Evidence map›Paper›PMID 10856248›Full record

ArticleThe EMBO journal2000

Two histone fold proteins, CHRAC-14 and CHRAC-16, are developmentally regulated subunits of chromatin accessibility complex (CHRAC).

D F Corona, A Eberharter, A Budde, R Deuring, S Ferrari, P Varga-Weisz, M Wilm, J Tamkun, P B Becker

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.3field-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

30 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
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  4. IMITATION SWITCH is required for normal chromatin structure and gene repression in PRC2 target domains.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  15. DNA polymerase epsilon: a polymerase of unusual size (and complexity).Progress in nucleic acid research and molecular biology · 2008
    Review
  16. Review
  17. ATP-dependent chromatin remodeling complexes in Drosophila.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2006
    Review
  18. Article
  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

9 authors at 1 institution in 1 country.

D F CoronaAdolf-Butenandt-Institut, Molekularbiologie, Schillerstrasse 44, 80336 München, Germany.
A Eberharter
A Budde
R Deuring
S Ferrari
P Varga-Weisz
M Wilm
J Tamkun
P B Becker
European Bioinformatics Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ISWI ATPase of Drosophila is a molecular engine that can drive a range of nucleosome remodelling reactions in vitro. ISWI is important for cell viability, developmental gene expression and chromosome structure. It interacts with other proteins to form several distinct nucleosome remodelling machines. The chromatin accessibility complex (CHRAC) is a biochemical entity containing ISWI in association with several other proteins. Here we report on the identification of the two smallest CHRAC subunits, CHRAC-14 and CHRAC-16. They contain histone fold domains most closely related to those found in sequence-specific transcription factors NF-YB and NF-YC, respectively. CHRAC-14 and CHRAC-16 interact directly with each other as well as with ISWI, and are associated with functionally active CHRAC. The developmental expression profiles of both subunits suggest specialized roles in chromatin remodelling reactions in the early embryo for both histone fold subunits.

Indexed as

CCAAT-Binding FactorDrosophila ProteinsAdenosine TriphosphatasesAmino Acid SequenceAnimalsChromatinDNA-Binding ProteinsDrosophilaGene Expression RegulationHistonesMolecular Sequence DataNucleoproteinsNucleosomesProtein BindingProtein ConformationProtein Structure, SecondaryAdenosine TriphosphatasesCCAAT-Binding FactorCHRAC-14 protein, DrosophilaCHRAC-16 protein, DrosophilaChromatinDNA-Binding ProteinsDrosophila ProteinsHistonesISWI proteinNucleoproteinsNucleosomesTranscription Factors

Identifiers

PMID10856248
PMCPMC203371
OpenAlexW2052652158

What OpenQuestion holds

Textmetadata
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.