Results 211 to 220 of about 157,972 (251)
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Structure and mechanism of the unique C2 domain of Aida
The FEBS Journal, 2014Axin interactor, dorsalization‐associated (Aida) was identified as a regulatory factor that utilizes its C‐terminal region to interact with axis formation inhibitor (Axin). Aida abrogates the Axin‐mediated Jun N‐terminal kinase activation required for proper dorsalization during zebrafish embryonic development, and thus functions as a proventralization
Li-Sha, Zheng +10 more
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Journal of Molecular Biology, 2001
Protein kinase Cepsilon (PKCepsilon) is a member of the novel PKCs which are activated by acidic phospholipids, diacylglycerol and phorbol esters, but lack the calcium dependence of classical PKC isotypes. The crystal structures of the C2 domain of PKCepsilon, crystallized both in the absence and in the presence of the two acidic phospholipids, 1,2 ...
Ochoa, Wendy F. +5 more
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Protein kinase Cepsilon (PKCepsilon) is a member of the novel PKCs which are activated by acidic phospholipids, diacylglycerol and phorbol esters, but lack the calcium dependence of classical PKC isotypes. The crystal structures of the C2 domain of PKCepsilon, crystallized both in the absence and in the presence of the two acidic phospholipids, 1,2 ...
Ochoa, Wendy F. +5 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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Roles of calcium ions in the membrane binding of C2 domains
Biochemical Journal, 2001The C2 domain is a membrane-targeting domain found in many cellular proteins involved in signal transduction or membrane trafficking. The majority of C2 domains co-ordinate multiple Ca2+ ions and bind the membrane in a Ca2+-dependent manner. To understand the mechanisms by which Ca2+ mediates the membrane binding of C2 domains, we measured the membrane
R V, Stahelin, W, Cho
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Otoferlin: a multi-C2 domain protein essential for hearing
Trends in Neurosciences, 2012Sound is encoded at synapses between cochlear inner hair cells and the auditory nerve. These synapses are anatomically and functionally specialized to transmit acoustic information with high fidelity over a lifetime. The molecular mechanisms of hair-cell transmitter release have recently attracted substantial interest.
Tina, Pangršič +2 more
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Crystal structure of human Intersectin-2L C2 domain
Biochemical and Biophysical Research Communications, 2013Intersectin-2L (ITSN-2L) is a long isoform of ITSN family, which is a multimodule scaffolding protein functioning in membrane-associated molecular trafficking and signal transduction pathways. ITSN-2L possesses a carboxy-terminal extension encoding a Dbl homology domain (DH), a pleckstrin homology domain (PH) and a C2 domain, suggesting that it could ...
Wei, Zhang +7 more
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DOC2B, C2 Domains, and Calcium: A Tale of Intricate Interactions
Molecular Neurobiology, 2010Ca(+2)-dependent exocytosis involves vesicle docking, priming, fusion, and recycling. This process is performed and regulated by a vast number of synaptic proteins and depends on proper protein-protein and protein-lipid interactions. Double C2 domain (DOC2) is a protein family of three isoforms found while screening DNA libraries with a C2 probe.
Reut, Friedrich +2 more
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Life Sciences, 2003
RGS (regulator of G protein signaling) proteins are GTPase-activating proteins (GAPs) for heterotrimeric G protein alpha subunits and negatively regulate G protein-mediated signal transduction. In this study, we determined the cDNA sequence of a novel Caenorhabditis elegans (C. elegans) RGS protein. The predicted protein, termed C2-RGS, consists of 782
Motoko, Sato +9 more
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RGS (regulator of G protein signaling) proteins are GTPase-activating proteins (GAPs) for heterotrimeric G protein alpha subunits and negatively regulate G protein-mediated signal transduction. In this study, we determined the cDNA sequence of a novel Caenorhabditis elegans (C. elegans) RGS protein. The predicted protein, termed C2-RGS, consists of 782
Motoko, Sato +9 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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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
openaire +2 more sources

