Evidence map›Paper›PMID 33050946›Full record

ReviewClinical epigenetics2020

Clinicopathologic significance of protein lysine methyltransferases in cancer.

Theodore Vougiouklakis, Benjamin J Bernard, Nupur Nigam, Kyunghee Burkitt, Yusuke Nakamura, Vassiliki Saloura

Open access · goldAbstract readReview
In one paragraph

Review in Clinical epigenetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. SETDB1 Methylates MCT1 Promoting Tumor Progression by Enhancing the Lactate Shuttle.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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

6 authors at 3 institutions in 2 countries.

Theodore VougiouklakisDepartment of Pathology, New York University Langone Health, New York, USA.
Benjamin J BernardThoracic and GI Malignancies Branch, Center for Cancer Research, National Cancer Institute, 41 Medlars Drive, National Cancer Institute, Bethesda, MD, 20892, USA.
Nupur NigamThoracic and GI Malignancies Branch, Center for Cancer Research, National Cancer Institute, 41 Medlars Drive, National Cancer Institute, Bethesda, MD, 20892, USA.
Kyunghee BurkittThoracic and GI Malignancies Branch, Center for Cancer Research, National Cancer Institute, 41 Medlars Drive, National Cancer Institute, Bethesda, MD, 20892, USA.
Yusuke NakamuraCancer Precision Medicine Research Center, Japanese Foundation for Cancer Research, Koto, Japan.
Vassiliki SalouraThoracic and GI Malignancies Branch, Center for Cancer Research, National Cancer Institute, 41 Medlars Drive, National Cancer Institute, Bethesda, MD, 20892, USA. vassiliki.saloura@nih.gov.ORCID 0000-0002-9736-8578
National Cancer Institute · USJapanese Foundation For Cancer Research · JPNYU Langone Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein lysine methyltransferases (PKMTs) constitute a large family of approximately 50 chromatin modifiers that mono-, di- and/or tri-methylate lysine residues on histone and non-histone substrates. With the advent of The Cancer Genome Atlas, it became apparent that this family of chromatin modifiers harbors frequent genetic and expression alterations in multiple types of cancer. In this regard, past and ongoing preclinical studies have provided insight into the mechanisms of action of some of these enzymes, laying the ground for the ongoing development of PKMT inhibitors as novel anticancer therapeutics. The purpose of this review is to summarize existing data obtained by different research groups through immunohistochemical analysis of the protein expression levels of PKMTs, and their respective clinicopathologic associations. We focused on studies that used immunohistochemistry to associate protein expression levels of specific PKMTs, as well as several established histone methylation marks, with clinicopathologic features and survival outcomes in various cancer types. We also review ongoing clinical trials of PKMT inhibitors in cancer treatment. This review underscores the clinical relevance and potential of targeting the family of PKMT enzymes as the next generation of cancer therapy.

Indexed as

AdolescentAdultClinical Trials as TopicDNA MethylationEnhancer of Zeste Homolog 2 ProteinEpigenomicsFemaleHistone-Lysine N-MethyltransferaseHistonesHumansImmunohistochemistryLysineNeoplasmsNeoplasm StagingSurvival AnalysisYoung AdultEnhancer of Zeste Homolog 2 ProteinEZH2 protein, humanHistone-Lysine N-MethyltransferaseHistonesLysineClinicopathologic associationsImmunohistochemistryProtein lysine methyltransferases

Identifiers

PMID33050946
PMCPMC7557092
OpenAlexW3092540352

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.