Evidence map›Paper›PMID 32824860›Full record

ReviewInternational journal of molecular sciences2020

Histone H1 Post-Translational Modifications: Update and Future Perspectives.

Marta Andrés, Daniel García-Gomis, Inma Ponte, Pedro Suau, Alicia Roque

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Nuclear destabilisation - a possible genesis of cancer?Biological reviews of the Cambridge Philosophical Society · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Histone Phosphorylation in DNA Damage Response.International journal of molecular sciences · 2025
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. A DNA condensation code for linker histones.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Review
  20. Chemical proteomics approaches for protein post-translational modification studies.Biochimica et biophysica acta. Proteins and proteomics · 2024
    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

5 authors at 1 institution in 1 country.

Marta AndrésBiochemistry and Molecular Biology Department, Biosciences Faculty, Autonomous University of Barcelona, 08193 Cerdanyola del Vallès, Spain.
Daniel García-GomisBiochemistry and Molecular Biology Department, Biosciences Faculty, Autonomous University of Barcelona, 08193 Cerdanyola del Vallès, Spain.
Inma PonteBiochemistry and Molecular Biology Department, Biosciences Faculty, Autonomous University of Barcelona, 08193 Cerdanyola del Vallès, Spain.
Pedro SuauBiochemistry and Molecular Biology Department, Biosciences Faculty, Autonomous University of Barcelona, 08193 Cerdanyola del Vallès, Spain.
Alicia RoqueBiochemistry and Molecular Biology Department, Biosciences Faculty, Autonomous University of Barcelona, 08193 Cerdanyola del Vallès, Spain.ORCID 0000-0002-6206-6481
Universitat Autònoma de Barcelona · ES

Funding

Ministerio de Economía, Industria y Competitividad, Gobierno de España BFU2017-82805-C2-2-P
6 · The paper itself

Abstract

Histone H1 is the most variable histone and its role at the epigenetic level is less characterized than that of core histones. In vertebrates, H1 is a multigene family, which can encode up to 11 subtypes. The H1 subtype composition is different among cell types during the cell cycle and differentiation. Mass spectrometry-based proteomics has added a new layer of complexity with the identification of a large number of post-translational modifications (PTMs) in H1. In this review, we summarize histone H1 PTMs from lower eukaryotes to humans, with a particular focus on mammalian PTMs. Special emphasis is made on PTMs, whose molecular function has been described. Post-translational modifications in H1 have been associated with the regulation of chromatin structure during the cell cycle as well as transcriptional activation, DNA damage response, and cellular differentiation. Additionally, PTMs in histone H1 that have been linked to diseases such as cancer, autoimmune disorders, and viral infection are examined. Future perspectives and challenges in the profiling of histone H1 PTMs are also discussed.

Indexed as

Histone CodeProtein Processing, Post-TranslationalAnimalsChromatin Assembly and DisassemblyHistonesHumansHistonesacetylationchromatin structurecitrullinationdiseasehistone H1mass spectrometrymethylationphosphorylationPTM functionubiquitylation

Identifiers

PMID32824860
PMCPMC7460583
OpenAlexW3078006487

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.