Evidence map›Paper›PMID 35277331›Full record

ReviewSeminars in cell & developmental biology2023

Histone variant-specific post-translational modifications.

Faith M Joseph, Nicolas L Young

Open access · greenAbstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  13. Article
  14. Review
  15. Acetylation of Histone H3 in Cancer Progression and Prognosis.International journal of molecular sciences · 2024
    Review
  16. Review
  17. Article
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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 2 institutions in 2 countries.

Faith M JosephTranslational Biology and Molecular Medicine Graduate Program, USA.
Nicolas L YoungTranslational Biology and Molecular Medicine Graduate Program, USA; Verna & Marrs McLean Department of Biochemistry & Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA; Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA; Center for Precision Environmental Health, Baylor College of Medicine, Houston, TX 77030, USA. Electronic address: Nicolas.Young@bcm.edu.
Baylor College of Medicine · USCenter for Translational Molecular Medicine · NL

Funding

TMEM106b as a lysosomal adaptor to influence brain aging and tau pathogenesisP01AG066606 · NIA · BAYLOR COLLEGE OF MEDICINE · PI ZHENG, HUI · 2021 to 2025
$13.5M
Initiative for Maximizing Student Development (IMSD) ProgramR25GM056929 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI PEREIRA, FRED A · 1998 to 2023
$12.4M
METABOLIC REGULATION IN LEUKEMIA-INITIATING CELLSR01CA193235 · NCI · BAYLOR COLLEGE OF MEDICINE · PI NAKADA, DAISUKE · 2015 to 2024
$4.6M
Neutron encoded activity based probesR01GM139295 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI YOUNG, DAMIAN WINSTON, YOUNG, NICOLAS L · 2020 to 2024
$2.2M
NCI NIH HHS R01 CA193235NIA NIH HHS P01 AG066606NIGMS NIH HHS R01 GM139295NIGMS NIH HHS R25 GM056929
6 · The paper itself

Abstract

Post-translational modifications (PTMs) of histones play a key role in DNA-based processes and contribute to cell differentiation and gene function by adding an extra layer of regulation. Variations in histone sequences within each family of histones expands the chromatin repertoire and provide further mechanisms for regulation and signaling. While variants are known to be present in certain genomic loci and carry out important functions, much remains unknown about variant-specific PTMs and their role in regulating chromatin. This ambiguity is in part due to the limited technologies and appropriate reagents to identify and quantitate variant-specific PTMs. Nonetheless, histone variants are an integral portion of the chromatin system and the understanding of their modifications and resolving how PTMs function differently on specific variants is paramount to the advancement of the field. Here we review the current knowledge on post-translational modifications specific to histone variants, with an emphasis on well-characterized PTMs of known function. While not every possible PTM is addressed, we present key variant-specific PTMs and what is known about their function and mechanisms in convenient reference tables.

Indexed as

HistonesProtein Processing, Post-TranslationalChromatinDNAChromatinDNAHistonesChromatinEpigeneticsHistonesHistone VariantsPost-translational modificationsReplication-independent

Identifiers

PMID35277331
PMCPMC9458767
OpenAlexW4221006354

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.