Bisubstrate analogues as structural tools to investigate m6A methyltransferase active sites
Published 2019 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Bisubstrate analogues as structural tools to investigate m6A methyltransferase active sites
Authors
Keywords
-
Journal
RNA Biology
Volume -, Issue -, Pages 1-11
Publisher
Informa UK Limited
Online
2019-03-17
DOI
10.1080/15476286.2019.1589360
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Synthesis of SAM-adenosine conjugates for the study of m6A-RNA methyltransferases.
- (2018) Colette Atdjian et al. EUROPEAN JOURNAL OF ORGANIC CHEMISTRY
- RNA-modifying proteins as anticancer drug targets
- (2018) P. Ann Boriack-Sjodin et al. NATURE REVIEWS DRUG DISCOVERY
- Structural Insights into N 6 -methyladenosine (m 6 A) Modification in the Transcriptome
- (2018) Jinbo Huang et al. GENOMICS PROTEOMICS & BIOINFORMATICS
- Structural Basis for Regulation of METTL16, an S-Adenosylmethionine Homeostasis Factor
- (2018) Katelyn A. Doxtader et al. MOLECULAR CELL
- Structural insights into the RNA methyltransferase domain of METTL16
- (2018) Agnieszka Ruszkowska et al. Scientific Reports
- MODOMICS: a database of RNA modification pathways. 2017 update
- (2017) Pietro Boccaletto et al. NUCLEIC ACIDS RESEARCH
- Recessive Mutations in TRMT10C Cause Defects in Mitochondrial RNA Processing and Multiple Respiratory Chain Deficiencies
- (2016) Metodi D. Metodiev et al. AMERICAN JOURNAL OF HUMAN GENETICS
- N6-Methylated Adenosine in RNA: From Bacteria to Humans
- (2016) Petr V. Sergiev et al. JOURNAL OF MOLECULAR BIOLOGY
- Structural Basis for Cooperative Function of Mettl3 and Mettl14 Methyltransferases
- (2016) Ping Wang et al. MOLECULAR CELL
- Structural basis of N6-adenosine methylation by the METTL3–METTL14 complex
- (2016) Xiang Wang et al. NATURE
- Dali server update
- (2016) Liisa Holm et al. NUCLEIC ACIDS RESEARCH
- Deficient methylation and formylation of mt-tRNAMet wobble cytosine in a patient carrying mutations in NSUN3
- (2016) Lindsey Van Haute et al. Nature Communications
- Structural insights into the molecular mechanism of the m6A writer complex
- (2016) Paweł Śledź et al. eLife
- Structural Chemistry of Human RNA Methyltransferases
- (2015) Matthieu Schapira ACS Chemical Biology
- Discovery of a Dual PRMT5–PRMT7 Inhibitor
- (2015) David Smil et al. ACS Medicinal Chemistry Letters
- Structural and functional insights into the molecular mechanism of rRNA m6A methyltransferase RlmJ
- (2013) Avinash S. Punekar et al. NUCLEIC ACIDS RESEARCH
- Towards automated crystallographic structure refinement withphenix.refine
- (2012) Pavel V. Afonine et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Genome-wide screen for Escherichia coli genes involved in repressing cell-to-cell transfer of non-conjugative plasmids
- (2012) Ayako Matsuda et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- The last rRNA methyltransferase of E. coli revealed: The yhiR gene encodes adenine-N6 methyltransferase specific for modification of A2030 of 23S ribosomal RNA
- (2012) A. Y. Golovina et al. RNA
- Overview of theCCP4 suite and current developments
- (2011) Martyn D. Winn et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Systematic errors in isothermal titration calorimetry: Concentrations and baselines
- (2011) Joel Tellinghuisen et al. ANALYTICAL BIOCHEMISTRY
- Selective Killing of Mixed Lineage Leukemia Cells by a Potent Small-Molecule DOT1L Inhibitor
- (2011) Scott R. Daigle et al. CANCER CELL
- The RNA modification database, RNAMDB: 2011 update
- (2010) W. A. Cantara et al. NUCLEIC ACIDS RESEARCH
- The YqfN protein of Bacillus subtilis is the tRNA: m 1 A22 methyltransferase (TrmK)
- (2008) Martine Roovers et al. NUCLEIC ACIDS RESEARCH
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