Evidence map›Paper›PMID 27871933›Full record

ReviewJournal of molecular biology2017

A Molecular Prospective for HIRA Complex Assembly and H3.3-Specific Histone Chaperone Function.

M Daniel Ricketts, Ronen Marmorstein

Abstract readReview
In one paragraph

Review in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  6. HIRA and dPCIF1 coordinately establish totipotent chromatin and control orderly ZGA inProceedings of the National Academy of Sciences of the United States of America · 2024
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  8. Review
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  12. Review
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  16. Review
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  19. Molecular basis for chromatin assembly and modification by multiprotein complexes.Protein science : a publication of the Protein Society · 2019
    Review
  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

2 authors at 1 institution in 1 country.

M Daniel RickettsDepartment of Biochemistry and Biophysics, Graduate Group in Biochemistry and Molecular Biophysics, Abramson Family Cancer Research Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104, USA.
Ronen MarmorsteinDepartment of Biochemistry and Biophysics, Graduate Group in Biochemistry and Molecular Biophysics, Abramson Family Cancer Research Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104, USA; Epigenetics Program, University of Pennsylvania, Philadelphia, PA 19104, USA. Electronic address: marmor@mail.med.upenn.edu.
Cancer Research Institute · US

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
STRUCTURAL BASIS FOR EPIGENETICS IN AGING AND LONGEVITYP01AG031862 · NIA · WISTAR INSTITUTE · PI ADAMS, PETER D. · 2008 to 2022
$28.3M
Molecular Mechanisms, Pathways and Inhibition of Acetyl-Transfer ReactionsR35GM118090 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Ronen Marmorstein · 2016 to 2026
$6.7M
Structure/Function of Histone AcetyltransferasesR01GM060293 · NIGMS · WISTAR INSTITUTE · PI MARMORSTEIN, RONEN · 2000 to 2016
$5.3M
NCI NIH HHS P30 CA010815NIA NIH HHS P01 AG031862NIGMS NIH HHS R01 GM060293NIGMS NIH HHS R35 GM118090
6 · The paper itself

Abstract

Incorporation of variant histone sequences, in addition to post-translational modification of histones, serves to modulate the chromatin environment. Different histone chaperone proteins mediate the storage and chromatin deposition of variant histones. Although the two non-centromeric histone H3 variants, H3.1 and H3.3, differ by only 5 aa, replacement of histone H3.1 with H3.3 can modulate the transcription for highly expressed and developmentally required genes, lead to the formation of repressive heterochromatin, or aid in DNA and chromatin repair. The human histone cell cycle regulator (HIRA) complex composed of HIRA, ubinuclein-1, CABIN1, and transiently anti-silencing function 1, forms one of the two complexes that bind and deposit H3.3/H4 into chromatin. A number of recent biochemical and structural studies have revealed important details underlying how these proteins assemble and function together as a multiprotein H3.3-specific histone chaperone complex. Here, we present a review of existing data and present a new model for the assembly of the HIRA complex and for the HIRA-mediated incorporation of H3.3/H4 into chromatin.

Indexed as

Protein MultimerizationAdaptor Proteins, Signal TransducingCell Cycle ProteinsChromatinDNA RepairGene Expression RegulationHistone ChaperonesHistonesHumansMolecular ChaperonesNuclear ProteinsTranscription FactorsTranscription, GeneticAdaptor Proteins, Signal TransducingASF1A protein, humanASF1B protein, humanCABIN1 protein, humanCell Cycle ProteinsChromatinHIRA protein, humanHistone ChaperonesHistonesMolecular ChaperonesNuclear ProteinsTranscription FactorsUBN1 protein, humanCABIN1HIRAhistone chaperoneshistone H3.3UBN1

Identifiers

PMID27871933
PMCPMC5438300
OpenAlexW2550027409

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.