Evidence map›Paper›PMID 19808676›Full record

ArticleThe Journal of biological chemistry2009

The target of the NSD family of histone lysine methyltransferases depends on the nature of the substrate.

Yan Li, Patrick Trojer, Chong-Feng Xu, Peggie Cheung, Alex Kuo, William J Drury, Qi Qiao, Thomas A Neubert, Rui-Ming Xu, Or Gozani and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 169 papers.

0numbers the graph read from it
0cells of the map it votes in
169citing papers in PubMed
7.9field-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

169 citing papers in PubMed, 295 citations in OpenAlex.

  1. Review
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  9. Article
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  13. Article
  14. Intestinal NSD2 Aggravates Nonalcoholic Steatohepatitis Through Histone Modifications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. CircWHSC1 (CircNSD2): A Novel Circular RNA in Multiple Cancers.Clinical Medicine Insights. Oncology · 2024
    Review
  19. Review
  20. Article

109 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

11 authors at 5 institutions in 2 countries.

Yan LiHoward Hughes Medical Institute, New York University School of Medicine, New York, New York 10016, USA.
Patrick Trojer
Chong-Feng Xu
Peggie Cheung
Alex Kuo
William J Drury
Qi Qiao
Thomas A Neubert
Rui-Ming Xu
Or Gozani
Danny Reinberg
Howard Hughes Medical Institute · USStanford University · USChinese Academy of Sciences · CNNew York University · USSidney Kimmel Cancer Center · US

Funding

Vaccine FacilityP30CA016087 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ADRIANA HEGUY · 1985 to 2026
$83.1M
Protein Mass Spectrometry Core Facility for NeuroscienceP30NS050276 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI NEUBERT, THOMAS A · 2005 to 2015
$7.9M
Initiation of Transcription of Protein Coding GenesR37GM037120 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI REINBERG, DANNY · 2004 to 2013
$4.5M
STRUCTURE STUDIES OF TRANSCRIPTIONAL SILENCINGR01GM063716 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI XU, RUI-MING · 2001 to 2010
$2.9M
Q-TOF Mass SpectrometerS10RR017990 · NCRR · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI NEUBERT, THOMAS A · 2003 to 2003
$500k
Howard Hughes Medical InstituteNCI NIH HHS P30 CA016087NCI NIH HHS P30CA016087NCRR NIH HHS S10 RR017990NIGMS NIH HHS 4R37GM037120-24NIGMS NIH HHS GM063716NIGMS NIH HHS R01 GM063716NIGMS NIH HHS R37 GM037120NINDS NIH HHS P30 NS050276
6 · The paper itself

Abstract

The NSD (nuclear receptor SET domain-containing) family of histone lysine methyltransferases is a critical participant in chromatin integrity as evidenced by the number of human diseases associated with the aberrant expression of its family members. Yet, the specific targets of these enzymes are not clear, with marked discrepancies being reported in the literature. We demonstrate that NSD2 can exhibit disparate target preferences based on the nature of the substrate provided. The NSD2 complex purified from human cells and recombinant NSD2 both exhibit specific targeting of histone H3 lysine 36 (H3K36) when provided with nucleosome substrates, but histone H4 lysine 44 is the primary target in the case of octamer substrates, irrespective of the histones being native or recombinant. This disparity is negated when NSD2 is presented with octamer targets in conjunction with short single- or double-stranded DNA. Although the octamers cannot form nucleosomes, the target is nonetheless nucleosome-specific as is the product, dimethylated H3K36. This study clarifies in part the previous discrepancies reported with respect to NSD targets. We propose that DNA acts as an allosteric effector of NSD2 such that H3K36 becomes the preferred target.

Indexed as

AnimalsCell Line, TumorChromatinDNAGenetic VectorsHistone-Lysine N-MethyltransferaseHistonesHumansLysineMass SpectrometryNucleosomesProtein Processing, Post-TranslationalProtein Structure, TertiaryRecombinant ProteinsXenopus laevisChromatinDNAHistone-Lysine N-MethyltransferaseHistonesLysineNucleosomesRecombinant Proteins

Identifiers

PMID19808676
PMCPMC2797197
OpenAlexW2168327939

What OpenQuestion holds

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LicenceCC BY-NC
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.