Evidence map›Paper›PMID 33184251›Full record

ReviewJournal of biosciences2020

Evaluation of post-translational modifications in histone proteins: A review on histone modification defects in developmental and neurological disorders.

Shahin Ramazi, Abdollah Allahverdi, Javad Zahiri

Abstract readReview
PubMed
In one paragraph

Review in Journal of biosciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing 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

101 citing papers in PubMed.

  1. Epigenetic regulation of transgenes.Journal of biotechnology · 2026
    Review
  2. Review
  3. Article
  4. Review
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  7. Article
  8. Review
  9. Article
  10. Review
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  12. Review
  13. The role of epigenetic alterations in canine mammary cancer.The Journal of reproduction and development · 2026
    Review
  14. Regulation of histones in thromboinflammation.Frontiers in immunology · 2026
    Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. [Prediction of protein Kbhb sites based on learnable feature embedding].Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2025
    Article
  20. Article

41 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

3 authors.

Shahin RamaziDepartment of Biophysics, Faculty of Biological Sciences, Tarbiat Modares University, Jalal Ale Ahmad Highway, P.O. Box: 14115-111, Tehran, Iran.
Abdollah Allahverdi
Javad Zahiri

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modification (PTM) in histone proteins is a covalent modification which mainly consists of methylation, phosphorylation, acetylation, ubiquitylation, SUMOylation, glycosylation, and ADP-ribosylation. PTMs have fundamental roles in chromatin structure and function. Histone modifications have also been known as epigenetic markers. The PTMs that have taken place in histone proteins can affect gene expression by altering chromatin structure. Histone modifications act in varied biological processes such as transcriptional activation/inactivation, chromosome packaging, mitosis, meiosis, apoptosis, and DNA damage/repair. Defects in the PTMs pathway have been associated with the occurrence and progression of various human diseases, such as cancer, heart failure, autoimmune diseases, and neurodegenerative disorders such as Parkinson's disease, Alzheimer's disease, and Huntington's disease. Histone modifications are reversible and used as potential targets for cancer therapy and prevention. Recent different histone PTMs have key roles in cancer cells since it has been shown that histone PTMs markers in cancers are acetylation, methylation, phosphorylation, and ubiquitylation. In this review, we have summarized the six most studied histone modifications and have examined the role of these modifications in the development of cancer.

Indexed as

AcetylationDevelopmental DisabilitiesGlycosylationHistone CodeHistonesHumansNervous System DiseasesPhosphorylationProtein Processing, Post-TranslationalUbiquitinationHistones

Identifiers

PMID33184251

What OpenQuestion holds

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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.