Evidence map›Paper›PMID 22024134›Full record

ArticleEpigenetics & chromatin2011

A proteomic approach for the identification of novel lysine methyltransferase substrates.

Dan Levy, Chih Long Liu, Ze Yang, Aaron M Newman, Ash A Alizadeh, Paul J Utz, Or Gozani

Open access · goldAbstract read
In one paragraph

Article in Epigenetics & chromatin, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

42 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
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  3. Review
  4. DynamicJournal of the American Chemical Society · 2025
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  10. Deletion of Mouse Setd4 Promotes the Recovery of Hematopoietic Failure.International journal of radiation oncology, biology, physics · 2020
    Article
  11. Article
  12. Review
  13. Lysine methylation signaling of non-histone proteins in the nucleus.Cellular and molecular life sciences : CMLS · 2019
    Review
  14. The methyltransferase SETD6 regulates Mitotic progression through PLK1 methylation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Article
  17. Review
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  19. Article
  20. Mechanisms of Nucleosome Dynamics In Vivo.Cold Spring Harbor perspectives in medicine · 2016
    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

7 authors at 1 institution in 1 country.

Dan Levy *Department of Biology, Stanford University, Stanford, CA 94305, USA.
Chih Long Liu *Department of Biology, Stanford University, Stanford, CA 94305, USA.
Ze YangDepartment of Biology, Stanford University, Stanford, CA 94305, USA.
Aaron M NewmanDivisions of Oncology, Department of Medicine, Stanford University, Stanford, CA 94305, USA.
Ash A AlizadehDivisions of Oncology, Department of Medicine, Stanford University, Stanford, CA 94305, USA.
Paul J UtzDivision of Immunology and Rheumatology, Stanford University, Stanford, CA 94305, USA.
Or GozaniDepartment of Biology, Stanford University, Stanford, CA 94305, USA.
Stanford University · US

Funding

Leveraging innovative technologies in basic and clinical cancer researchT32CA009302 · NCI · STANFORD UNIVERSITY · PI LAURA D ATTARDI, Aaron M Newman · 1985 to 2026
$19.1M
6 · The paper itself

Abstract

backgroundSignaling via protein lysine methylation has been proposed to play a central role in the regulation of many physiologic and pathologic programs. In contrast to other post-translational modifications such as phosphorylation, proteome-wide approaches to investigate lysine methylation networks do not exist.

resultsIn the current study, we used the ProtoArray® platform, containing over 9,500 human proteins, and developed and optimized a system for proteome-wide identification of novel methylation events catalyzed by the protein lysine methyltransferase (PKMT) SETD6. This enzyme had previously been shown to methylate the transcription factor RelA, but it was not known whether SETD6 had other substrates. By using two independent detection approaches, we identified novel candidate substrates for SETD6, and verified that all targets tested in vitro and in cells were genuine substrates.

conclusionsWe describe a novel proteome-wide methodology for the identification of new PKMT substrates. This technological advance may lead to a better understanding of the enzymatic activity and substrate specificity of the large number (more than 50) PKMTs present in the human proteome, most of which are uncharacterized.

Identifiers

PMID22024134
PMCPMC3212905
OpenAlexW2165479029

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.