Evidence map›Paper›PMID 20431927›Full record

ArticleThe protein journal2010

Characterization of the DOT1L network: implications of diverse roles for DOT1L.

Geunyeong Park, Zihua Gong, Junjie Chen, Ja-Eun Kim

Abstract read
PubMed Publisher
In one paragraph

Article in The protein journal, 2010. 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
1.5field-weighted citation impact, top 19% 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, 59 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. A novel role of DOT1L in kidney diseases.Molecular biology reports · 2023
    Review
  9. Connecting the DOTs on Cell Identity.Frontiers in cell and developmental biology · 2022
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Rewiring the Epigenetic Networks inFrontiers in cell and developmental biology · 2019
    Review
  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

4 authors at 2 institutions in 2 countries.

Geunyeong ParkDepartment of Pharmacology, School of Medicine, Kyung Hee University, 1 Hoegi-Dong, Dongdaemun-Gu, Seoul 130-701, Republic of Korea.
Zihua Gong
Junjie Chen
Ja-Eun Kim
Kyung Hee University · KRThe University of Texas MD Anderson Cancer Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methylation of lysine 79 on histone H3 (H3K79) is mediated by a methyltransferase called Dot1-like protein (DOT1L). DOT1L is involved in the regulation of telomeric silencing, development, cell cycle checkpoint and transcription. However, the mechanisms by which DOT1L controls these unrelated and diverse functions are unknown. To gain greater insight into DOT1L-mediated functions, we have purified a DOT1L-containing complex using tandem affinity purification. Mass spectrometry of the DOT1L-containing complex revealed that AF9, ENL and NPM1 were shown to be major DOT1L-interacting proteins. To construct a plausible DOT1L-interaction web, AF9-, ENL- and NPM1-containing complexes were also purified for mass spectrometry analysis. The data showed that DOT1L might control AF9- and ENL-mediated transcription, regulate RNA processing, and function as a histone chaperone in a NPM1-dependent manner. In addition, the purification of protein complexes identified a number of novel interacting partners associated with DOT1L, AF9, ENL and NPM1. These data define a unique DOT1L network and shed light on unknown functions of the DOT1L complex.

Indexed as

AnimalsBlotting, WesternCell LineDNA-Binding ProteinsHistonesHumansMethyltransferasesNuclear ProteinsNucleophosminProtein Interaction MappingRecombinant ProteinsTranscription FactorsTranscription, GeneticDNA-Binding ProteinsHistonesMethyltransferasesNPM1 protein, humanNuclear ProteinsNucleophosminRecombinant ProteinsTranscription Factors

Identifiers

PMID20431927
OpenAlexW2028500280

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.