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The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines

Overview of attention for article published in Journal of Biomedical Science, May 2007
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Title
The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines
Published in
Journal of Biomedical Science, May 2007
DOI 10.1007/s11373-007-9178-y
Pubmed ID
Authors

Sue Lin-Chao, Ni-Ting Chiou, Gadi Schuster

Abstract

The structure and function of polynucleotide phosphorylase (PNPase) and the exosome, as well as their associated RNA-helicases proteins, are described in the light of recent studies. The picture raised is of an evolutionarily conserved RNA-degradation machine which exonucleolytically degrades RNA from 3' to 5'. In prokaryotes and in eukaryotic organelles, a trimeric complex of PNPase forms a circular doughnut-shaped structure, in which the phosphorolysis catalytic sites are buried inside the barrel-shaped complex, while the RNA binding domains create a pore where RNA enters, reminiscent of the protein degrading complex, the proteasome. In some archaea and in the eukaryotes, several different proteins form a similar circle-shaped complex, the exosome, that is responsible for 3' to 5' exonucleolytic degradation of RNA as part of the processing, quality control, and general RNA degradation process. Both PNPase in prokaryotes and the exosome in eukaryotes are found in association with protein complexes that notably include RNA helicase.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 70 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United Kingdom 1 1%
United States 1 1%
Poland 1 1%
France 1 1%
Unknown 66 94%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 17 24%
Researcher 14 20%
Student > Bachelor 6 9%
Professor > Associate Professor 6 9%
Student > Postgraduate 5 7%
Other 10 14%
Unknown 12 17%
Readers by discipline Count As %
Agricultural and Biological Sciences 37 53%
Biochemistry, Genetics and Molecular Biology 12 17%
Medicine and Dentistry 3 4%
Social Sciences 1 1%
Chemical Engineering 1 1%
Other 2 3%
Unknown 14 20%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 3. 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 07 February 2024.
All research outputs
#7,542,164
of 23,009,818 outputs
Outputs from Journal of Biomedical Science
#298
of 997 outputs
Outputs of similar age
#25,206
of 71,322 outputs
Outputs of similar age from Journal of Biomedical Science
#1
of 4 outputs
Altmetric has tracked 23,009,818 research outputs across all sources so far. This one is in the 44th percentile – i.e., 44% of other outputs scored the same or lower than it.
So far Altmetric has tracked 997 research outputs from this source. They typically receive more attention than average, with a mean Attention Score of 8.7. This one is in the 45th percentile – i.e., 45% of its peers scored the same or lower than it.
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 71,322 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 16th percentile – i.e., 16% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 4 others from the same source and published within six weeks on either side of this one. This one has scored higher than all of them