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Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase

Overview of attention for article published in Nature Communications, December 2017
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Title
Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
Published in
Nature Communications, December 2017
DOI 10.1038/s41467-017-02253-1
Pubmed ID
Authors

Jeannette Abplanalp, Mario Leutert, Emilie Frugier, Kathrin Nowak, Roxane Feurer, Jiro Kato, Hans V. A. Kistemaker, Dmitri V. Filippov, Joel Moss, Amedeo Caflisch, Michael O. Hottiger

Abstract

ADP-ribosylation is a posttranslational modification that exists in monomeric and polymeric forms. Whereas the writers (e.g. ARTD1/PARP1) and erasers (e.g. PARG, ARH3) of poly-ADP-ribosylation (PARylation) are relatively well described, the enzymes involved in mono-ADP-ribosylation (MARylation) have been less well investigated. While erasers for the MARylation of glutamate/aspartate and arginine have been identified, the respective enzymes with specificity for serine were missing. Here we report that, in vitro, ARH3 specifically binds and demodifies proteins and peptides that are MARylated. Molecular modeling and site-directed mutagenesis of ARH3 revealed that numerous residues are critical for both the mono- and the poly-ADP-ribosylhydrolase activity of ARH3. Notably, a mass spectrometric approach showed that ARH3-deficient mouse embryonic fibroblasts are characterized by a specific increase in serine-ADP-ribosylation in vivo under untreated conditions as well as following hydrogen peroxide stress. Together, our results establish ARH3 as a serine mono-ADP-ribosylhydrolase and as an important regulator of the basal and stress-induced ADP-ribosylome.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 69 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 69 100%

Demographic breakdown

Readers by professional status Count As %
Student > Master 12 17%
Student > Ph. D. Student 11 16%
Student > Bachelor 10 14%
Researcher 7 10%
Student > Doctoral Student 3 4%
Other 7 10%
Unknown 19 28%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 26 38%
Agricultural and Biological Sciences 9 13%
Chemistry 7 10%
Immunology and Microbiology 2 3%
Medicine and Dentistry 2 3%
Other 4 6%
Unknown 19 28%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. 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 12 December 2017.
All research outputs
#17,922,331
of 23,011,300 outputs
Outputs from Nature Communications
#43,585
of 47,376 outputs
Outputs of similar age
#306,916
of 439,142 outputs
Outputs of similar age from Nature Communications
#1,313
of 1,436 outputs
Altmetric has tracked 23,011,300 research outputs across all sources so far. This one is in the 19th percentile – i.e., 19% of other outputs scored the same or lower than it.
So far Altmetric has tracked 47,376 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 55.9. This one is in the 6th percentile – i.e., 6% of its peers scored the same or lower than it.
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We're also able to compare this research output to 1,436 others from the same source and published within six weeks on either side of this one. This one is in the 6th percentile – i.e., 6% of its contemporaries scored the same or lower than it.