Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
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Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
Immunoprecipitation and far western blots reveal that CK 2 and PKD are in fact associated with CSN . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.65533712
By applying a modified overlay method using individual 35S labeled CK 2 subunits , obtained by in vitro translation in rabbit reticulate lysates , it was determined that CK 2 associates with IRS 1 through its alpha / alpha ' subunits ; i . e . in keeping with the fact that IRS 1 is a known substrate for CK 2 . 0.65533712^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.79949586
We have previously shown that CK 2 associates with the human high mobility group protein SSRP 1 and that this association increases in response to UV irradiation . 0.79949586^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
Another site that is theoretically suitable for phosphorylation by CK 2 , at the C terminus of the polypeptide , is not , in fact , phosphorylated . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
The fact that the enzyme activity is surprisingly high in brain and low in heart and lung may be indicative of involvement of CK 2 in processes other than proliferation . ( ABSTRACT TRUNCATED AT 400 WORDS ) . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
Despite the fact that E . coli expressed PIND required phosphorylation by CKII for activation , the phosphorylation negative P protein mutants generated by altering the phosphate acceptors S and T to alanine , surprisingly , showed transcription activity similar to wild type in vitro . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
A great number of studies deal with substrates of CK 2 , but the fact that over 160 substrates exist is more confusing than elucidatory . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
This kinase complex contains casein kinase 2 ( CK 2 ) and the chromatin transcriptional elongation factor FACT ( a heterodimer of hSpt 16 and SSRP 1 ) . ^^^ In vitro studies show that FACT alters the specificity of CK 2 in the complex such that it selectively phosphorylates p 53 over other substrates including casein . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
The occurrence of a cell surface receptor that specifically distinguishes between a phosphorylated and a non phosphorylated analog of Vn , together with the fact that it preferentially activates a distinct intra cellular signaling pathway , suggest that extra cellular CK 2 phosphorylation may play an important role in the regulation of cell adhesion and migration . . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
A search for strategies was conducted in order to obtain a human protein kinase CK 2 preparation which would be suitable for crystallization , despite the fact that the recombinant enzyme is abundant and can be readily purified to homogeneity . ^^^ This seemingly contradiction is based on the fact that the catalytic subunit moiety of the human CK 2 holoenzyme is not stable neither as a free subunit nor in the tetrameric complex . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
The in vivo efficacy of IQA has been assessed by using the fact that treatment of Jurkat cells with IQA inhibits endogenous CK 2 in a dose dependent manner . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
Thus CK 2 is inactive in CCVs because of the fact that it is bound to the CCV membrane via an interaction between PtdIns ( 4 , 5 ) P ( 2 ) in the CCV membrane and the active site in CK2 . . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
Furthermore , the formation of mature eIF5 / eIF2 / eIF3 complex is reduced in these cells , and , in fact , restricted diffusional motion of WT eIF 5 was almost abolished in a GFP tagged eIF 5 mutant lacking CK 2 phosphorylation sites , as measured by fluorescence correlation spectroscopy . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
Activation of casein kinase 2 ( CK 2 ) was one of the first observations made on how Theileria parasites manipulate host cell signal transduction pathways and we argue that CK 2 induction may in fact contribute to many of the different activation events that have been described since 1993 for Theileria infected lymphocytes such as sustained activation of transcription factors c Myc and NF kappaB . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
A major reason for this lack of knowledge is the fact that so far CK2alpha ' rather than CK2alpha has caused serious stability and solubility problems during standard heterologous expression procedures . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
Furthermore , the fact that the interaction between CK 2 subunits and AKT enhances AKT kinase activity identifies a novel molecular mechanism that leads to modulation of AKT activation raising the possibility that CK 2 and AKT might be implicated in common pathways that control cell proliferation and survival . . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
Previously , we purified a UV responsive p 53 serine 392 kinase from F 9 and HeLa cells and found that its activity is attributed to a high molecular weight protein complex containing the protein kinase CK 2 , along with the chromatin associated factors hSPT 16 and SSRP 1 . ^^^ Here we determine that these proteins interact in vitro and in cells via non overlapping domains and provide evidence consistent with the idea that hSPT 16 and SSRP 1 change the conformation of CK 2 upon binding such that it specifically targets p 53 over other substrates . ^^^
Interacting proteins: Q08945 and P68400 Pubmed SVM Score :0.0
Protein kinase CK 2 phosphorylates the high mobility group domain protein SSRP 1 , inducing the recognition of UV damaged DNA . ^^^ Using acetic acid urea polyacrylamide gel electrophoresis and mass spectrometry , we have examined the phosphorylation of maize SSRP 1 by protein kinase CK 2 alpha . ^^^ The affinity of CK 2 alpha phosphorylated SSRP 1 for the DNA correlates with the degree of UV induced DNA damage . ^^^