(PDF) Serine-195 Phosphorylation in the RNA-binding Protein

Serine-195 Phosphorylation in the RNA-binding Protein Rbm38 Increases P63 Expression by Modulating Rbm38’s Interaction With the Ago2–miR203 Complex

Journal of Biological Chemistry - United States

doi 10.1074/jbc.ra118.005779

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December 19, 2018

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American Society for Biochemistry & Molecular Biology (ASBMB)

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Serine-195 Phosphorylation in the RNA-binding Protein Rbm38 Increases P63 Expression by Modulating Rbm38’s Interaction With the Ago2–miR203 Complex

Journal of Biological Chemistry - United States

doi 10.1074/jbc.ra118.005779

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Disruption of the Rbm38-eIF4E Complex With a Synthetic Peptide Pep8 Increases P53 Expression

The RNA Binding Proteins RBM38 and DND1 Are Repressed in AML and Have a Novel Function in APL Differentiation

Interaction of the Histone mRNA Hairpin With Stem–Loop Binding Protein (SLBP) and Regulation of the SLBP–RNA Complex by Phosphorylation and Proline Isomerization

Diversity of RNA-Binding Proteins Modulating Post-Transcriptional Regulation of Protein Expression in the Maturing Mammalian Oocyte

Phosphorylation of Serine 282 in Cardiac Myosin Binding Protein-C Increases Myosin MgADP Release and MgATP Binding Rates in Mouse Myocardium

An RNA Mutation That Increases the Affinity of an RNA–protein Interaction

Phosphorylation at Serine 10, a Major Phosphorylation Site of P27Kip1, Increases Its Protein Stability

The RNA Binding Domain of Ribosomal Protein L11: Three-Dimensional Structure of the RNA-bound Form of the Protein and Its Interaction With 23 S rRNA

The Properties of the RNA-binding Protein NF90 Are Considerably Modulated by Complex Formation With NF45