Evidence map›Paper›PMID 25384982›Full record

ArticleThe Journal of biological chemistry2015

Human CHD2 is a chromatin assembly ATPase regulated by its chromo- and DNA-binding domains.

Jessica C Liu, Catarina G Ferreira, Timur Yusufzai

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

28 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Adult Phenotype ofNeurology. Genetics · 2024
    Article
  6. Neurodevelopmental Disorder Caused by Deletion ofThe New England journal of medicine · 2024
    Article
  7. Article
  8. Review
  9. Novel syndromic neurodevelopmental disorder caused bymedRxiv : the preprint server for health sciences · 2024
    Article
  10. Clinical analysis ofPediatric investigation · 2022
    Article
  11. Article
  12. Clinical Study of 8 Cases ofFrontiers in cell and developmental biology · 2022
    Article
  13. Review
  14. Article
  15. CHD2-Related CNS Pathologies.International journal of molecular sciences · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

3 authors at 1 institution in 1 country.

Jessica C LiuFrom the Department of Radiation Oncology, Dana-Farber Cancer Institute and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02215 and Graduate Program: Molecules, Cells, and Organisms, Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138.
Catarina G FerreiraFrom the Department of Radiation Oncology, Dana-Farber Cancer Institute and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02215 and.
Timur YusufzaiFrom the Department of Radiation Oncology, Dana-Farber Cancer Institute and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02215 and timur_yusufzai@dfci.harvard.edu.
Harvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chromodomain helicase DNA-binding protein 2 (CHD2) is an ATPase and a member of the SNF2-like family of helicase-related enzymes. Although deletions of CHD2 have been linked to developmental defects in mice and epileptic disorders in humans, little is known about its biochemical and cellular activities. In this study, we investigate the ATP-dependent activity of CHD2 and show that CHD2 catalyzes the assembly of chromatin into periodic arrays. We also show that the N-terminal region of CHD2, which contains tandem chromodomains, serves an auto-inhibitory role in both the DNA-binding and ATPase activities of CHD2. While loss of the N-terminal region leads to enhanced chromatin-stimulated ATPase activity, the N-terminal region is required for ATP-dependent chromatin remodeling by CHD2. In contrast, the C-terminal region, which contains a putative DNA-binding domain, selectively senses double-stranded DNA of at least 40 base pairs in length and enhances the ATPase and chromatin remodeling activities of CHD2. Our study shows that the accessory domains of CHD2 play central roles in both regulating the ATPase domain and conferring selectivity to chromatin substrates.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAnimalsBaculoviridaeBinding SitesChromatinChromatin Assembly and DisassemblyDNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsHistonesHumansMolecular Sequence DataProtein BindingProtein Interaction Domains and MotifsRecombinant ProteinsAdenosine TriphosphatasesCHD2 protein, humanChromatinDNA-Binding ProteinsDrosophila ProteinsHistonesRecombinant ProteinsATPaseCHD2Chromatin RemodelingChromodomainsDNA-binding ProteinEpilepsyNucleosome

Identifiers

PMID25384982
PMCPMC4281729
OpenAlexW2123883282

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.