Evidence map›Paper›PMID 24561874›Full record

ReviewBiochimica et biophysica acta2014

An unexpected journey: lysine methylation across the proteome.

Kaitlyn E Moore, Or Gozani

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

53 citing papers in PubMed, 96 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Protein methylation in mitochondria.The Journal of biological chemistry · 2022
    Review
  9. Review
  10. Epigenetics alternation in lung fibrosis and lung cancer.Frontiers in cell and developmental biology · 2022
    Review
  11. New Insights into the Methylation ofPathogens (Basel, Switzerland) · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Kaitlyn E MooreDepartment of Biology, Stanford University, Stanford, CA 94305, USA; Department of Chemical and Systems Biology, School of Medicine, Stanford University, Stanford, CA 94305, USA.
Or GozaniDepartment of Biology, Stanford University, Stanford, CA 94305, USA. Electronic address: ogozani@stanford.edu.
Stanford University · US

Funding

Function of PHD Domain Proteins in Chromatin RegulationR01GM079641 · NIGMS · STANFORD UNIVERSITY · PI GOZANI, OR P. · 2007 to 2020
$4.5M
Mechanisms of action of the Smyd3 methyltransferase in cancer cellsR01CA172560 · NCI · STANFORD UNIVERSITY · PI GOZANI, OR P., SAGE, JULIEN · 2013 to 2017
$2.3M
NCI NIH HHS R01 CA172560NIGMS NIH HHS R01 GM079641
6 · The paper itself

Abstract

The dynamic modification of histone proteins by lysine methylation has emerged over the last decade as a key regulator of chromatin functions. In contrast, our understanding of the biological roles for lysine methylation of non-histone proteins has progressed more slowly. Though recently it has attracted less attention, ε-methyl-lysine in non-histone proteins was first observed over 50 years ago. In that time, it has become clear that, like the case for histones, non-histone methylation represents a key and common signaling process within the cell. Recent work suggests that non-histone methylation occurs on hundreds of proteins found in both the nucleus and the cytoplasm, and with important biomedical implications. Technological advances that allow us to identify lysine methylation on a proteomic scale are opening new avenues in the non-histone methylation field, which is poised for dramatic growth. Here, we review historical and recent findings in non-histone lysine methylation signaling, highlight new methods that are expanding opportunities in the field, and discuss outstanding questions and future challenges about the role of this fundamental post-translational modification (PTM).

Indexed as

Protein Processing, Post-TranslationalAnimalsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHumansLysineMethylationProteomeHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesLysineProteomeLysine methylationMethylation signalingNon-histone methylationPost-translational modificationProteome-wide

Identifiers

PMID24561874
PMCPMC4139483
OpenAlexW1981412571

What Socratic holds

Textmetadata
LicenceTDM
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.