Evidence map›Paper›PMID 40372282›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2025

Intrinsically Disordered Regions Define Unique Protein Interaction Networks in CHD Family Remodelers.

Mehdi Sharifi Tabar, Chirag Parsania, Caroline Giardina, Yue Feng, Alex C H Wong, Cynthia Metierre, Rajini Nagarajah, Bijay P Dhungel, John E J Rasko, Charles G Bailey

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Human mutation · 2026
    Review
  5. 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

10 authors.

Mehdi Sharifi TabarFaculty of Medicine & Health, The University of Sydney, Camperdown, New South Wales, Australia.
Chirag ParsaniaFaculty of Medicine & Health, The University of Sydney, Camperdown, New South Wales, Australia.
Caroline GiardinaCancer & Gene Regulation Laboratory Centenary Institute, The University of Sydney, Camperdown, New South Wales, Australia.
Yue FengCancer & Gene Regulation Laboratory Centenary Institute, The University of Sydney, Camperdown, New South Wales, Australia.
Alex C H WongCancer & Gene Regulation Laboratory Centenary Institute, The University of Sydney, Camperdown, New South Wales, Australia.
Cynthia MetierreCancer & Gene Regulation Laboratory Centenary Institute, The University of Sydney, Camperdown, New South Wales, Australia.
Rajini NagarajahCancer & Gene Regulation Laboratory Centenary Institute, The University of Sydney, Camperdown, New South Wales, Australia.
Bijay P DhungelFaculty of Medicine & Health, The University of Sydney, Camperdown, New South Wales, Australia.
John E J RaskoCell & Molecular Therapies, Royal Prince Alfred Hospital, Camperdown, New South Wales, Australia.
Charles G BaileyFaculty of Medicine & Health, The University of Sydney, Camperdown, New South Wales, Australia.ORCID https://orcid.org/0000-0002-4725-7829

Funding

Federal Government | DHAC | National Health and Medical Research Council (NHMRC) #1128748Federal Government | DHAC | National Health and Medical Research Council (NHMRC) #1177305
6 · The paper itself

Abstract

Chromodomain helicase DNA-binding (CHD) enzymes play a pivotal role in genome regulation. They possess highly conserved ATPase domains flanked by poorly characterized and intrinsically disordered N- and C-termini. Using mass spectrometry, we identify dozens of novel protein-protein interactions (PPIs) within the N- and C-termini of human CHD family members. We also define a highly conserved aggregation-prone region (APR) within the C-terminus of CHD4 which is critical for its interaction with the nucleosome remodeling and deacetylase (NuRD), as well as ChAHP (CHD4, activity-dependent neuroprotective protein (ADNP), and HP1γ) complexes. Further analysis reveals a regulatory role for the CHD4 APR in gene transcription during erythrocyte formation. Our results highlight that the N- and C-termini of CHD chromatin remodelers shape protein interaction networks that drive unique transcriptional programs.

Indexed as

DNA-Binding ProteinsDNA HelicasesIntrinsically Disordered ProteinsProtein Interaction MapsChromatin Assembly and DisassemblyHumansMi-2 Nucleosome Remodeling and Deacetylase ComplexCHD4 protein, humanDNA-Binding ProteinsDNA HelicasesIntrinsically Disordered ProteinsMi-2 Nucleosome Remodeling and Deacetylase Complexaggregation‐prone regionschromatin remodelersDNA helicaseintrinsically disordered regionsprotein–protein interactionstranscription

Identifiers

PMID40372282
PMCPMC12080455

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.