Fusion pore expansion in horse eosinophils is modulated by Ca2+ and protein kinase C via distinct mechanisms.
about
Distinct initial SNARE configurations underlying the diversity of exocytosisFusion-activated Ca(2+) entry: an "active zone" of elevated Ca(2+) during the postfusion stage of lamellar body exocytosis in rat type II pneumocytesPhosphorylation of Munc18 by protein kinase C regulates the kinetics of exocytosis.Dynamin-dependent and dynamin-independent processes contribute to the regulation of single vesicle release kinetics and quantal size.Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin.Genetic control of fusion pore expansion in the epidermis of Caenorhabditis elegans.F-actin and myosin II accelerate catecholamine release from chromaffin granules.Fusion-activated Ca2+ entry via vesicular P2X4 receptors promotes fusion pore opening and exocytotic content release in pneumocytesMechanical forces impeding exocytotic surfactant release revealed by optical tweezers.Stimulation of exocytosis without a calcium signal.Controlling allergic inflammation by signaling regulation of eosinophils.Striatal dopamine neurotransmission: regulation of release and uptakeFusion pore modulation as a presynaptic mechanism contributing to expression of long-term potentiation.Paired-pulse depression of unitary quantal amplitude at single hippocampal synapsesActive zones for presynaptic plasticity in the brain.Biochemical and functional studies of cortical vesicle fusion: the SNARE complex and Ca2+ sensitivity.Fusion pore expansion is a slow, discontinuous, and Ca2+-dependent process regulating secretion from alveolar type II cellsRegulation of exocytosis by protein kinases and Ca(2+) in pancreatic duct epithelial cellsElementary properties of spontaneous fusion of peptidergic vesicles: fusion pore gating.The role of the C terminus of the SNARE protein SNAP-25 in fusion pore opening and a model for fusion pore mechanicsHigh resolution electrophysiological techniques for the study of calcium-activated exocytosis.How the stimulus defines the dynamics of vesicle pool recruitment, fusion mode, and vesicle recycling in neuroendocrine cells.Fusion pores and their control of neurotransmitter and hormone release.Fusion of lamellar body with plasma membrane is driven by the dual action of annexin II tetramer and arachidonic acid.Exocytosis of catecholamine (CA)-containing and CA-free granules in chromaffin cells.Properties of fast endocytosis at hippocampal synapses.New insights into the control of secretion.Vesicular calcium channels as regulators of the exocytotic post-fusion phase.Synaptotagmin-7 links fusion-activated Ca²⁺ entry and fusion pore dilation.Fusion proteins and fusion pores. Workshop: regulated exocytosis and the vesicle cycle.Munc-18-1 regulates the initial release rate of exocytosis.PKC theta activity maintains normal quantal size in chromaffin cells.Role of intracellular kinases in the regulation of equine eosinophil migration and actin polymerization.Subanesthetic doses of ketamine stabilize the fusion pore in a narrow flickering state in astrocytes.A rapid exocytosis mode in chromaffin cells with a neuronal phenotype.Visualization of Membrane Pore in Live Cells Reveals a Dynamic-Pore Theory Governing Fusion and Endocytosis.Calcium channel subtypes differentially regulate fusion pore stability and expansion
P2860
Q26866150-E2D912DF-ADCA-4242-896A-794B8AFDC435Q27325531-35F4D4B6-67D1-4314-94F6-252EBED7B0E0Q27863317-DF11A066-B722-4556-9D7A-D2CBA4CAA2D7Q30165438-1A443FB5-B28E-4F4A-8A1C-6EA5925BCDBCQ30440963-EE0F4818-B139-4993-8A3A-219E801C0319Q30479203-588C8F4D-4B10-4B1B-96E0-238E35088512Q30485822-8091153A-AF5C-4370-916D-1D169BDC0C65Q30503984-AFB4DF22-D6E6-4FEB-9D6D-A10C49535B8FQ30883497-AC6A3A53-8003-4AF5-ABB8-3C35DCBF68C0Q33750203-1704F20F-1AE5-48CE-971F-73A25FDE6F01Q34184626-CE265B0B-AC61-43C9-B084-6A1636FBE626Q34524803-10BC0227-B1F5-4C4B-AC50-A96916946E3CQ35124807-5CFB8F1E-3605-437C-811A-C78DB148BBD5Q35732483-772B37FB-91A9-486A-BB47-319E388DFDD0Q35998752-7E56101A-16B7-4662-80F1-8065BFE8B890Q36328525-BE19F4C1-1A36-4A21-969E-06A64E36402CQ36380016-FF5433D2-3DE1-4238-B738-B5F72CE371C6Q36438877-78EDA900-E8FA-4908-AF42-9B6125753136Q36843562-830486BF-14AE-4E49-988B-019BD3D66A88Q36926938-82249224-4572-4A4A-B6B2-AA7E5765FF71Q37972485-16D6AFB8-1170-4D6B-973A-00EBA044F399Q38724299-86AD20F2-6825-4656-BB29-B09C6F9C6FF1Q39123295-32EC3B9A-A4DB-47E6-BA89-C5E0C1DD2915Q39391919-A9061B30-C01E-4F45-9A45-83DEE5DA7D47Q40689422-686D6B58-6EA6-43BA-A1E0-CBA6C314CAB3Q40856117-6BAC1880-36FE-45F7-BB61-9FF7198E6C73Q42162321-1FCF7AA9-95F9-41F0-9851-10FCA16805A9Q42578339-BBA1E42D-1051-45A2-BCC8-149563CB0117Q42614881-5B5731A7-9666-44E9-9490-418489197868Q42724000-6FDAA9FD-779C-474F-A234-51A9DD50397DQ42935665-ADE08AFB-7B40-4D11-8462-2F478A2F3F7FQ46772962-6192DA99-DEC9-411A-80BD-2CA577E8DA06Q46821709-2EE0DD9B-C49C-41A4-ACBE-68D859DF5C86Q47417302-30EE5FCB-A8D6-4F78-A5FC-32E4FE03A9C4Q48454677-78AAF9A0-E6CE-404F-A7CB-B4DA33A595FDQ53833435-62F3BEC0-CC95-4BD2-8ADD-991D31B38F8FQ58422492-44499555-816E-44F7-A9E2-83C825B6B184
P2860
Fusion pore expansion in horse eosinophils is modulated by Ca2+ and protein kinase C via distinct mechanisms.
description
1998 nî lūn-bûn
@nan
1998 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Fusion pore expansion in horse ...... ase C via distinct mechanisms.
@ast
Fusion pore expansion in horse ...... ase C via distinct mechanisms.
@en
type
label
Fusion pore expansion in horse ...... ase C via distinct mechanisms.
@ast
Fusion pore expansion in horse ...... ase C via distinct mechanisms.
@en
prefLabel
Fusion pore expansion in horse ...... ase C via distinct mechanisms.
@ast
Fusion pore expansion in horse ...... ase C via distinct mechanisms.
@en
P2093
P2860
P356
P1433
P1476
Fusion pore expansion in horse ...... ase C via distinct mechanisms.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/17.15.4340
P407
P577
1998-08-01T00:00:00Z