Evidence map›Paper›PMID 26598646›Full record

ReviewMolecular & cellular proteomics : MCP2016

Histone H4 Lysine 20 (H4K20) Methylation, Expanding the Signaling Potential of the Proteome One Methyl Moiety at a Time.

Rick van Nuland, Or Gozani

Open access · hybridAbstract readReview
In one paragraph

Review in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 10% 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

45 citing papers in PubMed, 1 synthesis or guideline pooled it, 71 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Epigenetic alterations in Myeloid Malignancies.Advances in experimental medicine and biology · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Compromised Mitotic Fidelity in Human Pluripotent Stem Cells.International journal of molecular sciences · 2023
    Review
  15. Article
  16. Article
  17. Histone variant-specific post-translational modifications.Seminars in cell & developmental biology · 2023
    Review
  18. The X chromosome in C. elegans sex determination and dosage compensation.Current opinion in genetics & development · 2022
    Review
  19. Review
  20. An Improved Top-Down Mass Spectrometry Characterization ofJournal of the American Society for Mass Spectrometry · 2021
    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.

Rick van NulandFrom the Department of Biology, Stanford University, Stanford, California 94305.
Or GozaniFrom the Department of Biology, Stanford University, Stanford, California 94305 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
NIGMS NIH HHS R01 GM079641
6 · The paper itself

Abstract

Covalent post-translational modifications (PTMs) of proteins can regulate the structural and functional state of a protein in the absence of primary changes in the underlying sequence. Common PTMs include phosphorylation, acetylation, and methylation. Histone proteins are critical regulators of the genome and are subject to a highly abundant and diverse array of PTMs. To highlight the functional complexity added to the proteome by lysine methylation signaling, here we will focus on lysine methylation of histone proteins, an important modification in the regulation of chromatin and epigenetic processes. We review the signaling pathways and functions associated with a single residue, H4K20, as a model chromatin and clinically important mark that regulates biological processes ranging from the DNA damage response and DNA replication to gene expression and silencing.

Indexed as

AnimalsChromatinEpigenesis, GeneticHistonesHumansLysineMethylationProtein Processing, Post-TranslationalProteomeSignal TransductionChromatinHistonesLysineProteome

Identifiers

PMID26598646
PMCPMC4813698
OpenAlexW2303701162

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.