MinireviewSNARE Complex Structure and Function
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Cited by (83)
Soybean Golgi SNARE 12 protein interacts with Soybean mosaic virus encoded P3N-PIPO protein
2016, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Therefore, the potyvirus P3N-PIPO has been suggested as the classical movement protein (MP) [6,7]. soluble N-ethyl-maleimide-sensitive-factor attachment protein receptors (SNAREs) are small proteins (18–42 kDa) containing cytoplasmic amphipathic helices, referred to as SNARE motifs, that engage in pernicious coiled coil interactions with other SNAREs [8]. In eukaryotic cells, specific membrane fusion between transport vesicles and target membranes is mediated by the SNARE complex that assembles into a tight cluster of four coiled-coil helices [9–12].
Orchestrating Lymphocyte Polarity in Cognate Immune Cell–Cell Interactions
2016, International Review of Cell and Molecular BiologyCitation Excerpt :Specifically, vesicles carry specific vesicle (v-) SNARE and target membranes contain target (t-) SNAREs. Vesicle docking and priming is enabled by the formation of a complex between two t-SNAREs (syntaxin-3 or -4 and SNAP-23 in nonneuronal cells) and one v-SNARE, for example, VAMP3 (Hay, 2001). This process requires the presence of high Ca2+ (Hay, 2001) and depends on MTs (Beemiller et al., 2012).
Members of a mammalian SNARE complex interact in the endoplasmic reticulum in vivo and are found in COPI vesicles
2008, European Journal of Cell BiologySNAP-23 is not essential for constitutive exocytosis in HeLa cells
2007, FEBS LettersVAMP2 regulates phase separation of alpha-synuclein
2023, bioRxivUltrastructural analysis of nigrostriatal dopaminergic terminals in a knockin mouse model of DYT1 dystonia
2023, European Journal of Neuroscience
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