Results 21 to 30 of about 73,344 (342)
Lysophosphatidylcholine inhibits membrane‐associated SNARE complex disassembly [PDF]
Journal of Cellular and Molecular Medicine, 2012 AbstractIn cells, N‐ethylmaleimide‐sensitive factor (NSF) attachment protein receptors called SNAREs are involved in membrane fusion. In neurons, for example, target membrane proteins SNAP‐25 and syntaxin called t‐SNAREs present at the pre‐synaptic membrane, and a synaptic vesicle‐associated membrane protein (VAMP) or v‐SNARE, is part of the conserved ...
Shin, Leah +5 more
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The role of the N-D1 linker of the N-ethylmaleimide-sensitive factor in the SNARE disassembly. [PDF]
PLoS ONE, 2013 N-ethylmaleimide-sensitive factor (NSF) is a member of the type II AAA+ (ATPase associated with various cellular activities) family. It plays a critical role in intracellular membrane trafficking by disassembling soluble NSF attachment protein receptor ...
Cui-Cui Liu, Shan Sun, Sen-Fang Sui
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Molecular Dynamics Simulations of the Proteins Regulating Synaptic Vesicle Fusion
Membranes, 2023 Neuronal transmitters are packaged in synaptic vesicles (SVs) and released by the fusion of SVs with the presynaptic membrane (PM). An inflow of Ca2+ into the nerve terminal triggers fusion, and the SV-associated protein Synaptotagmin 1 (Syt1) serves as ...
Maria Bykhovskaia
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SNARE complex‐mediated degranulation in mast cells [PDF]
Journal of Cellular and Molecular Medicine, 2012 Introduction SNARE function in membrane fusion events Expression of SNAREs and SNARE complexes in mast cells Functional studies implicating specific SNAREs or SNARE complexes in mast cell degranulation RNA interference studies, SNARES and mast cells Regulation of mast cell SNAREs Conclusions Mast cell function and dysregulation is important in the ...
Woska, Joseph R, Gillespie, Marc E
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Epigallocatechin gallate inhibits SNARE‐dependent membrane fusion by blocking trans‐SNARE assembly
FEBS Open Bio, 2022 Insulin secretion is a signal‐triggered process that requires membrane fusion between the secretory granules and plasma membrane in pancreatic β cells. The exocytosis of insulin is mediated by target‐soluble N‐ethylmaleimide sensitive factor attachment ...
Min Zhu +4 more
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Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion [PDF]
The EMBO Journal, 2005 SNARE functions during membrane docking and fusion are regulated by Sec1/Munc18 (SM) chaperones and Rab/Ypt GTPase effectors. These functions for yeast vacuole fusion are combined in the six-subunit HOPS complex. HOPS facilitates Ypt7p nucleotide exchange, is a Ypt7p effector, and contains an SM protein.
Kevin M, Collins +3 more
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Cell Reports, 2023 Summary: The AAA+ NSF complex is responsible for SNARE complex disassembly both before and after membrane fusion. Loss of NSF function results in pronounced developmental and degenerative defects. In a genetic screen for sensory deficits in zebrafish, we
Yan Gao +8 more
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The COG complex interacts with multiple Golgi SNAREs and enhances fusogenic SNARE complexes assembly [PDF]
Journal of Cell Science, 2013 Multisubunit tethering complexes (MTCs) positively regulate vesicular fusion by as yet unclear mechanism. In this study we provide evidence that the MTC COG enhances the assembly of fusogenic Golgi SNARE complexes and concomitantly prevents nonfusogenic tSNARE interactions.
Orly Laufman, WanJin Hong, Sima Lev
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VAMP721 conformations unmask an extended motif for K+ channel binding and gating control [PDF]
, 2016 Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins play a major role in membrane fusion and contribute to cell expansion, signaling, and polar growth in plants.
Blatt, Mike R. +4 more
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COG complexes form spatial landmarks for distinct SNARE complexes [PDF]
Nature Communications, 2013 Vesicular tethers and SNAREs (soluble N-ethylmalemide-sensitive fusion attachment protein receptors) are two key protein components of the intracellular membrane-trafficking machinery. The conserved oligomeric Golgi (COG) complex has been implicated in the tethering of retrograde intra-Golgi vesicles.
Willett, Rose +6 more
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