Results 11 to 20 of about 157,920 (289)

The 1.7 Å X-ray crystal structure of the porcine factor VIII C2 domain and binding analysis to anti-human C2 domain antibodies and phospholipid surfaces. [PDF]

open access: yesPLoS ONE, 2015
The factor VIII C2 domain is essential for binding to activated platelet surfaces as well as the cofactor activity of factor VIII in blood coagulation. Inhibitory antibodies against the C2 domain commonly develop following factor VIII replacement therapy
Caileen M Brison   +8 more
doaj   +3 more sources

Structural basis of phosphatidylcholine recognition by the C2–domain of cytosolic phospholipase A2α [PDF]

open access: yeseLife, 2019
Ca2+-stimulated translocation of cytosolic phospholipase A2α (cPLA2α) to the Golgi induces arachidonic acid production, the rate-limiting step in pro-inflammatory eicosanoid synthesis.
Yoshinori Hirano   +8 more
doaj   +3 more sources

The C2 Domain of PKCδ Is a Phosphotyrosine Binding Domain [PDF]

open access: yesCell, 2005
In eukaryotic cells, the SH2 and PTB domains mediate protein-protein interactions by recognizing phosphotyrosine residues on target proteins. Here we make the unexpected finding that the C2 domain of PKCdelta directly binds to phosphotyrosine peptides in a sequence-specific manner. We provide evidence that this domain mediates PKCdelta interaction with
Benes, Cyril H.   +5 more
openaire   +3 more sources

Membrane-binding properties of the Factor VIII C2 domain [PDF]

open access: yesBiochemical Journal, 2011
Factor VIII functions as a cofactor for Factor IXa in a membrane-bound enzyme complex. Membrane binding accelerates the activity of the Factor VIIIa–Factor IXa complex approx. 100000-fold, and the major phospholipid-binding motif of Factor VIII is thought to be on the C2 domain.
Valerie A, Novakovic   +5 more
openaire   +3 more sources

Membrane binding and lipid-protein interaction of the C2 domain from coagulation factor V [PDF]

open access: yesCurrent Research in Structural Biology
Anchoring of coagulation factors to anionic regions of the membrane involves the C2 domain as a key player. The rate of enzymatic reactions of the coagulation factors is increased by several orders of magnitude upon membrane binding. However, the precise
Y. Zenmei Ohkubo   +3 more
doaj   +2 more sources

Structure of the C2 domain from novel protein kinase Cϵ. A membrane binding model for Ca2+-independent C2 domains

open access: yesJournal 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
openaire   +4 more sources

Intramolecular C2 Domain-Mediated Autoinhibition of Protein Kinase C βII [PDF]

open access: yesCell Reports, 2015
The signaling output of protein kinase C (PKC) is exquisitely controlled, with its disruption resulting in pathophysiologies. Identifying the structural basis for autoinhibition is central to developing effective therapies for cancer, where PKC activity ...
Corina E. Antal   +4 more
doaj   +2 more sources

Pancreatic β-cells package double C2-like domain beta protein into extracellular vesicles via tandem C2 domains

open access: yesFrontiers in Endocrinology
IntroductionDouble C2-like domain beta (DOC2B) is a vesicle priming protein critical for glucose-stimulated insulin secretion in β-cells. Individuals with type 1 diabetes (T1D) have lower levels of DOC2B in their residual functional β-cell mass and ...
Diana Esparza   +11 more
doaj   +3 more sources

A novel human TPIP splice-variant (TPIP-C2) mRNA, expressed in human and mouse tissues, strongly inhibits cell growth in HeLa cells. [PDF]

open access: yesPLoS ONE, 2011
Alternative splicing of mRNAs is known to involve a major regulation of gene expression at RNA level in mammalian cells. The PTEN (Phosphatase and TENsin homologue deleted from the human chromosome 10), TPTE (Transmembrane Phosphatase with TEnsin ...
Rasmi Rekha Mishra   +3 more
doaj   +1 more source

Functions of Vertebrate Ferlins

open access: yesCells, 2020
Ferlins are multiple-C2-domain proteins involved in Ca2+-triggered membrane dynamics within the secretory, endocytic and lysosomal pathways. In bony vertebrates there are six ferlin genes encoding, in humans, dysferlin, otoferlin, myoferlin, Fer1L5 and 6
Anna V. Bulankina, Sven Thoms
doaj   +1 more source

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