Results 11 to 20 of about 2,154,580 (280)
The C2 Domain of PKCδ Is a Phosphotyrosine Binding Domain [PDF]
Cell, 2005 SummaryIn 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 PKCδ directly binds to phosphotyrosine peptides
Elia, Andrew E.H. +5 more
core +4 more sources
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]
PLoS 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 +2 more sources
The Role of C2 Domains in Two Different Phosphatases: PTEN and SHIP2
Membranes, 2023 Phosphatase and tensin homologue (PTEN) and SH2-containing inositol 5′-phosphatase 2 (SHIP2) are structurally and functionally similar. They both consist of a phosphatase (Ptase) domain and an adjacent C2 domain, and both proteins dephosphorylate ...
Laura H. John +3 more
doaj +5 more sources
Functional mapping of factor VIII C2 domain.
Thrombosis and Haemostasis, 2017 International audienceSummary The factor VIII (FVIII) is a cofactor of the coagulation cascade. The FVIII C2 domain is a critical domain that participates in the interactions with the von Willebrand factor and the phospholipidic surfaces.
Pellequer, Jean-Luc +5 more
core +4 more sources
Membrane-binding properties of the Factor VIII C2 domain [PDF]
Biochemical 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.
Gary E. Gilbert +5 more
core +3 more sources
Frontiers in EndocrinologyIntroductionDouble 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
C2 domain plays critical roles in localization of novel C2 domain-containing protein OsC2DP. [PDF]
Plant Signal Behav, 2019 OsC2DP is a cytosolic protein containing a C2 domain recently identified in rice, which is translocated to the plasma membrane in response to salt stress. Here, we further investigated the subcellular localization of OsC2DP by truncation analysis. In consistent with OsC2DP, OsC2DP1-165 containing C2 domain at the N-terminus was localized to the cytosol.
Fu S, Huang J, Chen Z, Xia J.
europepmc +4 more sources
Effects of weak anchoring on C1 and C2 chevron structures [PDF]
, 2005 We present a theoretical study of the effect of weak anchoring on the transition between C1 and C2 chevron structures in smectic C liquid crystals. We employ a continuum theory which allows for variable cone, azimuthal and layer tilt angles.
Mottram, Nigel +2 more
core +5 more sources
Missense mutations on SynGAP C2 domain impair membrane diffusion. [PDF]
Protein SciSYNGAP1 mutations have been linked to a range of neuropathological disorders and, more recently, to the insurgence of cancer. SynGAP is a postsynaptic Ras GTPase-activating protein that regulates Ras/ERK signaling and synaptic plasticity.
Miotto M +4 more
europepmc +2 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]
PLoS 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