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1 nimal model for membrane fusion, inspired by SNARE proteins.
2 LegC7/YlfA] functionally mimic glutamine (Q)-SNARE proteins.
3 me degradation by disrupting the function of SNARE proteins.
4 ed at the end of the transmembrane domain of SNARE proteins.
5 ction between alpha-synuclein and any of the SNARE proteins.
6 ugh interactions with the syntaxin family of SNARE proteins.
7 rocessive unwinding mechanism to disassemble SNARE proteins.
8 ins in membrane fusion by directly acting on SNARE proteins.
9 r evolutionarily conserved structures in the SNARE proteins.
10 to neurons and specific cleavage of neuronal SNARE proteins.
11 c binding to nerve terminals and cleavage of SNARE proteins.
12 uires homotypic membrane fusion catalyzed by SNARE proteins.
13  Ca(2+) and through direct interactions with SNARE proteins.
14 rms and requires membrane integration of the SNARE proteins.
15  (SNARE) complexes between vesicle and Golgi SNARE proteins.
16 t ability to bind calcium, phospholipids, or SNARE proteins.
17 s and relies on membrane fusion catalyzed by SNARE proteins.
18 aptic vesicle (SV) exocytosis is mediated by SNARE proteins.
19  functional interactions between presynaptic SNARE proteins.
20 c1/Munc18 (SM) proteins to specific syntaxin SNARE proteins.
21 5 (STX5), a member of the syntaxin family of SNARE proteins.
22 ric Golgi (COG) complex and with intra-Golgi SNARE proteins.
23  transmission by endoproteolytic cleavage of SNARE proteins.
24 rm motility, calcium channel regulation, and SNARE proteins.
25 ensitive factor attachment protein receptor (SNARE) proteins.
26 ensitive-factor attachment protein receptor (SNARE) proteins.
27 ensitive factor attachment protein receptor (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
32 ucleins (maintain functional conformation of SNARE proteins after complex disassembly).
33 lexin clamps otherwise spontaneous fusion by SNARE proteins, allowing neurotransmitters and other med
34    Fusion involves complex formation between SNARE proteins anchored to adjacent membranes.
35 ficking through interactions with individual SNARE proteins and assembled SNARE complexes.
36 egregate cargo from source compartments, and SNARE proteins and associated factors that cause vesicle
37 sis particularly involving small G proteins, SNARE proteins and chaperone molecules.
38 an ENTH domain-containing protein that binds SNARE proteins and functions in vesicle trafficking; how
39 he plasma membrane (PM) in relation to other SNARE proteins and inhibition of exocytosis.
40 dylinositol 4,5-bisphosphate (PI(4,5)P2) and SNARE proteins and is proposed to promote SNARE protein
41 he internal distribution of fusion-competent SNARE proteins and limiting homotypic fusions among cont
42    Synapotagmin-1 (Syt1) interacts with both SNARE proteins and lipid membranes to synchronize neurot
43  calcium-binding proteins that interact with SNARE proteins and phospholipids.
44 n which direct interactions between specific SNARE proteins and PIP aquaporins modulate their post-Go
45 s containing elevated levels of the ER-Golgi SNARE proteins and Sly1p were less sensitive to PI(4)P i
46                                     Although SNARE proteins and tethering complexes mediate intracell
47                                   Individual SNARE proteins and the SNARE complex itself have been im
48 Furthermore, we discover a critical role for SNARE proteins and their adaptors during early stages of
49 ensitive factor attachment protein receptor (SNARE) proteins and cytoskeletal proteins.
50 ensitive factor attachment protein receptor (SNARE) proteins and lipid bilayer properties.
51 g of otoferlin C2 domains to target SNARE (t-SNARE) proteins and phospholipids.
52 rocesses are the vesicular fusion machinery (SNARE proteins) and the regulatory proteins, Synaptotagm
53       Exocytosis in platelets is mediated by SNARE proteins, and in most mammalian cells this process
54 icking requires membrane fusion, mediated by SNARE proteins, and upstream events that probably includ
55 ensitive factor attachment protein receptor (SNARE) proteins, and SNARE chaperones of the Sec1/Munc18
56 ent state in which the N-terminal domains of SNARE proteins are assembled.
57 ing scorpion envenomation as both of these v-SNARE proteins are associated with zymogen granule membr
58                                Although many SNARE proteins are available per vesicle, only one to th
59 only observe optimal lipid mixing when the t-SNARE proteins are coexpressed before purification.
60                                    Here, the SNARE proteins are essential by forming the SNARE comple
61                                              SNARE proteins are essential for exocytosis, mediating t
62    In eukaryotic cells, multiple isoforms of SNARE proteins are expressed and are involved in distinc
63         While it is widely accepted that the SNARE proteins are intrinsically disordered in their mon
64                                              SNARE proteins are the core machinery to drive fusion of
65                                              SNARE proteins are the core of the cell's fusion machine
66 ensitive factor attachment protein receptor (SNARE) proteins are key players in cellular trafficking
67 ensitive factor activating protein receptor (SNARE) proteins are the main catalysts for membrane fusi
68          Here using plasma membrane-resident SNARE proteins as model, we show that hydrophobic mismat
69                Vesicular (v)- and target (t)-SNARE proteins assemble in SNARE complex to mediate memb
70 Vesicle fusion is mediated by an assembly of SNARE proteins between opposing membranes, but it is unk
71    Vesicle fusion is mediated by assembly of SNARE proteins between opposing membranes.
72                                              SNARE protein binding by CAPS is novel and mediated by i
73 ctome in mouse brain, we identified not only SNARE proteins but also Munc-18-1 (stabilizes assembled
74   Complexins are unable to bind to monomeric SNARE proteins but bind with high affinity to ternary SN
75   Exocytosis depends on cytosolic domains of SNARE proteins but the function of the transmembrane dom
76 et merger using arresting point mutations in SNARE proteins, but the nature of these states remained
77 tosomal-associated protein of 25 kDa), a key SNARE protein, by immunocytochemistry with cell type-spe
78   Our study supports the idea that endosomal SNARE proteins can have functions unrelated to membrane
79                                              SNARE proteins catalyze many forms of biological membran
80 ensitive factor attachment protein receptor (SNARE) proteins catalyze membrane fusion events in the s
81 siologically, alpha-synuclein functions as a SNARE-protein chaperone that promotes SNARE-complex asse
82 y governed through light chain (LC) protease SNARE protein cleavage leading to a loss of neurotransmi
83 nd SNARE proteins and is proposed to promote SNARE protein complex assembly for vesicle docking and p
84 ules be docked to the plasma membrane by the SNARE protein complex.
85                                              SNARE protein complexes are key mediators of exocytosis
86             Interactions between exocyst and SNARE protein complexes are known, but their functional
87 e cells requires a priming step during which SNARE protein complexes assemble.
88 irect interaction of LegC3 with the vacuolar SNARE protein complexes required for fusion.
89 icking by mediating disassembly and reuse of SNARE protein complexes, which facilitate fusion of vesi
90 ensitive factor attachment protein receptor (SNARE) protein complexes play essential roles in catalyz
91 n, probably via formation of distinct Munc18/SNARE-protein complexes.
92 ve factor (NSF) attachment protein receptor (SNARE) proteins comprise the minimal machinery that trig
93 ensitive factor attachment protein receptor (SNARE) proteins constitute the minimal machinery that ca
94                                              SNARE proteins-core machinery for membrane fusion-are in
95 new insight into the spatial organization of SNARE protein cycling during synaptic activity.
96 lly driven expression of a dominant-negative SNARE protein (dnSNARE) increased baroreflex sensitivity
97 ensitive factor attachment protein receptor (SNARE) proteins drive membrane fusion by assembling into
98 eimide-sensitive factor attachment receptor (SNARE) proteins drive the fusion of synaptic vesicles to
99  which determines its interaction with other SNARE proteins during fusion, is largely unknown.
100 tion of a highly stable four-helix bundle of SNARE proteins embedded in the vesicle and target membra
101 eins with similar domains of plasma membrane SNARE proteins enhancing fusion of the two membranes to
102 ing microscopy between fluorescently labeled SNARE proteins expressed in cultured rat hippocampal neu
103 ntaxin-11 (Stx11), an atypical member of the SNARE protein family, is part of the cytolytic machinery
104                    Syntaxin-1 is the central SNARE protein for neuronal exocytosis.
105                               Before fusion, SNARE proteins form complexes bridging the membrane foll
106                                          The SNARE proteins found in vesicle membranes have previousl
107 yntaxin17, thereby preventing these two host SNARE proteins from mediating autophagosome-lysome fusio
108  by Soluble NSF Attachment Protein Receptor (SNARE) proteins from granule and plasma membranes.
109  of soluble NSF attachment protein receptor (SNARE) proteins from the vesicle membrane (R-SNAREs or v
110 a novel, broadly applied mechanism governing SNARE protein function.
111                        Our data suggest that SNARE proteins function during fusion primarily as force
112 y Lobe A of the COG complex and the purified SNARE proteins Gos1, Sed5 and Sft1.
113              Here, we characterize the Golgi SNARE protein, Gos28, and its role in rhodopsin (Rh1) tr
114 xin-8 mutant that cannot assemble with other SNARE proteins had virtually the same effect as wild-typ
115                            Although multiple SNARE proteins have been implicated in cytotoxic granule
116                 Synaptotagmin-1 and neuronal SNARE proteins have central roles in evoked synchronous
117 Here, we show that syntaxin 8 (MoSyn8), a Qc-SNARE protein homolog, also plays important roles in gro
118 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
121 Munc13-1, CAPS1 binds to syntaxin-1, a key t-SNARE protein in neurosecretion.
122 or protein quality control surveillance of a SNARE protein in the endo-vacuolar system.
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
126 e local interactions of fluorescently tagged SNARE proteins in live cells.
127         Botulinum neurotoxins (BoNTs) cleave SNARE proteins in motor neurons that inhibits synaptic v
128  potently inhibit exocytosis by sequestering SNARE proteins in nonfusogenic complexes.
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
131 ensitive factor attachment protein receptor (SNARE) protein in spontaneous neurotransmission.
132 osed for the transmembrane regions (TMRs) of SNARE proteins, including formation of channel-like tran
133 tors via exocytosis, a process that requires SNARE proteins, including syntaxins (Stxs).
134 olemma, as the response was prevented by the SNARE protein inhibitor N-ethylmaleimide and the calcium
135 t can generate new biological insight of the SNARE protein interactions in plant cells.
136 sicles with the plasma membrane is driven by SNARE protein interactions.
137 eport that syntaxin17 (Stx17), an autophagic SNARE protein interacts with CFTR under nutritional stre
138 thylmaleimide attachment protein receptor (t-SNARE) protein, interferes with VEGFR2 trafficking to th
139 mbly, with continuous generation of reactive SNARE-protein intermediates.
140 king vesicles is mediated by the assembly of SNARE proteins into membrane-bridging complexes.
141 membrane (-v) SNARE and target membrane (t-) SNARE proteins into separate liposome populations.
142 eimide-sensitive factor attachment receptor (SNARE) proteins into a parallel four-helix bundle to dri
143 42 targeted the GHRH receptor and depleted a SNARE protein involved in GH exocytosis, vesicle-associa
144      Thus, the fusogenic F protein resembles SNARE proteins involved in vesicle fusion by having wate
145  mammalian horizontal cells along with other SNARE proteins is consistent with vesicular exocytosis.
146  domain, but whether Munc13-4 interacts with SNARE proteins is unknown.
147 al-associated protein of 25 kDa (SNAP-25), a SNARE protein, is functionally relevant to PKC-dependent
148 binding is specific for a subset of exocytic SNARE protein isoforms and requires membrane integration
149 s exocytotic processes mediated by different SNARE protein isoforms, we systematically analyzed the i
150 lexin binding are regulated by the different SNARE protein isoforms.
151 plexes composed of different combinations of SNARE protein isoforms.
152 ed of exocytosis, but total vesicle numbers, SNARE protein levels, and postsynaptic densities remaine
153                         Syntaxin 3 (Stx3), a SNARE protein located and functioning at the apical plas
154 ow that lipid-anchored STX11 and its cognate SNARE proteins mainly support exchange of lipids but not
155                          We hypothesize that SNARE proteins mediate fusion events at the chlamydial i
156                                In platelets, SNARE proteins mediate the membrane fusion events requir
157 to represent the cytotoxic granule vesicular SNARE protein mediating exocytosis in mice.
158                               SNAP-25 is a Q-SNARE protein mediating exocytosis of neurosecretory ves
159 in 1/SNAP-25 as the ubiquitous and essential SNARE proteins mediating multiple fusion events on neuro
160                                        Among SNARE proteins mediating synaptic vesicle fusion, syntax
161 resynaptic compartments, but does not cleave SNARE proteins nor impair spontaneous neurotransmitter r
162                The stimulatory effect of the SNARE protein on the endocytosis of the channel was abol
163                 However, discrete effects of SNARE proteins on synaptic function have been difficult
164 sential processes require the interaction of SNARE proteins on vesicle and cell membranes, as well as
165 erlin and synaptotagmin bind membrane fusion SNARE proteins, only otoferlin interacts with the L-type
166 ng is driven by the assembly of heterologous SNARE proteins orchestrated by the binding of Sec1/Munc1
167            Synaptobrevin-2, a snap receptor (SNARE) protein, participates in this process by interact
168                                              SNARE proteins play a critical role in intracellular mem
169                                              SNARE proteins play a crucial role in intracellular traf
170                                              SNARE proteins play indispensable roles in membrane fusi
171 ensitive factor attachment protein receptor (SNARE) proteins play a major role in membrane fusion and
172                                              SNARE proteins promote membrane fusion by forming a four
173 um-sensitive scaffolding protein, localizing SNARE proteins proximal to the calcium channel so as to
174 pends on endosomal fusion events mediated by SNARE proteins, Rab-GTPases, and multisubunit tethering
175             How and in what form interacting SNARE proteins reach their sites of action is virtually
176 document a postsynaptic action of this major SNARE protein relevant to synaptic plasticity.
177 livery of large stoichiometric quantities of SNARE proteins required for forming the partitioning mem
178 n at least three respects: 1) The density of SNARE proteins required for fusion in vitro is substanti
179 re highly potent toxins that cleave neuronal SNARE proteins required for neurotransmission, causing f
180  interactions of CAPS with each of the three SNARE proteins required for vesicle exocytosis.
181 ane protein 2 (VAMP2/synaptobrevin2), a core SNARE protein residing on synaptic vesicles (SVs), forms
182 ing factor, the Dsl1 complex, bound with two SNARE proteins, revealing new insights into how tetherin
183                                              SNARE protein's functionality is further regulated by a
184 ensitive factor attachment protein receptor (SNARE) proteins, Sec17p, Sec18p, the Rab Ypt7p, and the
185      Here we monitored interactions of the R-SNARE protein Sec22 through a cysteine scanning approach
186                         The highly conserved SNARE protein SEC22B mediates diverse and critical funct
187 fection there is noncanonical pairing of the SNARE protein Sec22b on ER-derived vesicles with plasma
188 unit Sec6 directly bound the plasma membrane SNARE protein Sec9 in vitro and that Sec6 inhibited the
189 een the Sec6 subunit and the plasma membrane SNARE protein Sec9.
190         We have previously characterized two SNARE proteins, secretory protein (MoSec22) and vesicle-
191  is necessary and sufficient for binding the SNARE protein Sed5 and the COG complex.
192 nown whether transmembrane domains (TMDs) of SNARE proteins serve mechanistic functions that go beyon
193 studies have indicated that the gene for the SNARE protein SNAP-25 is a candidate susceptibility gene
194 is by enzymatically cleaving the presynaptic SNARE protein SNAP-25, which results in lasting inhibiti
195 SPalpha) functions as a co-chaperone for the SNARE protein SNAP-25.
196 age-dependent redistribution of the synaptic SNARE proteins SNAP-25, syntaxin-1 and synaptobrevin-2,
197           Inhibiting the function of two key SNARE proteins, SNAP-25 and syntaxin 4, also eliminated
198 for FcepsilonRI-triggered association of the SNARE protein SNAP23 with the SGs.
199                           S-Acylation of the SNARE protein SNAP25 (synaptosome-associated protein of
200 , we generated mice expressing a form of the SNARE protein SNAP25 with premature truncation of the C
201 aptotagmin-1 (Syt-1) and indirectly with the SNARE proteins SNAP25 and Syntaxin (Stx-1).
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
204 ng exocytosis, directly interacts with the t-SNARE protein Sso2.
205 ect is mediated by the binding of Mig-6 to a SNARE protein STX8, a protein known to be required for l
206        However, insertion of early endosomal SNARE proteins suffices to convert liposomes into traffi
207    The previously reported interactions with SNARE proteins suggested the involvement of septins in e
208 py (EM) studies indicated that the vesicular SNARE protein synaptobrevin (syb) was dispensable for do
209                       The neuronal vesicular SNARE protein synaptobrevin 2 (syb2) is anchored in the
210 s" interactions between the synaptic vesicle SNARE protein synaptobrevin 2 and the plasma membrane sy
211    In contrast, C2F did not bind the vesicle SNARE protein synaptobrevin-1 (VAMP-1).
212                           In contrast, the R-SNARE protein synaptobrevin-2/VAMP2 contributes to both
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
219                               The TMD of the SNARE protein synaptobrevin2/VAMP2 contains two highly c
220 ly, we find that septin 7 interacts with the SNARE protein syntaxin 11 and facilitates its interactio
221  cells and human pseudoislets showed reduced SNARE protein syntaxin 1a (STX1A), a key SNARE component
222 n secretory dysfunction, we identified the t-SNARE protein Syntaxin 4 as a target of modification by
223 demonstrate the involvement of a CAL-binding SNARE protein syntaxin 6 (STX6) in this process.
224 lin responsive aminopeptidase (IRAP) and the SNARE protein Syntaxin 6.
225 eptor (SNARE)-mediated process, and that the SNARE protein syntaxin binds directly to Kv2.1 channels.
226 ically, the SM protein Munc18-1 traps the Qa-SNARE protein syntaxin-1 in an autoinhibited closed conf
227 smitter release and requires that the target-SNARE protein syntaxin-1 switches from a closed to an op
228 ge of ER morphogenic proteins, including the SNARE protein syntaxin-18.
229                                     The core SNARE protein syntaxin-1a (syn1a) was expressed by murin
230                                The endosomal SNARE protein syntaxin-8 interacts with the acid-sensiti
231  the enigmatic protein Munc18 that binds the SNARE protein Syntaxin.
232 Y1 is known to interact with the ER-specific SNARE proteins Syntaxin 17 and 18, however only Syntaxin
233                             Furthermore, the SNARE proteins syntaxin 1A and SNAP-25 were unable to mo
234 direct interaction between dysferlin and the SNARE proteins syntaxin 4 and SNAP-23.
235 chment protein receptor (SNARE) complexes by SNARE proteins syntaxin-1 (Stx1), synaptosomal-associate
236 between the neuronal SM protein Munc18-1 and SNARE proteins syntaxin-1 and SNAP-25 (25 kDa synaptosom
237  AMPAR exocytosis, we demonstrate that the Q-SNARE proteins syntaxin-3 and SNAP-47 are required for r
238 ensitive factor attachment protein receptor (SNARE) protein syntaxin-1 adopts a closed conformation w
239 c18-1 protein and its binding partner, the t-SNARE-protein Syntaxin-1, by approximately 30% and decre
240 ilamellar vesicles containing preassembled t-SNARE proteins (syntaxin 1.SNAP-25), we determined how M
241 ensitive factor attachment protein receptor (SNARE) proteins (syntaxin, synaptosomal-associated prote
242  (i) stabilizing and trafficking the central SNARE protein, syntaxin-1 (i.e. chaperoning function), b
243     Exogenous expression of other homologous SNARE proteins, syntaxin 2/3/4 and SNAP-23, which are re
244 n activity-dependent redistribution of the t-SNARE proteins, SYNTAXIN and SNAP-25, away from neurotra
245 ed for mammalian regulated exocytosis: three SNARE proteins, syntaxin, SNAP-25, and synaptobrevin, an
246 mplex intermediate containing Munc18-1 and 2 SNARE proteins-syntaxin 1 and VAMP2.
247 to evaluate the contribution of the neuronal SNARE protein Syntaxin1 (Stx1) in vesicle docking, primi
248 ation of both Atg9 and the autophagy-related SNARE protein syntaxin17 with the autophagosome remained
249  interacts with a closed conformation of the SNARE protein syntaxin1a (Syx1a) and with an assembled S
250 ng full-length and truncation mutants of the SNARE proteins syntaxin1A, SNAP-25B, and synaptobrevin2,
251                                          The SNARE protein syntaxin4 (Stx4) is involved in the format
252                      Here we report that the SNARE protein SYP121 (SYR1/PEN1), which mediates vesicle
253 urthermore, we show that the target membrane SNARE protein SYX-5 colocalizes with a constitutively ac
254             Tomosyn is a 130-kDa cytosolic R-SNARE protein that associates with Q-SNAREs and reduces
255 it was shown that PI(4,5)P2and syntaxin 1, a SNARE protein that catalyzes regulated exocytosis, form
256 ically modifying LCs to target a nonneuronal SNARE protein that extends therapeutic potential for tre
257 d that Bves directly interacts with VAMP3, a SNARE protein that facilitates vesicular transport and s
258                    The Vam7 gene encodes a v-SNARE protein that involved in vesicle trafficking in fu
259 ceptions, such as SNAP-25, a neuron-specific SNARE protein that is essential for synaptic vesicle rel
260 s that Syn-2 could function as an inhibitory SNARE protein that, when relieved, could promote exocyto
261  Syntaxins are a family of membrane-anchored SNARE proteins that are essential components required fo
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 has been extensively studied in its
264 ensitive factor attachment protein receptor (SNARE) protein that is known to participate in the regul
265 e-attached (t-SNARE) and vesicle-attached (v-SNARE) proteins that zipper together to form a coiled-co
266 thought to act primarily through one type of SNARE protein, the syntaxins.
267 agonism between SNORD50A/B RNAs and specific SNARE proteins thus controls KRAS localization, signalin
268 ctivating syntaxin-4 (STX-4) to bind cognate SNARE proteins to form a SNARE complex that mediates exo
269 ate that syntaxin 1 and SNAP-25 cooperate as SNARE proteins to support neuron survival.
270  is essential for eukaryotic life, requiring SNARE proteins to zipper up in an alpha-helical bundle t
271  pulling the transmembrane regions (TMRs) of SNARE proteins together, thus allowing their TMRs to for
272 sicles to target membranes, recruit multiple SNARE proteins, trigger their conformational changes, an
273                       The surface density of SNARE proteins turns out to be the most critical paramet
274 unction of FolVam7, a homologue of the yeast SNARE protein Vam7p in Fusarium oxysporum f. sp. lycoper
275                      Here we show that the v-SNARE protein Vamp-7 is associated with Lamp-1(+) lysoso
276  our results reveal that B-cells rely on the SNARE protein Vamp-7 to promote the local exocytosis of
277 Fusion is mediated by trans complexes of the SNARE proteins VAMP-2, syntaxin-1, and SNAP-25 that brid
278 ytes, where it interacts with a post-Golgi v-SNARE protein, VAMP1, and acetylated microtubules.
279                  VAMP2 encodes the vesicular SNARE protein VAMP2 (also called synaptobrevin-2).
280                                  The vesicle SNARE proteins VAMP2 (vesicle associated membrane protei
281 mission, whereas the structurally homologous SNARE protein VAMP4 selectively maintains bulk Ca(2+)-de
282 L1 precursor homotypic fusion depends on the SNARE protein VAMP7 together with partner SNAREs.
283 w mutant allele of VTI11 that implicates the SNARE protein VTI11 in homotypic fusion of protein stora
284                                          The SNARE protein vti1a is proposed to drive fusion of intra
285 s or to liposomes containing PI(4,5)P2 and Q-SNARE proteins was mainly dimer.
286                     Studies with recombinant SNARE proteins were used to determine the specific cleav
287  a Rab GTPase, a large Rab effector complex, SNARE proteins which can form a 4-helical bundle, and th
288 ng to SNAREs and the Habc domain of the Vam3 SNARE protein, which may explain its function during fus
289 ng nerve endings, they cleave and inactivate SNARE proteins, which are essential for neurotransmitter
290 , the HIV-1 glycoprotein 41 and the synaptic SNARE proteins, which involved transitions between two a
291 nderlying initial plasma membrane contact by SNARE proteins, which subsequently become palmitoylated
292 cles with the plasma membrane is mediated by SNARE proteins, which transfer a force to the membranes.
293 ve fusion (NSF) attachment protein receptor (SNARE) proteins, which promote fusion of synaptic vesicl
294     We site-specifically labeled recombinant SNARE proteins with a FRET donor and acceptor before mic
295 ely charged amino acids of secretory vesicle SNARE proteins with similar domains of plasma membrane S
296 n with the co-opted the syntaxin18-like Ufe1 SNARE protein within the TBSV replication compartments.
297 rified fraction selectively cleave essential SNARE proteins within exocrine pancreatic tissue.
298 response to lysosomal stress by impeding the SNARE protein ykt6.
299                                              SNARE proteins zipper to form complexes (SNAREpins) that
300      Vesicular and target membrane-localized SNARE proteins zipper up into an alpha-helical bundle th

 
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