Evidence map›Paper›PMID 27234562›Full record

ReviewMutation research. Reviews in mutation research

The many faces of histone H3K79 methylation.

Zeenat Farooq, Shahid Banday, Tej K Pandita, Mohammad Altaf

Abstract readReview
In one paragraph

Review in Mutation research. Reviews in mutation research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
8.7field-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

90 citing papers in PubMed, 167 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Development of Dimethylsulfonium Probes for Broad Profiling of Methyllysine Reader Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  8. Review
  9. Epigenetic alterations in Myeloid Malignancies.Advances in experimental medicine and biology · 2026
    Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Interrogating the regulatory epigenome of cellular senescence.Cellular and molecular life sciences : CMLS · 2025
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

30 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Zeenat FarooqChromatin and Epigenetics Lab, Department of Biotechnology, University of Kashmir, Srinagar, Jammu, Kashmir 190006, India.
Shahid BandayChromatin and Epigenetics Lab, Department of Biotechnology, University of Kashmir, Srinagar, Jammu, Kashmir 190006, India.
Tej K PanditaDepartment of Radiation Oncology, Houston Methodist Research Institute, Houston, TX 77030, USA.
Mohammad AltafChromatin and Epigenetics Lab, Department of Biotechnology, University of Kashmir, Srinagar, Jammu, Kashmir 190006, India. Electronic address: altafbhat@uok.edu.in.
University of Kashmir · INHouston Methodist · US

Funding

CHROMATIN MODIFYING FACTORS CONTROL RADIATION RESPONSE AND GENOMIC STABILITYR01CA129537 · NCI · WASHINGTON UNIVERSITY · PI PANDITA, TEJ K · 2008 to 2018
$3.3M
Tumor-cell-specific targets for combined hyperthermia and radiation effectsR01CA154320 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI PANDITA, TEJ K · 2010 to 2014
$1.6M
NCI NIH HHS R01 CA129537NCI NIH HHS R01 CA154320
6 · The paper itself

Abstract

Dot1/DOT1L (disruptor of telomeric silencing-1) is an evolutionarily conserved histone methyltransferase that methylates lysine 79 located within the globular domain of histone H3. Dot1 was initially identified by a genetic screen as a disruptor of telomeric silencing in Saccharomyces cerevisiae; further, it is the only known non-SET domain containing histone methyltransferase. Methylation of H3K79 is involved in the regulation of telomeric silencing, cellular development, cell-cycle checkpoint, DNA repair, and regulation of transcription. hDot1L-mediated H3K79 methylation appears to have a crucial role in transformation as well as disease progression in leukemias involving several oncogenic fusion proteins. This review summarizes the multiple functions of Dot1/hDOT1L in a range of cellular processes.

Indexed as

AnimalsCell CycleCell Transformation, NeoplasticDisease SusceptibilityDNA RepairEpigenesis, GeneticGene Expression RegulationGene SilencingHistonesHumansMethylationTelomereHistonesChromatinDNA repairHistone methylation

Identifiers

PMID27234562
PMCPMC4889126
OpenAlexW2330169170

What OpenQuestion 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 OpenQuestion graph.