Evidence map›Paper›PMID 34681795›Full record

ReviewInternational journal of molecular sciences2021

Conserved Structure and Evolution of DPF Domain of PHF10-The Specific Subunit of PBAF Chromatin Remodeling Complex.

Anton O Chugunov, Nadezhda A Potapova, Natalia S Klimenko, Victor V Tatarskiy, Sofia G Georgieva, Nataliya V Soshnikova

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. TheInternational journal of molecular sciences · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Special Issue: Structure, Function and Evolution of Protein Domains.International journal of molecular sciences · 2022
    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

6 authors at 4 institutions in 1 country.

Anton O ChugunovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya St., 117997 Moscow, Russia.ORCID 0000-0003-1331-3949
Nadezhda A PotapovaInstitute for Information Transmission Problems (Kharkevich Institute), Russian Academy of Sciences, 127051 Moscow, Russia.
Natalia S KlimenkoCenter for Precision Genome Editing and Genetic Technologies for Biomedicine, Institute of Gene Biology, Russian Academy of Sciences, 34/5 Vavilov St., 119334 Moscow, Russia.ORCID 0000-0001-9640-0102
Victor V TatarskiyInstitute of Gene Biology, Russian Academy of Sciences, 34/5 Vavilov St., 119334 Moscow, Russia.
Sofia G GeorgievaDepartment of Transcription Factors, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilov St., 119991 Moscow, Russia.
Nataliya V SoshnikovaInstitute of Gene Biology, Russian Academy of Sciences, 34/5 Vavilov St., 119334 Moscow, Russia.ORCID 0000-0001-9260-3068
Engelhardt Institute of Molecular Biology · RUInstitute of Gene Biology · RUInstitute for Information Transmission Problems · RUNational Research University Higher School of Economics · RU

Funding

Russian Science Foundation #21-14-00258
6 · The paper itself

Abstract

Transcription activation factors and multisubunit coactivator complexes get recruited at specific chromatin sites via protein domains that recognize histone modifications. Single PHDs (plant homeodomains) interact with differentially modified H3 histone tails. Double PHD finger (DPF) domains possess a unique structure different from PHD and are found in six proteins: histone acetyltransferases MOZ and MORF; chromatin remodeling complex BAF (DPF1-3); and chromatin remodeling complex PBAF (PHF10). Among them, PHF10 stands out due to the DPF sequence, structure, and functions. PHF10 is ubiquitously expressed in developing and adult organisms as four isoforms differing in structure (the presence or absence of DPF) and transcription regulation functions. Despite the importance of the DPF domain of PHF10 for transcription activation, its structure remains undetermined. We performed homology modeling of the human PHF10 DPF domain and determined common and distinct features in structure and histone modifications recognition capabilities, which can affect PBAF complex chromatin recruitment. We also traced the evolution of

Indexed as

Homeodomain ProteinsNeoplasm ProteinsAnimalsChromatin Assembly and DisassemblyConserved SequenceEvolution, MolecularGene DuplicationHistonesHumansPHD Zinc FingersProtein SubunitsTranscriptional ActivationHistonesHomeodomain ProteinsNeoplasm ProteinsPHF10 protein, humanProtein Subunitschromatin remodelingdomain evolutionDPF domainsduplicationgenes activationH3K14acPBAFPHDPHF10

Identifiers

PMID34681795
PMCPMC8538644
OpenAlexW3207756362

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.