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1 erivative that cleaves SNAP23, a nonneuronal SNARE protein.
2 is a unique intracellular location for this SNARE protein.
3 5 (STX5), a member of the syntaxin family of SNARE proteins.
4 me degradation by disrupting the function of SNARE proteins.
5 ed at the end of the transmembrane domain of SNARE proteins.
6 ction between alpha-synuclein and any of the SNARE proteins.
7 ugh interactions with the syntaxin family of SNARE proteins.
8 rocessive unwinding mechanism to disassemble SNARE proteins.
9 ins in membrane fusion by directly acting on SNARE proteins.
10 r evolutionarily conserved structures in the SNARE proteins.
11 ric Golgi (COG) complex and with intra-Golgi SNARE proteins.
12 to neurons and specific cleavage of neuronal SNARE proteins.
13 c binding to nerve terminals and cleavage of SNARE proteins.
14 uires homotypic membrane fusion catalyzed by SNARE proteins.
15 Ca(2+) and through direct interactions with SNARE proteins.
16 rms and requires membrane integration of the SNARE proteins.
17 (SNARE) complexes between vesicle and Golgi SNARE proteins.
18 transmission by endoproteolytic cleavage of SNARE proteins.
19 nd R-SNARE and plasma membrane Qa, Qb and Qc SNARE proteins.
20 calcium channel function by interaction with SNARE proteins.
21 c1/Munc18 (SM) proteins to specific syntaxin SNARE proteins.
22 rm motility, calcium channel regulation, and SNARE proteins.
23 nimal model for membrane fusion, inspired by SNARE proteins.
24 LegC7/YlfA] functionally mimic glutamine (Q)-SNARE proteins.
25 ensitive-factor attachment protein receptor (SNARE) proteins.
26 ensitive factor attachment protein receptor (SNARE) proteins.
27 fusion protein-attachment protein receptors (SNARE) proteins.
28 ensitive factor attachment protein receptor (SNARE) proteins.
29 YP73, a member of the plant Syp7 subgroup of SNARE proteins [9] containing actin-binding domains, is
30 rough the regulation of NMDAR exocytosis via SNARE proteins, a family of proteins involved in vesicle
31 ys can be used to study the roles of various SNARE proteins, accessory proteins and effects of differ
33 lexin clamps otherwise spontaneous fusion by SNARE proteins, allowing neurotransmitters and other med
34 coupled to associations between F-actin and SNARE proteins, although the nature and function of thes
38 egregate cargo from source compartments, and SNARE proteins and associated factors that cause vesicle
40 an ENTH domain-containing protein that binds SNARE proteins and functions in vesicle trafficking; how
42 dylinositol 4,5-bisphosphate (PI(4,5)P2) and SNARE proteins and is proposed to promote SNARE protein
43 he internal distribution of fusion-competent SNARE proteins and limiting homotypic fusions among cont
44 n which direct interactions between specific SNARE proteins and PIP aquaporins modulate their post-Go
45 T to the surface by a mechanism dependent on SNARE proteins and protein kinase C-beta but independent
46 s containing elevated levels of the ER-Golgi SNARE proteins and Sly1p were less sensitive to PI(4)P i
49 ific for UNC-64 Syntaxin-1, because 14 other SNARE proteins and two active zone markers were unaffect
53 icking requires membrane fusion, mediated by SNARE proteins, and upstream events that probably includ
55 ing scorpion envenomation as both of these v-SNARE proteins are associated with zymogen granule membr
58 In eukaryotic cells, multiple isoforms of SNARE proteins are expressed and are involved in distinc
62 ensitive factor attachment protein receptor (SNARE) proteins are key players in cellular trafficking
63 ensitive factor activating protein receptor (SNARE) proteins are the main catalysts for membrane fusi
64 core membrane fusion machinery proteins, the SNARE proteins, are assisted by a group of regulatory fa
67 Vesicle fusion is mediated by an assembly of SNARE proteins between opposing membranes, but it is unk
69 ctome in mouse brain, we identified not only SNARE proteins but also Munc-18-1 (stabilizes assembled
70 Complexins are unable to bind to monomeric SNARE proteins but bind with high affinity to ternary SN
71 Exocytosis depends on cytosolic domains of SNARE proteins but the function of the transmembrane dom
72 tosomal-associated protein of 25 kDa), a key SNARE protein, by immunocytochemistry with cell type-spe
73 Our study supports the idea that endosomal SNARE proteins can have functions unrelated to membrane
75 ensitive factor attachment protein receptor (SNARE) proteins catalyze membrane fusion events in the s
76 siologically, alpha-synuclein functions as a SNARE-protein chaperone that promotes SNARE-complex asse
77 y governed through light chain (LC) protease SNARE protein cleavage leading to a loss of neurotransmi
78 nd SNARE proteins and is proposed to promote SNARE protein complex assembly for vesicle docking and p
85 icking by mediating disassembly and reuse of SNARE protein complexes, which facilitate fusion of vesi
86 ensitive factor attachment protein receptor (SNARE) protein complexes play essential roles in catalyz
88 ve factor (NSF) attachment protein receptor (SNARE) proteins comprise the minimal machinery that trig
89 ensitive factor attachment protein receptor (SNARE) proteins constitute the minimal machinery that ca
93 ensitive factor attachment protein receptor (SNARE) proteins drive membrane fusion by assembling into
94 eimide-sensitive factor attachment receptor (SNARE) proteins drive the fusion of synaptic vesicles to
96 ensitive factor attachment protein receptor (SNARE) proteins during vesicle formation, and SNARE-medi
97 tion of a highly stable four-helix bundle of SNARE proteins embedded in the vesicle and target membra
98 eins with similar domains of plasma membrane SNARE proteins enhancing fusion of the two membranes to
99 ing microscopy between fluorescently labeled SNARE proteins expressed in cultured rat hippocampal neu
100 fusion involves the action of members of the SNARE protein family as well as Sec1/Munc18 (SM) protein
101 ntaxin-11 (Stx11), an atypical member of the SNARE protein family, is part of the cytolytic machinery
106 yntaxin17, thereby preventing these two host SNARE proteins from mediating autophagosome-lysome fusio
112 xin-8 mutant that cannot assemble with other SNARE proteins had virtually the same effect as wild-typ
115 by soluble NSF attachment protein receptor (SNARE) proteins have been difficult to establish because
116 Here, we show that syntaxin 8 (MoSyn8), a Qc-SNARE protein homolog, also plays important roles in gro
117 ic granule exocytosis, the role of vesicular SNARE proteins, i.e., vesicle-associated membrane protei
119 Syntaxin 3 and 4 are apical and basolateral SNARE proteins important for the specificity of vesicle
120 Our results identify Gos28 as an essential SNARE protein in Drosophila photoreceptors and provide m
123 tudy of MoSyn8 advances our understanding of SNARE proteins in effector secretion which underlies the
124 een implicated in regulating the function of SNARE proteins in exocytosis, but their precise mode of
125 ngs demonstrate for the first time a role of SNARE proteins in HIV-1 assembly and release, likely by
129 interaction of positively charged regions in SNARE proteins in synaptic or secretory vesicle membrane
130 bilayers with positively charged regions in SNARE proteins in the plasma membrane lipid bilayer to f
132 osed for the transmembrane regions (TMRs) of SNARE proteins, including formation of channel-like tran
133 olemma, as the response was prevented by the SNARE protein inhibitor N-ethylmaleimide and the calcium
134 rescence microscopy, cell fractionation, and SNARE protein interaction studies that acinar cells cont
136 thylmaleimide attachment protein receptor (t-SNARE) protein, interferes with VEGFR2 trafficking to th
139 eimide-sensitive factor attachment receptor (SNARE) proteins into a parallel four-helix bundle to dri
140 42 targeted the GHRH receptor and depleted a SNARE protein involved in GH exocytosis, vesicle-associa
141 Thus, the fusogenic F protein resembles SNARE proteins involved in vesicle fusion by having wate
142 mammalian horizontal cells along with other SNARE proteins is consistent with vesicular exocytosis.
144 al-associated protein of 25 kDa (SNAP-25), a SNARE protein, is functionally relevant to PKC-dependent
145 binding is specific for a subset of exocytic SNARE protein isoforms and requires membrane integration
146 s exocytotic processes mediated by different SNARE protein isoforms, we systematically analyzed the i
149 ed of exocytosis, but total vesicle numbers, SNARE protein levels, and postsynaptic densities remaine
152 endent on the formation of complexes between SNARE proteins located at the target membrane and on tra
153 thesize that taste cell synapses utilize the SNARE protein machinery syntaxin, SNAP-25, and synaptobr
154 ow that lipid-anchored STX11 and its cognate SNARE proteins mainly support exchange of lipids but not
159 in 1/SNAP-25 as the ubiquitous and essential SNARE proteins mediating multiple fusion events on neuro
161 resynaptic compartments, but does not cleave SNARE proteins nor impair spontaneous neurotransmitter r
162 hat otoferlin interacts with two main target-SNARE proteins of the hair-cell synaptic complex, syntax
165 sential processes require the interaction of SNARE proteins on vesicle and cell membranes, as well as
166 erlin and synaptotagmin bind membrane fusion SNARE proteins, only otoferlin interacts with the L-type
167 r vesicle-associated membrane protein type v-SNARE proteins (or synaptobrevins) reveals characteristi
168 ng is driven by the assembly of heterologous SNARE proteins orchestrated by the binding of Sec1/Munc1
172 ensitive factor attachment protein receptor (SNARE) proteins play a major role in membrane fusion and
175 um-sensitive scaffolding protein, localizing SNARE proteins proximal to the calcium channel so as to
176 pends on endosomal fusion events mediated by SNARE proteins, Rab-GTPases, and multisubunit tethering
182 livery of large stoichiometric quantities of SNARE proteins required for forming the partitioning mem
183 n at least three respects: 1) The density of SNARE proteins required for fusion in vitro is substanti
184 re highly potent toxins that cleave neuronal SNARE proteins required for neurotransmission, causing f
186 supernatants, indicating that extracellular SNARE proteins retain their ability to bind one another.
187 ensitive factor attachment protein receptor (SNARE) proteins, Sec17p, Sec18p, the Rab Ypt7p, and the
189 Here we monitored interactions of the R-SNARE protein Sec22 through a cysteine scanning approach
190 fection there is noncanonical pairing of the SNARE protein Sec22b on ER-derived vesicles with plasma
191 unit Sec6 directly bound the plasma membrane SNARE protein Sec9 in vitro and that Sec6 inhibited the
194 nown whether transmembrane domains (TMDs) of SNARE proteins serve mechanistic functions that go beyon
195 studies have indicated that the gene for the SNARE protein SNAP-25 is a candidate susceptibility gene
196 is by enzymatically cleaving the presynaptic SNARE protein SNAP-25, which results in lasting inhibiti
198 age-dependent redistribution of the synaptic SNARE proteins SNAP-25, syntaxin-1 and synaptobrevin-2,
202 ensitive factor attachment protein receptor (SNARE) proteins soluble N-ethylmaleimide-sensitive facto
203 dding (COPII) detected by the packaging of a SNARE protein (soluble N-ethylmaleimide-sensitive attach
205 ect is mediated by the binding of Mig-6 to a SNARE protein STX8, a protein known to be required for l
206 c domain (BoNT E) in complex with SNAP-25 (a SNARE protein) substrate peptide Arg(180)-Ile(181)-Met(1
208 The previously reported interactions with SNARE proteins suggested the involvement of septins in e
209 py (EM) studies indicated that the vesicular SNARE protein synaptobrevin (syb) was dispensable for do
213 Neurotransmitter release is mediated by the SNARE proteins synaptobrevin II (sybII, also known as VA
214 e factor attachment protein (SNAP) receptor (SNARE) proteins synaptobrevin 2, syntaxin-1A, and SNAP-2
215 Moreover, a juxtamembranous mutation in the SNARE-protein synaptobrevin-2, which presumably impairs
216 cally, alpha-synuclein directly bound to the SNARE-protein synaptobrevin-2/vesicle-associated membran
217 sm by alpha-latrotoxin requires the synaptic SNARE-proteins synaptobrevin/VAMP and SNAP-25, and, at l
218 ors; and the exocytosis machinery, including SNARE proteins (synaptobrevin, SNAP25, and syntaxin), is
220 eading candidate for such a regulator is the SNARE protein syntaxin 1A (Syn1A), previously found to i
222 n secretory dysfunction, we identified the t-SNARE protein Syntaxin 4 as a target of modification by
224 eptor (SNARE)-mediated process, and that the SNARE protein syntaxin binds directly to Kv2.1 channels.
225 smitter release and requires that the target-SNARE protein syntaxin-1 switches from a closed to an op
229 Y1 is known to interact with the ER-specific SNARE proteins Syntaxin 17 and 18, however only Syntaxin
232 chment protein receptor (SNARE) complexes by SNARE proteins syntaxin-1 (Stx1), synaptosomal-associate
233 between the neuronal SM protein Munc18-1 and SNARE proteins syntaxin-1 and SNAP-25 (25 kDa synaptosom
234 overns neurotransmitter release includes the SNARE proteins syntaxin-1, SNAP-25 and synaptobrevin, wh
235 AMPAR exocytosis, we demonstrate that the Q-SNARE proteins syntaxin-3 and SNAP-47 are required for r
236 r of accessibility of the target membrane (t-SNARE) protein syntaxin 4 to participate in SNARE core c
237 ensitive factor attachment protein receptor (SNARE) protein syntaxin-1 adopts a closed conformation w
238 ensitive factor-attachment protein receptor (SNARE) protein syntaxin-1 exhibits two conformations tha
240 e factor attachment protein (SNAP) receptor (SNARE) proteins syntaxin-1, SNAP-25, and synaptobrevin/V
241 c18-1 protein and its binding partner, the t-SNARE-protein Syntaxin-1, by approximately 30% and decre
242 ilamellar vesicles containing preassembled t-SNARE proteins (syntaxin 1.SNAP-25), we determined how M
243 ensitive factor attachment protein receptor (SNARE) proteins (syntaxin, synaptosomal-associated prote
244 (i) stabilizing and trafficking the central SNARE protein, syntaxin-1 (i.e. chaperoning function), b
245 Exogenous expression of other homologous SNARE proteins, syntaxin 2/3/4 and SNAP-23, which are re
246 n activity-dependent redistribution of the t-SNARE proteins, SYNTAXIN and SNAP-25, away from neurotra
247 ed for mammalian regulated exocytosis: three SNARE proteins, syntaxin, SNAP-25, and synaptobrevin, an
248 to evaluate the contribution of the neuronal SNARE protein Syntaxin1 (Stx1) in vesicle docking, primi
249 ation of both Atg9 and the autophagy-related SNARE protein syntaxin17 with the autophagosome remained
250 interacts with a closed conformation of the SNARE protein syntaxin1a (Syx1a) and with an assembled S
251 ng full-length and truncation mutants of the SNARE proteins syntaxin1A, SNAP-25B, and synaptobrevin2,
254 urthermore, we show that the target membrane SNARE protein SYX-5 colocalizes with a constitutively ac
256 it was shown that PI(4,5)P2and syntaxin 1, a SNARE protein that catalyzes regulated exocytosis, form
257 ically modifying LCs to target a nonneuronal SNARE protein that extends therapeutic potential for tre
258 d that Bves directly interacts with VAMP3, a SNARE protein that facilitates vesicular transport and s
259 ceptions, such as SNAP-25, a neuron-specific SNARE protein that is essential for synaptic vesicle rel
260 aining vesicles and binds to syntaxin 4, a t-SNARE protein that regulates fusion of transport vesicle
261 s that Syn-2 could function as an inhibitory SNARE protein that, when relieved, could promote exocyto
262 hand-off" in channel control between the two SNARE proteins that is woven together with vesicle fusio
263 ensitive factor attachment protein receptor (SNARE) protein that is known to participate in the regul
264 e-attached (t-SNARE) and vesicle-attached (v-SNARE) proteins that zipper together to form a coiled-co
266 oxins (BoNTs) are zinc proteases that cleave SNARE proteins to elicit flaccid paralysis by inhibiting
267 ctivating syntaxin-4 (STX-4) to bind cognate SNARE proteins to form a SNARE complex that mediates exo
268 opportunities for in vitro investigations of SNARE proteins to improve our understanding of their rol
269 e neurotoxins are zinc proteases that cleave SNARE proteins to inhibit synaptic vesicle fusion to the
271 is essential for eukaryotic life, requiring SNARE proteins to zipper up in an alpha-helical bundle t
272 pulling the transmembrane regions (TMRs) of SNARE proteins together, thus allowing their TMRs to for
275 our results reveal that B-cells rely on the SNARE protein Vamp-7 to promote the local exocytosis of
276 Fusion is mediated by trans complexes of the SNARE proteins VAMP-2, syntaxin-1, and SNAP-25 that brid
278 COOH of nephrin interacts with the vesicular SNARE protein VAMP2 in vitro and ex vivo (using yeast-2
280 from DA-IPC varicosities, but the vesicular SNARE protein, vamp2, was present in a fraction of those
281 mission, whereas the structurally homologous SNARE protein VAMP4 selectively maintains bulk Ca(2+)-de
284 on process is mediated by a conserved set of SNARE proteins: vesicular synaptobrevin and plasma membr
285 w mutant allele of VTI11 that implicates the SNARE protein VTI11 in homotypic fusion of protein stora
289 a Rab GTPase, a large Rab effector complex, SNARE proteins which can form a 4-helical bundle, and th
290 ng to SNAREs and the Habc domain of the Vam3 SNARE protein, which may explain its function during fus
291 , the HIV-1 glycoprotein 41 and the synaptic SNARE proteins, which involved transitions between two a
292 nderlying initial plasma membrane contact by SNARE proteins, which subsequently become palmitoylated
293 cles with the plasma membrane is mediated by SNARE proteins, which transfer a force to the membranes.
294 ve fusion (NSF) attachment protein receptor (SNARE) proteins, which promote fusion of synaptic vesicl
295 We site-specifically labeled recombinant SNARE proteins with a FRET donor and acceptor before mic
296 ely charged amino acids of secretory vesicle SNARE proteins with similar domains of plasma membrane S
300 Vesicular and target membrane-localized SNARE proteins zipper up into an alpha-helical bundle th
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