Multiple pathways control protein kinase C phosphorylation
By D. Parekh, W. Ziegler, P. Parker. EMBO Journal, 2000
629 citations recorded by the source corpus.
Subfields: Molecular Biology, Pharmacology, Plant Science
View Paper: https://www.semanticscholar.org/paper/4775cd3d95bc7d62ec81a7cc9920855a158af31d
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Citations in the corpus
- Protein kinase C and other diacylglycerol effectors in cancer (2007, background): “The mechanisms involved in PKC activation have been extensively studie”
- Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling (2008, background): “In contrast, phosphorylations of all three sites in PKC are constitutive, whereas binding of second messengers, such as DAG and calcium, to regulatory domain provides the major signal input for PKC activation (Parekh et al, 2000; Newton, 2003).”
- Reactive Oxygen Species in Inflammation and Tissue Injury (2014, positive): “The atypical PKCs (f, k) are regulated by PS and are independent of DAG and Ca(2) + (250, 334).”
- Structural Basis of Protein Kinase C Isoform Function (2008, background): “The “priming” Ser/Thr phosphorylations that lock the enzyme in a closed, stabilized, catalytically-competent, phosphatase/ protease-resistant conformation have only recently become the focus of research interest (141, 153).”