Evidence map›Paper›PMID 35733009›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Detection and Quantification of Histone Methyltransferase Activity In Vitro.

Nwamaka J Idigo, Philipp Voigt

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 41% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 1 citations in OpenAlex.

  1. Article
  2. Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Nwamaka J IdigoWellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh, UK.
Philipp VoigtEpigenetics Programme, Babraham Institute, Cambridge, UK. philipp.voigt@babraham.ac.uk.
Babraham Institute · GBWellcome Centre for Cell Biology · GB

Funding

Wellcome Trust 104175/Z/14/ZWellcome Trust 203149
6 · The paper itself

Abstract

Histone methyltransferases (HMTs) catalyze the methylation of lysine and arginine residues in histone as well as nonhistone substrates. In vitro histone methyltransferase assays have been instrumental in identifying HMTs, and they continue to be invaluable tools for the study of these important enzymes, revealing novel substrates and modes of regulation.Here we describe a universal protocol to examine HMT activity in vitro that can be adapted to a range of HMTs, substrates, and experimental objectives. We provide protocols for the detection of activity based on incorporation of

Indexed as

Histone-Lysine N-MethyltransferaseProtein Processing, Post-TranslationalHistone MethyltransferasesHistonesMethylationS-AdenosylmethionineHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesS-AdenosylmethionineChromatinHistone methylationHistone posttranslational modificationNucleosomesS-adenosylhomocysteineS-adenosylmethionineTranscription

Identifiers

PMID35733009
OpenAlexW4285166865

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.