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Schiavo, G.1
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46
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Transcytosis-associated protein (TAP)/p115 is a general fusion factor required for bidning of vesicles to acceptor membranes
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Barroso, M.1
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Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes
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Lupashin VV, Hamamoto S, Schekman RW. Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes. J Cell Biol. 132:1996;277-289.
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48
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0031040763
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Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
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Biochemical and microscopic assays for the docking step of in vitro vacuole fusion are described and used to show that Sec18p (NSF) and Sec17p (α-SNAP) have to prime both fusion partners and that the small GTP-binding protein Ypt7p plays an essential role in stabilising membrane docking. of special interest
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Mayer A, Wickner W. Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF). J Cell Biol. 136:1997;307-317 Biochemical and microscopic assays for the docking step of in vitro vacuole fusion are described and used to show that Sec18p (NSF) and Sec17p (α-SNAP) have to prime both fusion partners and that the small GTP-binding protein Ypt7p plays an essential role in stabilising membrane docking. of special interest.
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Mayer, A.1
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49
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Piccolo, a novel 420 kDa protein associated with the presynaptic cytomatrix
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Cases-Langhoff C, Voss B, Garner AM, Appeltauer U, Takei K, Kindler S, Veh RW, De Camilli P, Gundelfinger ED, Garner CC. Piccolo, a novel 420 kDa protein associated with the presynaptic cytomatrix. Eur J Cell Biol. 69:1996;214-223.
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Cases-Langhoff, C.1
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Veh, R.W.7
De Camilli, P.8
Gundelfinger, E.D.9
Garner, C.C.10
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50
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0029809130
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2+-dependent exocytosis
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2+-stimulated membrane fusion at a point following ATP hydrolysis. As SNAREs are cleaved by toxins (and, in particular, by the botulinum neurotoxin type E used here) in their post-NSF conformation (i.e. only when disassembled), this suggests that SNAREs must be involved in a reaction subsequent to their disassembly by NSF that is important for membrane fusion and that is perturbed by toxin cleavage. of special interest
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2+-stimulated membrane fusion at a point following ATP hydrolysis. As SNAREs are cleaved by toxins (and, in particular, by the botulinum neurotoxin type E used here) in their post-NSF conformation (i.e. only when disassembled), this suggests that SNAREs must be involved in a reaction subsequent to their disassembly by NSF that is important for membrane fusion and that is perturbed by toxin cleavage. of special interest.
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Banerjee, A.1
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51
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Calcium-regulated exocytosis is required for cell membrane resealing
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Bi, G.1
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52
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0024966027
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Dissection of a single round of vesicular transport: Sequential intermediates for intercisternal movement in the Golgi stack
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Orci L, Malhotra V, Amherdt M, Serafini T, Rothman JE. Dissection of a single round of vesicular transport: sequential intermediates for intercisternal movement in the Golgi stack. Cell. 56:1989;357-368.
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53
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0029980441
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Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles
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Homotypic fusion between vacuole precursors in vitro is used to establish that the action of Sec17p (α-SNAP) and Sec18p (NSF) can precede membrane docking. This study marks a turning point in thinking about the role of NSF in membrane fusion, as it argues against the previously accepted contention that NSF action is important primarily at a point between docking and fusion. of outstanding interest
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Mayer A, Wickner W, Haas A. Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles. Cell. 85:1996;83-94 Homotypic fusion between vacuole precursors in vitro is used to establish that the action of Sec17p (α-SNAP) and Sec18p (NSF) can precede membrane docking. This study marks a turning point in thinking about the role of NSF in membrane fusion, as it argues against the previously accepted contention that NSF action is important primarily at a point between docking and fusion. of outstanding interest.
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Cell
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Mayer, A.1
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Haas, A.3
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54
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0030954439
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Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of monodisperse synaptic vesicles
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Isolated synaptic vesicles contain ternary SNARE complexes that can be reversibly disassembled by NSF. SNARE complexes can thus assemble when the SNARE components reside in the same membrane, and NSF can act on such single-membrane complexes. of special interest
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Otto H, Hanson PI, Jahn R. Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of monodisperse synaptic vesicles. Proc Natl Acad Sci USA. 94:1997;6197-6201 Isolated synaptic vesicles contain ternary SNARE complexes that can be reversibly disassembled by NSF. SNARE complexes can thus assemble when the SNARE components reside in the same membrane, and NSF can act on such single-membrane complexes. of special interest.
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Proc Natl Acad Sci USA
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Otto, H.1
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Jahn, R.3
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A possible predocking attachment site for N-ethylmaleimide-sensitive fusion protein
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Colombo MI, Taddese M, Whiteheart SW, Stahl PD. A possible predocking attachment site for N-ethylmaleimide-sensitive fusion protein. J Biol Chem. 271:1996;18810-18816.
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Colombo, M.I.1
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Stahl, P.D.4
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