SNAREs — engines for membrane fusion
By R. Jahn, R. Scheller. Nature reviews. Molecular cell biology, 2006
2,617 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/fd3b47ec37ea35f8983abd9fa313dcd146512d50
How researchers see this paper
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In Cell Biology
- Emmanuel Boucrot
- S. Martens
- Michael M. Kozlov
- P. Saftig
- H. McMahon
- Y. Ohsumi
- D. Fasshauer
- L. Chernomordik
In Molecular Biology
- Emmanuel Boucrot
- H. McMahon
- Michael M. Kozlov
- P. Saftig
- L. Chernomordik
- R. Jahn
- D. Fasshauer
- S. Martens
Citations in the corpus
- SNARE Protein Recycling by aSNAP and bSNAP Supports Synaptic Vesicle Priming (2010, neutral): “The latter reside on the SV (Synaptobrevin-2) and synaptic plasma membrane (Syntaxin-1, SNAP-25), and their zipper-like assembly into a tight complex drives the membrane fusion reaction (Jahn and Scheller, 2006).”
- The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. (2012, neutral): “Specific membrane fusion is generally achieved by soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes (Hong, 2005; Jahn and Scheller, 2006).”
- Botulinum Neurotoxins: Biology, Pharmacology, and Toxicology (2017, neutral): “5B (Chai et al., 2006; Jin et al., 2006; Berntsson et al., 2013a,b).”
- Molecular machines governing exocytosis of synaptic vesicles (2012, background): “Furthermore, we consider it unlikely that the control of the neuronal SNAREs is exerted by tinkering with its structurally highly conserved engine core, that is, the helical bundle whose major features (structure, stability, folding– unfolding hysteresis) are remarkably similar between SNAREs in reg”
- Lysosomes: fusion and function (2007, background): “A functional trans -SNARE complex must contain one helix of each typ”
- Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. (2007, background): “For a recent review on SNAREs and their role in membrane fusion, see Jahn and Scheller (2006).”
- Do astrocytes really exocytose neurotransmitters? (2010, background): “At neuronal synapses, VAMP2 forms a SNARE complex with the plasma membrane proteins synaptosomal-associated protein 25 ( SNAP25 ) and syntaxi”
- Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion. (2007, background): “As has been suggested for SNARE-mediated fusion (Jahn and Scheller , 2006), a tight association between Atg8-PE molecules on different membranes may bring the two lipid bilayers in close proximity and induce their deformation, leading to hemifusion.”
- Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function (2009, background): “Although the cytoplasmic domains of SNAREs are essential for sortin”
- Physiology of Astroglia. (2018, neutral): “Of these, R(arginine)-SNAREs (also known as vesicle-associated membrane proteins or VAMPs) are associated with the membranes of secretory vesicles, while Q(glutamine)SNAREs are associated with plasmalemma (784, 839).”
- Computed structures of core eukaryotic protein complexes (2021, neutral): “This model also recapit-ulates the disulfide bond between Gpi8 (Cys 85 ) and Gpi16 (Cys 202 ), previously characterized for human GPI-T ( 94 ) [the existence of this disulfide bond in yeast GPI-T has been called into question ( 90 )].”
- Mechanisms of regulated unconventional protein secretion (2009, background): “As is the case for most cellular fusion events, direct fusion of ER-derived vesicles to either the endosomal/lysosomal compartment or the plasma membrane is likely to depend on the typical fusion machinery, which comprises the formation of cognate complexes of SNARE proteins, the ATPase NSF and its ”