Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
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Interacting proteins: P02686 and P17252 Pubmed SVM Score :1.1344993
Purified PKC delta was 3 fold more reactive with CPI 17 compared with myelin basic protein , whereas purified PKC alpha and recombinant RhoA activated kinases ( Rho associated coiled coil forming protein Ser / Thr kinase and protein kinase N ) showed equal activity with CPI 17 and myelin basic protein . inhibited CPI 17 phosphorylation by purified PKC delta with IC ( 50 ) of 0 . 6 microm ( in the presence of 0 . 1 mm ATP ) or 14 microm ( 2 . 0 mm ATP ) . significantly suppressed CPI 17 phosphorylation in smooth muscle cells , and the contraction of permeabilized rabbit femoral artery induced by stimulation with phorbol ester . 1.1344993^^^
Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
In contrast to PKC zeta , the PKC delta enzyme activity phosphorylated MBP or histone in a phosphatidylserine ( PS ) / diacylglycerol ( DG ) dependent manner , albeit not to the same extent as PKC alpha . ^^^
Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
PKC inhibition resulting from long term exposure to 4 beta phorbol 12 , 13 dibutyrate ( 4 beta PDB ) reduced steady state levels of MBP , PLP , MAG , CNP , and PKC alpha mRNAs , as detected by slot blots or in situ hybridization , and downregulated the oligodendrocyte specific markers O 4 , galactosyl cerebroside , and the major constituent proteins MBP and PLP , as detected by immunocytochemistry . ^^^
Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
Additionally , a myelin basic protein ( MBP ) derived peptide , which was readily phosphorylated by PKC alpha , was a poor substrate for PKC theta . ^^^
Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
Except for PKC zeta , all subtypes tested phosphorylated myelin basic protein ( MBP ) , histone , or a peptide derived from the pseudosubstrate region of PKC alpha in a PS / DAG dependent manner but to varying extents . ^^^
Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
Increasing concentrations of myelin basic protein as a PKC alpha or delta substrate also caused increased potency of inhibition by UCN 01 . ^^^
Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
In the presence of the classical PKC activators phosphatidylserine / diacylglycerol , PKC alpha phosphorylates a PKC alpha pseudosubstrate derived peptide , an epidermal growth factor receptor derived peptide , histone 3 S and myelin basic protein to an equal extent , whilst PKC zeta phosphorylates only the PKC alpha derived peptide . ^^^ However , arachidonic acid greatly diminishes PKC alpha activity towards the epidermal growth factor receptor derived peptide , histone 3 S and myelin basic protein , but enhances PKC zeta activity towards the PKC alpha derived peptide . ^^^
Interacting proteins: P02686 and P17252 Pubmed SVM Score :0.0
The phosphorylation of MBP 4 14 ( from myelin basic protein ) was partially dependent on extracellular Ca2+ , implicating activation of PKC alpha , whereas phosphorylation of the so called epsilon peptide was Ca ( 2+ ) independent and prolonged . ^^^