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Structure and Function of p97 and Pex1/6 Type II AAA+ Complexes

Overview of attention for article published in Frontiers in Molecular Biosciences, May 2017
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Title
Structure and Function of p97 and Pex1/6 Type II AAA+ Complexes
Published in
Frontiers in Molecular Biosciences, May 2017
DOI 10.3389/fmolb.2017.00033
Pubmed ID
Authors

Paul Saffert, Cordula Enenkel, Petra Wendler

Abstract

Protein complexes of the Type II AAA+ (ATPases associated with diverse cellular activities) family are typically hexamers of 80-150 kDa protomers that harbor two AAA+ ATPase domains. They form double ring assemblies flanked by associated domains, which can be N-terminal, intercalated or C-terminal to the ATPase domains. Most prominent members of this family include NSF (N-ethyl-maleimide sensitive factor), p97/VCP (valosin-containing protein), the Pex1/Pex6 complex and Hsp104 in eukaryotes and ClpB in bacteria. Tremendous efforts have been undertaken to understand the conformational dynamics of protein remodeling type II AAA+ complexes. A uniform mode of action has not been derived from these works. This review focuses on p97/VCP and the Pex1/6 complex, which both structurally remodel ubiquitinated substrate proteins. P97/VCP plays a role in many processes, including ER- associated protein degradation, and the Pex1/Pex6 complex dislocates and recycles the transport receptor Pex5 from the peroxisomal membrane during peroxisomal protein import. We give an introduction into existing knowledge about the biochemical and cellular activities of the complexes before discussing structural information. We particularly emphasize recent electron microscopy structures of the two AAA+ complexes and summarize their structural differences.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 46 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 46 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 9 20%
Student > Master 7 15%
Student > Doctoral Student 6 13%
Student > Ph. D. Student 6 13%
Student > Bachelor 4 9%
Other 4 9%
Unknown 10 22%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 22 48%
Agricultural and Biological Sciences 5 11%
Medicine and Dentistry 3 7%
Chemistry 2 4%
Pharmacology, Toxicology and Pharmaceutical Science 1 2%
Other 2 4%
Unknown 11 24%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 2. 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 29 May 2017.
All research outputs
#14,061,899
of 22,968,808 outputs
Outputs from Frontiers in Molecular Biosciences
#1,039
of 3,838 outputs
Outputs of similar age
#169,227
of 314,090 outputs
Outputs of similar age from Frontiers in Molecular Biosciences
#10
of 26 outputs
Altmetric has tracked 22,968,808 research outputs across all sources so far. This one is in the 37th percentile – i.e., 37% of other outputs scored the same or lower than it.
So far Altmetric has tracked 3,838 research outputs from this source. They receive a mean Attention Score of 3.3. This one has gotten more attention than average, scoring higher than 70% 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 314,090 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 44th percentile – i.e., 44% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 26 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 50% of its contemporaries.