O-GlcNAcylation of Co-Activator-Associated Arginine Methyltransferase 1 Regulates Its Protein Substrate Specificity

Biochemical Journal - United Kingdom
doi 10.1042/bj20141072
Full Text
Abstract

Available in full text

Date
Authors
Publisher

Portland Press Ltd.

Related search

Protein Arginine Methyltransferase 6 Regulates Embryonic Stem Cell Identity

Stem Cells and Development
Developmental BiologyHematologyCell Biology
2012English

Mechanistic Studies on Transcriptional Coactivator Protein Arginine Methyltransferase 1

Biochemistry
Biochemistry
2011English

Protein Arginine Methyltransferase 6 (PRMT6)

Science-Business eXchange
2014English

Substrate Specificity of the HEMK2 Protein Glutamine Methyltransferase and Identification of Novel Substrates

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2016English

O-GlcNAcylation of Core Components of the Translation Initiation Machinery Regulates Protein Synthesis

Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
2019English

The Predominant Protein-Arginine Methyltransferase fromSaccharomyces Cerevisiae

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
1996English

Chromatin Target of Protein Arginine Methyltransferase (CHTOP) Regulates Invasion, Chemoresistance, and Stemness in Epithelial Ovarian Cancer

Bioscience Reports
BiochemistryCell BiologyMolecular BiologyBiophysics
2019English

The Novel Human Protein ArginineN-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2001English

Signal-Dependent Control of Gluconeogenic Key Enzyme Genes Through Coactivator-Associated Arginine Methyltransferase 1

Journal of Biological Chemistry
BiochemistryCell BiologyMolecular Biology
2005English

Amanote Research

Note-taking for researchers

Follow Amanote

© 2024 Amaplex Software S.P.R.L. All rights reserved.

Privacy PolicyRefund Policy