An engineered variant of SETD3 methyltransferase alters target specificity from histidine to lysine methylation
出版年份 2020 全文链接
标题
An engineered variant of SETD3 methyltransferase alters target specificity from histidine to lysine methylation
作者
关键词
-
出版物
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 295, Issue 9, Pages 2582-2589
出版商
American Society for Biochemistry & Molecular Biology (ASBMB)
发表日期
2020-01-08
DOI
10.1074/jbc.ra119.012319
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Post-translational modifications and chromatin dynamics
- (2019) Thomas O. Tolsma et al. Essays in Biochemistry
- KMT9 monomethylates histone H4 lysine 12 and controls proliferation of prostate cancer cells
- (2019) Eric Metzger et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Structural insights into SETD3-mediated histidine methylation on β-actin
- (2019) Qiong Guo et al. eLife
- Lysine methylation signaling of non-histone proteins in the nucleus
- (2019) Dan Levy CELLULAR AND MOLECULAR LIFE SCIENCES
- Introduction to the multi-author review on methylation in cellular physiology
- (2019) David Shechter CELLULAR AND MOLECULAR LIFE SCIENCES
- Enterovirus pathogenesis requires the host methyltransferase SETD3
- (2019) Jonathan Diep et al. Nature Microbiology
- Human HemK2/KMT9/N6AMT1 is an active protein methyltransferase, but does not act on DNA in vitro, in the presence of Trm112
- (2019) Clayton B. Woodcock et al. Cell Discovery
- Structural basis for the target specificity of actin histidine methyltransferase SETD3
- (2019) Shaobo Dai et al. Nature Communications
- SETD3 is an actin histidine methyltransferase that prevents primary dystocia
- (2018) Alex W. Wilkinson et al. NATURE
- SETD3 protein is the actin-specific histidine N-methyltransferase
- (2018) Sebastian Kwiatkowski et al. eLife
- Substrate Specificity of the HEMK2 Protein Glutamine Methyltransferase and Identification of Novel Substrates
- (2016) Denis Kusevic et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Methyltransferase-Glo: a universal, bioluminescent and homogenous assay for monitoring all classes of methyltransferases
- (2016) Kevin Hsiao et al. Epigenomics
- Nonhistone Lysine Methylation in the Regulation of Cancer Pathways
- (2016) Scott M. Carlson et al. Cold Spring Harbor Perspectives in Medicine
- Use of knowledge-based restraints inphenix.refineto improve macromolecular refinement at low resolution
- (2012) Jeffrey J. Headd et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- The SET8 H4K20 protein lysine methyltransferase has a long recognition sequence covering seven amino acid residues
- (2012) Srikanth Kudithipudi et al. BIOCHIMIE
- Specificity Analysis-Based Identification of New Methylation Targets of the SET7/9 Protein Lysine Methyltransferase
- (2011) Arunkumar Dhayalan et al. CHEMISTRY & BIOLOGY
- Structural basis of SETD6-mediated regulation of the NF-kB network via methyl-lysine signaling
- (2011) Yanqi Chang et al. NUCLEIC ACIDS RESEARCH
- Lysine methylation of the NF-κB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-κB signaling
- (2010) Dan Levy et al. NATURE IMMUNOLOGY
- Rubisco in complex with Rubisco large subunit methyltransferase
- (2009) S. Raunser et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Analysis of the Substrate Specificity of the Dim-5 Histone Lysine Methyltransferase Using Peptide Arrays
- (2008) Philipp Rathert et al. CHEMISTRY & BIOLOGY
- HemK2 protein, encoded on human chromosome 21, methylates translation termination factor eRF1
- (2008) Sabine Figaro et al. FEBS LETTERS
- Protein lysine methyltransferase G9a acts on non-histone targets
- (2008) Philipp Rathert et al. Nature Chemical Biology
Publish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn MoreAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started