Evidence map›Paper›PMID 18215768›Full record

ArticleChemistry & biology2008

Analysis of the substrate specificity of the Dim-5 histone lysine methyltransferase using peptide arrays.

Philipp Rathert, Xing Zhang, Christian Freund, Xiaodong Cheng, Albert Jeltsch

Open access · greenAbstract read
In one paragraph

Article in Chemistry & biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 72 citations in OpenAlex.

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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

5 authors at 3 institutions in 2 countries.

Philipp RathertBiochemistry Laboratory, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany.
Xing Zhang
Christian Freund
Xiaodong Cheng
Albert Jeltsch
Constructor University · DEEmory University · USLeibniz Institute for Neurobiology · DE

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

Histone methylation is an epigenetic mark essential for gene regulation and development. We introduce peptide SPOT synthesis to study sequence specificity of the Dim-5 histone-3 lysine-9 methyltransferase. Dim-5 recognizes R8-G12 of the H3 tail with T11 and G12 being the most important specificity determinants. Exchange of H3 tail residue S10 and T11 by E strongly reduced methylation by Dim-5, suggesting that phosphorylation of S10 or T11 may regulate the activity of Dim-5. In the Dim-5/peptide structure, E227 interacts with H3R8 and D209 with H3-S10. Mutations of E227 or D209 caused predictable changes in the substrate preference, illustrating that peptide recognition of histone methyltransferases can be altered by protein design. Comparative analyses of peptide arrays with wild-type and mutant enzymes, therefore, are well suited to investigate the target specificity of protein methyltransferases and study epigenetic crosstalk.

Indexed as

Amino Acid SequenceHistone-Lysine N-MethyltransferaseHistonesMethylationMolecular Sequence DataMutationNeurospora crassaPeptide LibraryPeptidesPhosphorylationProtein Array AnalysisSubstrate SpecificityHistone-Lysine N-MethyltransferaseHistonesPeptide LibraryPeptides

Identifiers

PMID18215768
PMCPMC2723807
OpenAlexW2055678358

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.