Evidence map›Paper›PMID 25489813›Full record

ArticleJournal of visualized experiments : JoVE2014

Specificity analysis of protein lysine methyltransferases using SPOT peptide arrays.

Srikanth Kudithipudi, Denis Kusevic, Sara Weirich, Albert Jeltsch

Open access · bronzeAbstract readVideo-Audio Media
In one paragraph

Article in Journal of visualized experiments : JoVE, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

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  16. Analysis of Histone Antibody Specificity with Peptide Microarrays.Journal of visualized experiments : JoVE · 2017
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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

4 authors at 1 institution in 1 country.

Srikanth KudithipudiInstitute of Biochemistry, Stuttgart University.
Denis KusevicInstitute of Biochemistry, Stuttgart University.
Sara WeirichInstitute of Biochemistry, Stuttgart University.
Albert JeltschInstitute of Biochemistry, Stuttgart University; albert.jeltsch@ibc.uni-stuttgart.de.
Institute of Biochemistry · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine methylation is an emerging post-translation modification and it has been identified on several histone and non-histone proteins, where it plays crucial roles in cell development and many diseases. Approximately 5,000 lysine methylation sites were identified on different proteins, which are set by few dozens of protein lysine methyltransferases. This suggests that each PKMT methylates multiple proteins, however till now only one or two substrates have been identified for several of these enzymes. To approach this problem, we have introduced peptide array based substrate specificity analyses of PKMTs. Peptide arrays are powerful tools to characterize the specificity of PKMTs because methylation of several substrates with different sequences can be tested on one array. We synthesized peptide arrays on cellulose membrane using an Intavis SPOT synthesizer and analyzed the specificity of various PKMTs. Based on the results, for several of these enzymes, novel substrates could be identified. For example, for NSD1 by employing peptide arrays, we showed that it methylates K44 of H4 instead of the reported H4K20 and in addition H1.5K168 is the highly preferred substrate over the previously known H3K36. Hence, peptide arrays are powerful tools to biochemically characterize the PKMTs.

Indexed as

Amino Acid SequenceHistone-Lysine N-MethyltransferaseHistonesLysineMethylationOligopeptidesProtein Array AnalysisSubstrate SpecificityHistone-Lysine N-MethyltransferaseHistonesLysineOligopeptides

Identifiers

PMID25489813
PMCPMC4354377
OpenAlexW1995553979

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.