Evidence map›Paper›PMID 39165358›Full record

ReviewFrontiers in immunology2024

The modification role and tumor association with a methyltransferase: KMT2C.

Yunjuan Jiao, Yuanhao Lv, Mingjie Liu, Yun Liu, Miaomiao Han, Xiwen Xiong, Hongyan Zhou, Jiateng Zhong, Xiaohong Kang, Wei Su

Abstract readReview
In one paragraph

Review in Frontiers in immunology, 2024. 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
–field-weighted citation impact
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.

  1. Article
  2. SLA2 is Associated With Immune evasion and Exhaustion of CD8Journal of cellular and molecular medicine · 2026
    Article
  3. Review
  4. Genome-Wide Analysis of Copy Number Variation in Vietnamese Local Chickens.Animals : an open access journal from MDPI · 2026
    Article
  5. Review
  6. Review
  7. Biomolecules · 2025
    Article
  8. Article
  9. Epigenetic regulation of cancer stemness.Signal transduction and targeted therapy · 2025
    Review
  10. Review
  11. 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

10 authors.

Yunjuan Jiao *Department of Pathology, The First Affiliated Hospital of Xinxiang Medical University, Xinxiang, China.
Yuanhao Lv *Department of Pathology, The First Affiliated Hospital of Xinxiang Medical University, Xinxiang, China.
Mingjie LiuDepartment of Pathology, The First Affiliated Hospital of Xinxiang Medical University, Xinxiang, China.
Yun LiuDepartment of Pathology, Xinxiang Medical University, Xinxiang, China.
Miaomiao HanDepartment of Pathology, Xinxiang Medical University, Xinxiang, China.
Xiwen XiongHenan Health Commission Key Laboratory of Gastrointestinal Cancer Prevention and Treatment, The First Affiliated Hospital of Xinxiang Medical University, Xinxiang, China.
Hongyan ZhouXinxiang Key Laboratory of Precision Diagnosis and Treatment for Colorectal Cancer, Xinxiang First People's Hospital, Xinxiang, China.
Jiateng ZhongDepartment of Pathology, The First Affiliated Hospital of Xinxiang Medical University, Xinxiang, China.
Xiaohong KangDepartment of Oncology, The First Affiliated Hospital of Xinxiang Medical University, Xinxiang, China.
Wei SuDepartment of Pathology, The First Affiliated Hospital of Xinxiang Medical University, Xinxiang, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone methylation can affect chromosome structure and binding to other proteins, depending on the type of amino acid being modified and the number of methyl groups added, this modification may promote transcription of genes (H3K4me2, H3K4me3, and H3K79me3) or reduce transcription of genes (H3K9me2, H3K9me3, H3K27me2, H3K27me3, and H4K20me3). In addition, advances in tumor immunotherapy have shown that histone methylation as a type of protein post-translational modification is also involved in the proliferation, activation and metabolic reprogramming of immune cells in the tumor microenvironment. These post-translational modifications of proteins play a crucial role in regulating immune escape from tumors and immunotherapy. Lysine methyltransferases are important components of the post-translational histone methylation modification pathway. Lysine methyltransferase 2C (KMT2C), also known as MLL3, is a member of the lysine methyltransferase family, which mediates the methylation modification of histone 3 lysine 4 (H3K4), participates in the methylation of many histone proteins, and regulates a number of signaling pathways such as EMT, p53, Myc, DNA damage repair and other pathways. Studies of KMT2C have found that it is aberrantly expressed in many diseases, mainly tumors and hematological disorders. It can also inhibit the onset and progression of these diseases. Therefore, KMT2C may serve as a promising target for tumor immunotherapy for certain diseases. Here, we provide an overview of the structure of KMT2C, disease mechanisms, and diseases associated with KMT2C, and discuss related challenges.

Indexed as

NeoplasmsAnimalsDNA-Binding ProteinsGene Expression Regulation, NeoplasticHistone-Lysine N-MethyltransferaseHistonesHumansMethylationNeoplasm ProteinsProtein Processing, Post-TranslationalTumor MicroenvironmentDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistonesKMT2C protein, humanNeoplasm Proteinsbiological processcancerhistone methylationimmunotherapyKMT2C

Identifiers

PMID39165358
PMCPMC11333232

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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.