ArticleProceedings of the National Academy of Sciences of the United States of America2016
Kinetic isotope effects reveal early transition state of protein lysine methyltransferase SET8.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Methanol-specific methyltransferase isozymes have large carbon kinetic isotope effects that impact methane isotopic signatures.Applied and environmental microbiology · 2026Article
- Probing the Human 4-Oxo-l-proline Reductase-Catalyzed Reaction by Deuterium Kinetic and Equilibrium Isotope Effects.Biochemistry · 2026Article
- Direct Competitive Kinetic Isotope Effect Measurement Using Quantitative Whole Molecule Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry.Chembiochem : a European journal of chemical biology · 2026Article
- Isotope Decluttering Reduces Spectral Complexity while Maintaining Protein Structure.Analytical chemistry · 2026Article
- Assembling Ternary Dead-End Complex for Covalent Trapping of Protein Lysine Methyltransferases.Journal of the American Chemical Society · 2026Article
- Structure, Function, and Activity of Small Molecule and Peptide Inhibitors of Protein Arginine Methyltransferase 1.Journal of medicinal chemistry · 2024Review
- Rational engineering of an elevator-type metal transporter ZIP8 reveals a conditional selectivity filter critically involved in determining substrate specificity.Communications biology · 2023Article
- Roles for the methyltransferase SETD8 in DNA damage repair.Clinical epigenetics · 2022Review
- Total synthesis of nahuoic acid AChemical science · 2021Article
- Trimethyllysine: From Carnitine Biosynthesis to Epigenetics.International journal of molecular sciences · 2020Review
- Fine-tuning of lysine side chain modulates the activity of histone lysine methyltransferases.Scientific reports · 2020Article
- Examining sterically demanding lysine analogs for histone lysine methyltransferase catalysis.Scientific reports · 2020Article
- A chemical probe of CARM1 alters epigenetic plasticity against breast cancer cell invasion.eLife · 2019Article
- Substrate-Differentiated Transition States of SET7/9-Catalyzed Lysine Methylation.Journal of the American Chemical Society · 2019Article
- Article
- Stuffed Methyltransferase Catalyzes the Penultimate Step of Pyochelin Biosynthesis.Biochemistry · 2019Article
- The transition to magic bullets - transition state analogue drug design.MedChemComm · 2018Review
- Crystallographic and Computational Characterization of Methyl Tetrel Bonding in S-Adenosylmethionine-Dependent Methyltransferases.Molecules (Basel, Switzerland) · 2018Article
- Chemical and Biochemical Perspectives of Protein Lysine Methylation.Chemical reviews · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Protein lysine methyltransferases (PKMTs) catalyze the methylation of protein substrates, and their dysregulation has been linked to many diseases, including cancer. Accumulated evidence suggests that the reaction path of PKMT-catalyzed methylation consists of the formation of a cofactor(cosubstrate)-PKMT-substrate complex, lysine deprotonation through dynamic water channels, and a nucleophilic substitution (S
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.