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ATP5O — SNAP25

Text-mined interactions from Literome

Polgár et al., Blood 1999 : The peptides that inhibited platelet granule secretion also inhibited the human recombinant alpha-SNAP stimulated ATPase activity of recombinant NSF ... It was also found that anti-NSF antibodies, which inhibited recombinant alpha-SNAP stimulated ATPase activity of NSF, inhibited platelet granule secretion in permeabilized cells
Matveeva et al., Biochemistry 2002 : Mutation of two conserved arginine residues in the NSF-D1 SRH ( R385A and R388A ) did not effect basal or soluble NSF attachment protein (SNAP) stimulated ATPase activity ; however, neither mutant underwent ATP dependent release from SNAP-SNARE complexes
Horsnell et al., Biochemistry 2002 : Instead, the stimulation of ATPase activity by alpha-SNAP required for wild-type NSF to disassemble SNARE complexes does not occur in the mutant NSF ( st53 ) protein ... Furthermore, the mutants characterized here define key residues involved in two essential, but mechanistically distinct, biochemical functions of NSF : SNAP binding and SNAP dependent ATPase stimulation
Bełtowski et al., J Physiol Pharmacol 2003 : In addition, inhibitory effect of either SNAP or 8-bromo-cGMP on medullary Na+, K ( + ) -ATPase was abolished by 17-octadecynoic acid ( 17-ODYA ), which inhibits cytochrome P450 dependent metabolism of arachidonic acid
Parnas et al., J Neurophysiol 2006 (Synaptic Transmission) : Peptides that inhibit the SNAP stimulated ATPase activity of N-ethylmaleimide-sensitive fusion protein ( NSF-2, NSF-3 ) were injected intra-axonally to study the role of this protein in the release of glutamate at the crayfish neuromuscular junction
Liu et al., PloS one 2013 : This study presents detailed mutagenesis analyses of NSF N-D1 linker, dissecting its role in the SNARE disassembly, the SNARE/a-SNAP complex binding, the basal ATPase activity and the SNARE/a-SNAP stimulated ATPase activity ... Our results show that the N-terminal region of the N-D1 linker associated mutants cause severe defect in SNARE complex disassembly, but little effects on the SNARE/a-SNAP complex binding, the basal and the SNARE/a-SNAP stimulated ATPase activity, suggesting this region may be involved in the motion transmission from D1 to N domain
Sato et al., Brain Res 1995 : These results suggest that NO generating compounds, SNAP , SIN-1 and NOR 3 but not SNP, may release NO or NO-derived products and may inhibit ( Na+, K+ ) -ATPase activity by interacting with a SH group at the active site of the enzyme
Barnard et al., J Cell Biol 1997 : Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis ... Deletion of up to 160 NH2-terminal amino acids had little effect on the ability of alpha-SNAP to stimulate the ATPase activity of NSF
Colombo et al., J Biol Chem 1998 : We present evidence that alpha-SNAP is released from the membranes in a temperature- and time dependent manner and that this release is mediated by the ATPase activity of NSF
Matveeva et al., FEBS Lett 1998 : The effects of SNAP/SNARE complexes on the ATPase of NSF ... While NSF interacts with all alpha-SNAP containing complexes, only the alpha-SNAP/t-SNARE complex significantly stimulated ATPase activity