Results 181 to 190 of about 4,044,136 (204)
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Trends in Neurosciences, 2003
Abstract Ca 2+ influx into the presynaptic terminal triggers fusion of synaptic vesicles with the plasma membrane and release of neurotransmitters. A decade of intensive study of the synaptic vesicle protein synaptotagmin I has led to the general belief that this polypeptide functions as a Ca 2+ sensor in this process.
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Abstract Ca 2+ influx into the presynaptic terminal triggers fusion of synaptic vesicles with the plasma membrane and release of neurotransmitters. A decade of intensive study of the synaptic vesicle protein synaptotagmin I has led to the general belief that this polypeptide functions as a Ca 2+ sensor in this process.
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The C2 domains of synaptotagmin – partners in exocytosis
Trends in Biochemical Sciences, 2004Rapid signaling between neurons relies on the Ca(2+)-triggered exocytosis of neurotransmitters. Release is mediated by 'kiss-and-run' or complete fusion of secretory organelles with the plasma membrane. Current models indicate that exocytosis is regulated by synaptotagmin I (syt) and mediated by SNARE (soluble NSF-attachment protein receptor) proteins.
Jihong, Bai, Edwin R, Chapman
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The Role of C2 Domains in PKC Signaling
2012More than two decades ago, the discovery of the first C2 domain in conventional Protein Kinase Cs (cPKCs) and of its role as a calcium-binding motif began to shed light on the activation mechanism of this family of Serine/Threonine kinases which are involved in several critical signal transduction pathways.
Carole A, Farah, Wayne S, Sossin
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C2 domain conformational changes in phospholipase C-δ1
Nature Structural & Molecular Biology, 1996The structure of the PH-domain truncated core of rat phosphoinositide-specific phospholipase C-delta 1 has been determined at 2.4 A resolution and compared to the structure previously determined in a different crystal form. The stereochemical relationship between the EF, catalytic, and C2 domains is essentially identical.
J A, Grobler +3 more
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Arabidopsis PLDs with C2‐domain function distinctively in hypoxia
Physiologia Plantarum, 2018Hypoxia (oxygen deprivation) causes metabolic disturbances at physiological, biochemical and genetic levels and results in decreased plant growth and development. Phospholipase D (PLD)‐mediated signaling was reported for abiotic and biotic stress signaling events in plants.
Premkumar, Albert +4 more
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Analysis of Protein–Lipid Interactions Using Purified C2 Domains
2016C2 domains (C2s) are regulatory protein modules identified in eukaryotic proteins targeted to cell membranes. C2s were initially characterized as independently folded Ca(2+)-dependent phospholipids binding domains; however, later studies have shown that C2s have evolutionarily diverged into Ca(2+)-dependent and Ca(2+)-independent forms.
Perez-Sancho, Jessica +3 more
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Blood, 2000
AbstractFactor VIII C domains contain key binding sites for von Willebrand factor (vWF) and phospholipid membranes. Hemophilic patients were screened for factor VIII C-domain mutations to provide a well-characterized series. Mutated residues were localized to the high-resolution C2 structure and to a homology model of C1.
M L, Liu +7 more
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AbstractFactor VIII C domains contain key binding sites for von Willebrand factor (vWF) and phospholipid membranes. Hemophilic patients were screened for factor VIII C-domain mutations to provide a well-characterized series. Mutated residues were localized to the high-resolution C2 structure and to a homology model of C1.
M L, Liu +7 more
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The AD3 locus of synaptotagmin-1 C2 domains modulates domain stability
Biophysical JournalSynaptotagmin-1 (syt1) functions as the Ca2+-dependent sensor that triggers the rapid and synchronous release of neurotransmitters from neurotransmitter-containing vesicles during neuronal exocytosis. The syt1 protein has two homologous tandem C2 domains that interact with phospholipids in a Ca2+-dependent manner.
Matthew J, Dominguez +9 more
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Role of C2 domain proteins during synaptic vesicle exocytosis
Biochemical Society Transactions, 2010Neurotransmitter release is mediated by the fusion of synaptic vesicles with the presynaptic plasma membrane. Fusion is triggered by a rise in the intracellular calcium concentration and is dependent on the neuronal SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) complex.
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