Evidence map›Paper›PMID 18072589›Full record

ArticleBioTechniques2007

Continuous enzymatic assay for histone lysine methyltransferases.

Philipp Rathert, Xiaodong Cheng, Albert Jeltsch

Abstract read
In one paragraph

Article in BioTechniques, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Small Molecule Inhibitors of Protein Arginine Methyltransferases.Expert opinion on investigational drugs · 2016
    Review
  8. Article
  9. Assay development for histone methyltransferases.Assay and drug development technologies · 2013
    Article
  10. Review
  11. Article
  12. Article
  13. Article
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

3 authors.

Philipp RathertJacobs University Bremen, Bremen, Germany.
Xiaodong Cheng
Albert Jeltsch

Funding

Histone Lysine Methylation: Structures and FunctionsR01GM068680 · NIGMS · EMORY UNIVERSITY · PI CHENG, XIAODONG · 2005 to 2012
$2.6M
NIGMS NIH HHS GM068680NIGMS NIH HHS R01 GM068680
6 · The paper itself

Abstract

We describe a continuous peptide methylation assay using the Neurospora crassa Dim-5 histone H3 lysine 9 (H3K9) methyltransferase as a model system. The assay uses streptavidin FlashPlates coated with target peptide. Since no washing and pipeting steps were required after the addition of the enzyme/S-adenosyl-L-methionine (AdoMet) mixture to the microplate, a continuous readout of the reaction progress was possible. We show that this assay is highly reproducible (with errors in the order of +/- 3%). The continuous assay is well suited for the simultaneous analysis of up to 384 samples, thus allowing for a rapid screening of methylation rates of different substrates under different conditions or in the presence of inhibitors.

Indexed as

Biological AssayHistone-Lysine N-MethyltransferaseKineticsMethylationNeurospora crassaPeptidesReproducibility of ResultsS-AdenosylmethionineHistone-Lysine N-MethyltransferasePeptidesS-Adenosylmethionine

Identifiers

PMID18072589
PMCPMC2703000

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.