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CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality

Overview of attention for article published in Nucleic Acids Research, August 2017
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About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • Good Attention Score compared to outputs of the same age (69th percentile)
  • Above-average Attention Score compared to outputs of the same age and source (63rd percentile)

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9 Mendeley
Title
CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality
Published in
Nucleic Acids Research, August 2017
DOI 10.1093/nar/gkx711
Pubmed ID
Authors

Hoffmeister, Helen, Fuchs, Andreas, Erdel, Fabian, Pinz, Sophia, Gröbner-Ferreira, Regina, Bruckmann, Astrid, Deutzmann, Rainer, Schwartz, Uwe, Maldonado, Rodrigo, Huber, Claudia, Dendorfer, Anne-Sarah, Rippe, Karsten, Längst, Gernot, Helen Hoffmeister, Andreas Fuchs, Fabian Erdel, Sophia Pinz, Regina Gröbner-Ferreira, Astrid Bruckmann, Rainer Deutzmann, Uwe Schwartz, Rodrigo Maldonado, Claudia Huber, Anne-Sarah Dendorfer, Karsten Rippe, Gernot Längst

Abstract

CHD3 and CHD4 (Chromodomain Helicase DNA binding protein), two highly similar representatives of the Mi-2 subfamily of SF2 helicases, are coexpressed in many cell lines and tissues and have been reported to act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). Besides CHD proteins, NuRD contains several repressors like HDAC1/2, MTA2/3 and MBD2/3, arguing for a role as a transcriptional repressor. However, the subunit composition varies among cell- and tissue types and physiological conditions. In particular, it is unclear if CHD3 and CHD4 coexist in the same NuRD complex or whether they form distinct NuRD complexes with specific functions. We mapped the CHD composition of NuRD complexes in mammalian cells and discovered that they are isoform-specific, containing either the monomeric CHD3 or CHD4 ATPase. Both types of complexes exhibit similar intranuclear mobility, interact with HP1 and rapidly accumulate at UV-induced DNA repair sites. But, CHD3 and CHD4 exhibit distinct nuclear localization patterns in unperturbed cells, revealing a subset of specific target genes. Furthermore, CHD3 and CHD4 differ in their nucleosome remodeling and positioning behaviour in vitro. The proteins form distinct CHD3- and CHD4-NuRD complexes that do not only repress, but can just as well activate gene transcription of overlapping and specific target genes.

Twitter Demographics

The data shown below were collected from the profiles of 8 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 9 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 9 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 3 33%
Student > Master 2 22%
Professor > Associate Professor 2 22%
Other 1 11%
Student > Doctoral Student 1 11%
Other 0 0%
Readers by discipline Count As %
Agricultural and Biological Sciences 4 44%
Biochemistry, Genetics and Molecular Biology 3 33%
Medicine and Dentistry 2 22%

Attention Score in Context

This research output has an Altmetric Attention Score of 4. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 19 November 2017.
All research outputs
#2,049,089
of 8,686,494 outputs
Outputs from Nucleic Acids Research
#2,973
of 11,308 outputs
Outputs of similar age
#71,256
of 236,435 outputs
Outputs of similar age from Nucleic Acids Research
#112
of 318 outputs
Altmetric has tracked 8,686,494 research outputs across all sources so far. Compared to these this one has done well and is in the 76th percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 11,308 research outputs from this source. They receive a mean Attention Score of 4.6. This one has gotten more attention than average, scoring higher than 73% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 236,435 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 69% of its contemporaries.
We're also able to compare this research output to 318 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 63% of its contemporaries.