Results 51 to 60 of about 72,246 (300)
Frontiers in Molecular Neuroscience, 2017 The Ca2+ sensor synaptotagmin-1 (Syt1) plays an essential function in synaptic exocytosis. Recently, Syt1 has been implicated in synaptic vesicle priming, a maturation step prior to Ca2+-triggered membrane fusion that is believed to involve formation of ...
Yun Li +5 more
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Lamellipodium extension and membrane ruffling require different SNARE-mediated trafficking pathways [PDF]
, 2010 Background Intracellular membrane traffic is an essential component of the membrane remodeling that supports lamellipodium extension during cell adhesion.
Michael Skalski +6 more
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A Dynamic t-SNARE Complex [PDF]
Structure, 2008 Syntaxin-1/SNAP-25 heterodimers with 1:1 stoichiometry likely play a key role in neurotransmitter release but they have been difficult to characterize. In this issue of Structure, Weninger et al. present a beautiful single molecule spectroscopy study showing the dynamic nature of these heterodimers and how they are influenced by other factors.
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Three-dimensional structure of the complexin/snare complex [PDF]
Acta Crystallographica Section A Foundations of Crystallography, 2002 During neurotransmitter release, the neuronal SNARE proteins synaptobrevin/VAMP, syntaxin, and SNAP-25 form a four-helix bundle, the SNARE complex, that pulls the synaptic vesicle and plasma membranes together possibly causing membrane fusion. Complexin binds tightly to the SNARE complex and is essential for efficient Ca(2+)-evoked neurotransmitter ...
Chen, Xiaocheng +6 more
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eLife, 2016 Complexin regulates spontaneous and activates Ca2+-triggered neurotransmitter release, yet the molecular mechanisms are still unclear. Here we performed single molecule fluorescence resonance energy transfer experiments and uncovered two conformations of
Ucheor B Choi +4 more
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Multiple factors maintain assembled trans-SNARE complexes in the presence of NSF and αSNAP
eLife, 2019 Neurotransmitter release requires formation of trans-SNARE complexes between the synaptic vesicle and plasma membranes, which likely underlies synaptic vesicle priming to a release-ready state.
Eric A Prinslow +4 more
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SNARE VTI13 plays a unique role in endosomal trafficking pathways associated with the vacuole and is essential for cell wall organization and root hair growth in arabidopsis [PDF]
, 2014 Background and Aims: Root hairs are responsible for water and nutrient uptake from the soil and their growth is responsive to biotic and abiotic changes in their environment.
Domozych, David S. +2 more
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N-terminal domain of vacuolar SNARE Vam7p promotes trans -SNARE complex assembly [PDF]
Proceedings of the National Academy of Sciences, 2012 SNARE-dependent membrane fusion in eukaryotic cells requires that the heptad-repeat SNARE domains from R- and Q-SNAREs, anchored to apposed membranes, assemble into four-helix coiled-coil bundles. In addition to their SNARE and transmembrane domains, most SNAREs have N-terminal domains (N-domains), although their functions are unclear. The
Hao, Xu, William T, Wickner
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Syntaxin 16 and syntaxin 5 are required for efficient retrograde transport of several exogenous and endogenous cargo proteins [PDF]
, 2007 Retrograde transport allows proteins and lipids to leave the endocytic pathway to reach other intracellular compartments, such as trans-Golgi network (TGN)/Golgi membranes, the endoplasmic reticulum and, in some instances, the cytosol. Here, we have used
Amessou, Mohamed +7 more
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Neurotransmitter release — four years of SNARE complexes
Current Opinion in Neurobiology, 1997 Exocytosis in neurons requires proteins known as SNAREs, membrane proteins that have now been implicated in many intracellular fusion events. SNAREs assemble into stable ternary complexes that are dissociated by the ATPase NSF (N-ethylmaleimide-sensitive factor), working together with SNAPs (soluble NSF attachment proteins).
P I, Hanson, J E, Heuser, R, Jahn
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