Two novel methyltransferases acting upon eukaryotic elongation factor 1A in Saccharomyces cerevisiae
Author:
Funder
NIH
the National Center for Research Resources
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference34 articles.
1. Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase
2. The Function and Regulation of the JARID1 Family of Histone H3 Lysine 4 Demethylases: the Myc Connection
3. Structural origins for the product specificity of SET domain protein methyltransferases
4. The emerging field of dynamic lysine methylation of non-histone proteins
5. Specificity of protein lysine methyltransferases and methods for detection of lysine methylation of non-histone proteins
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1. Methylation of elongation factor 1A by yeast Efm4 or human eEF1A-KMT2 involves a beta-hairpin recognition motif and crosstalks with phosphorylation;Journal of Biological Chemistry;2024-02
2. Misregulation of cell cycle-dependent methylation of budding yeast CENP-A contributes to chromosomal instability;Molecular Biology of the Cell;2023-09-01
3. Profiling The Compendium Of Changes InSaccharomyces cerevisiaeDue To Mutations That Alter Availability Of The Main Methyl Donor S-Adenosylmethionine;2023-06-10
4. Human seven-β-strand (METTL) methyltransferases - conquering the universe of protein lysine methylation;Journal of Biological Chemistry;2023-06
5. The protein methylation network in yeast: A landmark in completeness for a eukaryotic post-translational modification;Proceedings of the National Academy of Sciences;2023-05-30
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