Evidence map›Paper›PMID 31128216›Full record

ReviewCancer letters2019

COMPASS Ascending: Emerging clues regarding the roles of MLL3/KMT2C and MLL2/KMT2D proteins in cancer.

Richard J Fagan, Andrew K Dingwall

Open access · greenAbstract readReview
In one paragraph

Review in Cancer letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
8.0field-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

105 citing papers in PubMed, 182 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Review
  8. Article
  9. Mapping of the hSOX10 protein interactome in human melanoma.bioRxiv : the preprint server for biology · 2025
    Article
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  16. Review
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  18. Article
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  20. Article

45 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

2 authors at 1 institution in 1 country.

Richard J FaganStritch School of Medicine, Loyola University Chicago, Maywood, IL, 60521, USA.
Andrew K DingwallStritch School of Medicine, Loyola University Chicago, Maywood, IL, 60521, USA; Department of Cancer Biology and Pathology & Laboratory Medicine, Stritch School of Medicine, Loyola University Chicago, Maywood, IL, 60521, USA. Electronic address: adingwall@luc.edu.
Loyola University Chicago · US

Funding

Basic and Clinical Research Training for Medical StudentsT35HL120835 · NHLBI · LOYOLA UNIVERSITY CHICAGO · PI ZELEZNIK-LE, NANCY J · 2015 to 2024
$628k
NHLBI NIH HHS T35 HL120835
6 · The paper itself

Abstract

The KMT2 (lysine methyltransferase) family of histone modifying proteins play essential roles in regulating developmental pathways, and mutations in the genes encoding these proteins have been strongly linked to many blood and solid tumor cancers. The KMT2A-D proteins are histone 3 lysine 4 (H3K4) methyltransferases embedded in large COMPASS-like complexes important for RNA Polymerase II-dependent transcription. KMT2 mutations were initially associated with pediatric Mixed Lineage Leukemias (MLL) and found to be the result of rearrangements of the MLL1/KMT2A gene at 11q23. Over the past several years, large-scale tumor DNA sequencing studies have revealed the potential involvement of other KMT2 family genes, including heterozygous somatic mutations in the paralogous MLL3/KMT2C and MLL2(4)/KMT2D genes that are now among the most frequently associated with human cancer. Recent studies have provided a better understanding of the potential roles of disrupted KMT2C and KMT2D family proteins in cell growth aberrancy. These findings, together with an examination of cancer genomics databases provide new insights into the contribution of KMT2C/D proteins in epigenetic gene regulation and links to carcinogenesis.

Indexed as

AnimalsDNA-Binding ProteinsEpigenesis, GeneticHistone-Lysine N-MethyltransferaseHumansMutationMyeloid-Lymphoid Leukemia ProteinNeoplasm ProteinsNeoplasmsDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseKMT2C protein, humanKMT2D protein, humanMyeloid-Lymphoid Leukemia ProteinNeoplasm ProteinsChromatinCo-occurrenceEpigeneticLysine methyltransferase

Identifiers

PMID31128216
PMCPMC6638576
OpenAlexW2946567852

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.