ArticleThe Biochemical journal1993
Monoclonal antibodies to phosphatidylinositol 4-phosphate 5-kinase: distribution and intracellular localization of the C isoform.
Article in The Biochemical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 18 citations in OpenAlex.
- Nuclear Phosphoinositides as Key Determinants of Nuclear Functions.Biomolecules · 2023Review
- Type IIalpha phosphatidylinositol phosphate kinase associates with the plasma membrane via interaction with type I isoforms.The Biochemical journal · 2002Article
- Regulation of PtdIns4P 5-kinase C by thrombin-stimulated changes in its phosphorylation state in human platelets.The Biochemical journal · 1998Article
- Aggregation-dependent, integrin-mediated increases in cytoskeletally associated PtdInsP2 (4,5) levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton.The EMBO journal · 1996Article
- The cloning and sequence of the C isoform of PtdIns4P 5-kinase.The Biochemical journal · 1995Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have raised a panel of monoclonal antibodies to PtdIns4P 5-kinase C purified from bovine brain [Divecha, Brooksbank and Irvine (1992) Biochem. J. 288, 637-642]. This panel includes antibodies which specifically recognize PtdIns4P 5-kinase C both in a native catalytically active condition, and/or when presented on Western blots. Some of the former antibodies will also inhibit PtdIns4P 5-kinase C activity. We have used the blotting antibodies to study the bovine tissue distribution of PtdIns4P 5-kinase C and its distribution in mammalian species. We have also studied its localization in Jurkat cells and found it to be predominantly bound to membranes, with only a minority localized to the cytoskeleton. Neither PtdIns4P 5-kinase activity nor PtdIns4P 5-kinase C, as detected by Western blotting, were increased in the cytoskeleton after stimulation of Jurkat cells with OKT3. These antibodies should prove to be extremely useful tools with which to study the regulation of PtdIns4P 5-kinase C.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.