Evidence map›Paper›PMID 29933573›Full record

ReviewProteomes2018

Proteomic Analysis of Histone Variants and Their PTMs: Strategies and Pitfalls.

Sara El Kennani, Marion Crespo, Jérôme Govin, Delphine Pflieger

Abstract readReview
In one paragraph

Review in Proteomes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Histone variant-specific post-translational modifications.Seminars in cell & developmental biology · 2023
    Review
  9. Review
  10. Epigenetic Modulation of Opioid Receptors by Drugs of Abuse.International journal of molecular sciences · 2022
    Review
  11. Article
  12. Chemical biology approaches to study histone interactors.Biochemical Society transactions · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Epigenetic memory in development and disease: Unraveling the mechanism.Biochimica et biophysica acta. Reviews on cancer · 2020
    Review
  19. Article
  20. 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

4 authors.

Sara El KennaniUniversity Grenoble Alpes, CEA, INSERM, BIG-BGE, 38000 Grenoble, France. sara.elkennani@cea.fr.
Marion CrespoUniversity Grenoble Alpes, CEA, INSERM, BIG-BGE, 38000 Grenoble, France. marion.crespo@cea.fr.
Jérôme GovinUniversity Grenoble Alpes, CEA, INSERM, BIG-BGE, 38000 Grenoble, France. jerome.govin@univ-grenoble-alpes.fr.
Delphine PfliegerUniversity Grenoble Alpes, CEA, INSERM, BIG-BGE, 38000 Grenoble, France. delphine.pflieger@cea.fr.ORCID 0000-0003-2122-3900

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epigenetic modifications contribute to the determination of cell fate and differentiation. The molecular mechanisms underlying histone variants and post-translational modifications (PTMs) have been studied in the contexts of development, differentiation, and disease. Antibody-based assays have classically been used to target PTMs, but these approaches fail to reveal combinatorial patterns of modifications. In addition, some histone variants are so similar to canonical histones that antibodies have difficulty distinguishing between these isoforms. Mass spectrometry (MS) has progressively developed as a powerful technology for the study of histone variants and their PTMs. Indeed, MS analyses highlighted exquisitely complex combinations of PTMs, suggesting “crosstalk” between them, and also revealed that PTM patterns are often variant-specific. Even though the sensitivity and acquisition speed of MS instruments have considerably increased alongside the development of computational tools for the study of multiple PTMs, it remains challenging to correctly describe the landscape of histone PTMs, and in particular to confidently assign modifications to specific amino acids. Here, we provide an inventory of MS-based strategies and of the pitfalls inherent to histone PTM and variant characterization, while stressing the complex interplay between PTMs and histone sequence variations. We will particularly illustrate the roles played by MS-based analyses in identifying and quantifying histone variants and modifications.

Indexed as

bottom-up analysiscomputational toolscrosstalkhistone variantsmass spectrometrypost-translational modifications

Identifiers

PMID29933573
PMCPMC6161106

What OpenQuestion holds

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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.