Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion.
about
Dynamics of SNARE assembly and disassembly during sperm acrosomal exocytosisHOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusionThree v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion.Activation of annexin 7 by protein kinase C in vitro and in vivoSupramaximal cholecystokinin displaces Munc18c from the pancreatic acinar basal surface, redirecting apical exocytosis to the basal membranev-SNAREs control exocytosis of vesicles from priming to fusion.Geranylgeranylated SNAREs are dominant inhibitors of membrane fusionA genomic view of the sea urchin nervous systemDe novo sequencing of peptides using MALDI/TOF-TOF.Sea urchin egg preparations as systems for the study of calcium-triggered exocytosis.Membrane tethering and fusion in the secretory and endocytic pathways.Functional and physical coupling of voltage-sensitive calcium channels with exocytotic proteins: ramifications for the secretion mechanism.Discovery of the Porosome: revealing the molecular mechanism of secretion and membrane fusion in cells.SNARE-mediated lipid mixing depends on the physical state of the vesicles.Ca2+-dependent regulation of synaptic SNARE complex assembly via a calmodulin- and phospholipid-binding domain of synaptobrevin.Transition from hemifusion to pore opening is rate limiting for vacuole membrane fusionSNAREpins are functionally resistant to disruption by NSF and alphaSNAP.Biochemical and functional studies of cortical vesicle fusion: the SNARE complex and Ca2+ sensitivity.Physical and functional interactions of SNAP-23 with annexin A2.A single amino acid near the C terminus of the synaptosomeassociated protein of 25 kDa (SNAP-25) is essential for exocytosis in chromaffin cells.A kinetic analysis of calcium-triggered exocytosisCholesterol, regulated exocytosis and the physiological fusion machine.The Multifaceted Role of SNARE Proteins in Membrane Fusion.Mechanical coupling via the membrane fusion SNARE protein syntaxin 1A: a molecular dynamics study.Membrane hemifusion is a stable intermediate of exocytosis.Enhancement of the Ca(2+)-triggering steps of native membrane fusion via thiol-reactivity.Identifying critical components of native Ca2+-triggered membrane fusion. Integrating studies of proteins and lipids.Membrane fusion. Ready...aim...fire!Protein kinase C phosphorylation of syntaxin 4 in thrombin-activated human platelets.
P2860
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P2860
Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
Calcium can disrupt the SNARE ...... irreversibly blocking fusion.
@en
Calcium can disrupt the SNARE ...... irreversibly blocking fusion.
@nl
type
label
Calcium can disrupt the SNARE ...... irreversibly blocking fusion.
@en
Calcium can disrupt the SNARE ...... irreversibly blocking fusion.
@nl
prefLabel
Calcium can disrupt the SNARE ...... irreversibly blocking fusion.
@en
Calcium can disrupt the SNARE ...... irreversibly blocking fusion.
@nl
P2093
P2860
P356
P1476
Calcium can disrupt the SNARE ...... irreversibly blocking fusion.
@en
P2093
P2860
P304
33667-33673
P356
10.1074/JBC.273.50.33667
P407
P50
P577
1998-12-01T00:00:00Z