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1 hagy, demonstrating an unexpected role for a golgin.
2 olecular weight coiled-coil proteins, termed golgins.
5 dominantly prevented cleavage of endogenous golgin-160 after ligation of death receptors or inductio
7 ese findings not only reveal novel roles for golgin-160 and GMAP210 in conferring membrane motility b
11 some pro-apoptotic stimuli; thus cleavage of golgin-160 appears to play a role in apoptotic signaling
13 lized to the Golgi complex, where it cleaves golgin-160 at a unique site not susceptible to cleavage
15 P60 interacts preferentially with one of the golgin-160 caspase cleavage fragments (residues 140-311)
17 ptosis in cells expressing caspase-resistant golgin-160 could not be bypassed by expression of potent
25 ybrid assay to screen for interactors of the golgin-160 head and identified GCP60 (Golgi complex-asso
26 event regulated not only by cleavage of the golgin-160 head but also by the oxidation state of GCP60
27 resident protein, interacts weakly with the golgin-160 head domain but has a strong interaction with
40 d and integrated at Golgi membranes and that golgin-160 plays an important role in transduction of th
42 nterfering RNA (siRNA)-mediated reduction in golgin-160 protein resulted in an increase accumulation
43 information is present in the same region of golgin-160 suggests that this protein may have more than
46 itive; in its reduced form, interaction with golgin-160 was diminished or abolished, whereas oxidatio
47 ing to the plasma membrane in the absence of golgin-160 was independent of TGN/Golgi sorting, because
48 lls expressing a caspase-resistant mutant of golgin-160 were strikingly resistant to apoptosis induce
50 identify the Golgi targeting information in golgin-160, full-length and deletion constructs tagged w
51 lso discovered a widely expressed isoform of golgin-160, golgin-160B, which lacks the exon encoding t
52 n of potential caspase cleavage fragments of golgin-160, or by drug-induced disassembly of the Golgi
53 ndings suggest that nuclear translocation of golgin-160-(140-311) is a highly coordinated event regul
63 gin-230/245/256, golgin-97, GM130/golgin-95, golgin-160/MEA-2/GCP170, giantin/macrogolgin and a relat
66 ed a widely expressed isoform of golgin-160, golgin-160B, which lacks the exon encoding the leucine r
69 een ARL1 and two binding proteins, SCOCO and Golgin-245, are defined and characterized in more detail
72 al. report the discovery of a protein named Golgin-45 that is located on the surface of the middle (
75 t showed that the N-terminal 497 residues of golgin-84 contain a coiled-coil domain that when fused t
83 ng cryoelectron microscopy we could localize golgin-84 to the cis-Golgi network and found that it is
84 II, GOS-28, GS15, GPP130, CASP, giantin, and golgin-84) whose abundances were reduced in the mutant c
87 ncludes golgin-230/245/256, golgin-97, GM130/golgin-95, golgin-160/MEA-2/GCP170, giantin/macrogolgin
91 discuss the potential role and functions of golgin-97 in poxvirus replication and propose two workin
93 Thus, we propose that FIP1/RCP binding to Golgin-97 is required for tethering and fusion of recycl
94 ing of FIP1/RCP to Golgin-97 does not affect Golgin-97 recruitment to the TGN, but appears to regulat
95 lular localization of the trans-Golgi marker Golgin-97 suggested differences in the organization of t
98 gi complex with specific markers, anti-human Golgin-97, anti-KDEL receptor, and BODIPY-TR ceramide, s
99 This family includes golgin-230/245/256, golgin-97, GM130/golgin-95, golgin-160/MEA-2/GCP170, gia
100 esiding in the trans-Golgi network membrane, golgin-97, is transported to the sites of virus replicat
104 e the distance between the distal end of the golgin and the target membrane thereby promoting tighter
109 malian cells more emphasis has been given to golgins as a potentially stable assembly framework.
111 115 lacking its phosphorylation site and the golgin-binding domains also restored the Golgi apparatus
114 hout in HeLa cells, we found that scattered, golgin-enriched, structures formed early and contained g
116 mall GTPases and coiled-coil proteins of the golgin family help to tether COPI vesicles to Golgi memb
117 x proteins--the best characterized being the golgin family of fibrous, coiled-coil proteins and the G
121 We show here that GCC185, a member of the Golgin family of putative tethering proteins, is a Rab9
123 We have found that these VCs use different golgins for docking: C2GnT-M-carrying VC (C2GnT-M-VC) ut
124 cidic COOH-terminal domain of p115 links the Golgins, Giantin on COPI vesicles, to GM130 on Golgi mem
127 In this study, we show that depletion of the golgin GMAP-210 causes a loss of Golgi cisternae and acc
128 racterized genes by identifying ten putative golgins/Golgi-associated proteins amongst 8219 genes of
129 Apart from giantin and GM130, none of the golgins has yet been assigned a function in the Golgi ap
132 1p, which was accompanied by accumulation of golgin Imh1p at late Golgi, but whether and how this fun
135 iched, structures formed early and contained golgins including giantin, ranging across the entire cis
137 nce microscopy were employed to identify the golgins involved in the Golgi docking of vesicular compl
138 urs in the absence of GRASP65/55 when either Golgin is overexpressed, as judged by quantitative elect
145 proteins 55 and 65 (GRASP55 and GRASP65) and Golgin of 45 kDa and Golgi matrix protein of 130 kDa.
146 with long coiled-coil domains, like lamins, golgins, or microtubule organization center components,
149 ng mitosis, we found that the formation of a golgin-positive acceptor compartment in early telophase
155 with deletions in other putative retrograde Golgins (sgm1Delta and rud3Delta) caused strong glycosyl
156 ser predicted protein-coding genes, GOLGA8E (golgin subfamily a, 8E) and WHDC1L1 (WAS protein homolog
160 ingly different from those bound by the p115-golgin tether in that they lacked members of the p24 fam
164 r to obtain clues as to the functions of the golgins, the targeting to the Golgi apparatus of two mem
166 s have shown, however, that mice lacking the golgin TRIP11/GMAP-210 have normal Golgi stacks, but sho
167 n this study, we report that the GRIP domain golgins, whose C termini bind the Arf-like 1 G protein o
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