uclear protein import pathway, including the Ran-GTPase, and the dimeric import receptor, importin-al
53 to the nucleus of 10-20% of the cytoplasmic Ran GTPase-binding protein (RanBP1) indicating that RanB
59 rt through the NPC can be uncoupled from the Ran GTPase cycle and can occur without GTP hydrolysis.
60 karyopherin-alpha, karyopherin-beta1 and the Ran GTPase cycle are required for INM targeting, undersc
62 Here, we report the first evidence that the Ran GTPase cycle is required for nuclear pore complex (N
66 control of the Ras-related nuclear protein (Ran) GTPase cycle depends on the regulated activity of r
70 al. (2014) describe how microtubules and the RAN GTPase/importin-beta system collaborate to control t
72 L segment that makes subsequent contact with Ran GTPase in the nucleus, and Ran can displace 2A from
77 n guanine-nucleotide exchange factor for the Ran GTPase, is an approximately 45-kD nuclear protein th
79 d microtubule formation system that uses the Ran-GTPase nuclear transport machinery, but no targets o
85 ith an expression vector for OPN to identify RAN GTPase (RAN) as the most overexpressed gene, in addi
87 se (DDR) and the cell cycle depends on their Ran GTPase-regulated nuclear-cytoplasmic transport (NCT)
88 nbp2(-/-) share proteostatic deregulation of Ran GTPase, serotransferrin, and gamma-tubulin and suppr
89 uclear pore complex and interaction with the Ran-GTPase support also its role in nucleocytoplasmic tr
94 protein and RNA in eukaryotes depends on the Ran-GTPase system to regulate cargo-receptor interaction
95 rm1, a nuclear export receptor that binds to Ran GTPase, thereby inducing nuclear localization of NF-
96 s that interact with the GTP-charged form of Ran GTPase through a conserved Ran-binding domain (RBD).
97 se, Nek6, and also binds specifically to the Ran GTPase through both its catalytic and its RCC1-like
99 , we show that importin beta cooperates with Ran GTPase to promote ubiquitination and proteasomal deg
100 e mechanisms of Ran function, mutants of the Ran GTPase were characterized, several of which are capa
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