Evidence map›Paper›PMID 31123776›Full record

ReviewCellular and molecular life sciences : CMLS2019

Lysine methylation signaling of non-histone proteins in the nucleus.

Dan Levy

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2019. 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
2.7field-weighted citation impact, top 9% 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, 56 citations in OpenAlex.

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  16. Mechanisms of Interaction between Enhancers and Promoters in ThreeInternational journal of molecular sciences · 2023
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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

1 author at 1 institution in 1 country.

Dan LevyThe Shraga Segal Department of Microbiology, Immunology and Genetics, Ben-Gurion University of the Negev, 84105, Beersheba, Israel. ledan@post.bgu.ac.il.
Ben-Gurion University of the Negev · IL

Funding

Marie Curie Career Integration Grant 333242The Israel Cancer Association 20180022The Israel Science Foundation 262/18The Israel Science Foundation 285/14The Research Career Development Award from the Israel Cancer Research Fund 13-704
6 · The paper itself

Abstract

Lysine methylation, catalyzed by protein lysine methyltransferases (PKMTs), is a central post-translational modification regulating many signaling pathways. It has direct and indirect effects on chromatin structure and transcription. Accumulating evidence suggests that dysregulation of PKMT activity has a fundamental impact on the development of many pathologies. While most of these works involve in-depth analysis of methylation events in the context of histones, in recent years, it has become evident that methylation of non-histone proteins also plays a pivotal role in cell processes. This review highlights the importance of non-histone methylation, with focus on methylation events taking place in the nucleus. Known experimental platforms which were developed to identify new methylation events, as well as examples of specific lysine methylation signaling events which regulate key transcription factors, are presented. In addition, the role of these methylation events in normal and disease states is emphasized.

Indexed as

Cell NucleusHistone-Lysine N-MethyltransferaseHumansLysineMethylationProtein Array AnalysisSignal TransductionTranscription FactorsHistone-Lysine N-MethyltransferaseLysineTranscription FactorsLysine methylationMethylation signalingNon-histone methylationPost-translational modifications (PTMs)Protein lysine methyltransferases (PKMTs)

Identifiers

PMID31123776
PMCPMC11105312
OpenAlexW2945582389

What Socratic 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 Socratic graph.