Evidence map›Paper›PMID 20236312›Full record

ReviewThe FEBS journal2010

Mixed lineage leukemia: histone H3 lysine 4 methyltransferases from yeast to human.

Shivani Malik, Sukesh R Bhaumik

Open access · bronzeAbstract readReview
In one paragraph

Review in The FEBS journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Facilitates Chromatin Transcription in Breast and Other Cancers.Advances in experimental medicine and biology · 2024
    Review
  6. HOXA9 Regulome and Pharmacological Interventions in Leukemia.Advances in experimental medicine and biology · 2024
    Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. The role of BRD7 in embryo development and glucose metabolism.Journal of cellular and molecular medicine · 2016
    Article
  17. Article
  18. Article
  19. Review
  20. Histone modifications as regulators of life and death inMicrobial cell (Graz, Austria) · 2015
    Review
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.

Shivani MalikDepartment of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901, USA.
Sukesh R Bhaumik
Southern Illinois University School of Medicine · US

Funding

Ubiquitin-proteasome system regulation of a transcriptional co-activator, SAGA, and associated functionsR15GM088798 · NIGMS · SOUTHERN ILLINOIS UNIVERSITY CARBONDALE · PI BHAUMIK, SUKESH R. · 2009 to 2018
$997k
NIGMS NIH HHS 1R15GM088798-01NIGMS NIH HHS R15 GM088798
6 · The paper itself

Abstract

The fourth lysine of histone H3 is post-translationally modified by a methyl group via the action of histone methyltransferase, and such a covalent modification is associated with transcriptionally active and/or repressed chromatin states. Thus, histone H3 lysine 4 methylation has a crucial role in maintaining normal cellular functions. In fact, misregulation of this covalent modification has been implicated in various types of cancer and other diseases. Therefore, a large number of studies over recent years have been directed towards histone H3 lysine 4 methylation and the enzymes involved in this covalent modification in eukaryotes ranging from yeast to human. These studies revealed a set of histone H3 lysine 4 methyltransferases with important cellular functions in different eukaryotes, as discussed here.

Indexed as

Histone-Lysine N-MethyltransferaseEukaryotaHistonesHumansLysineMethylationProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsSpecies SpecificityHistone-Lysine N-MethyltransferaseHistonesLysineSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID20236312
PMCPMC2873088
OpenAlexW1633517437

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.