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Proton-Translocating Nicotinamide Nucleotide Transhydrogenase: A Structural Perspective

Overview of attention for article published in Frontiers in Physiology, December 2017
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Title
Proton-Translocating Nicotinamide Nucleotide Transhydrogenase: A Structural Perspective
Published in
Frontiers in Physiology, December 2017
DOI 10.3389/fphys.2017.01089
Pubmed ID
Authors

Qinghai Zhang, Pius S. Padayatti, Josephine H. Leung

Abstract

Nicotinamide nucleotide transhydrogenase (TH) is an enzyme complex in animal mitochondria and bacteria that utilizes the electrochemical proton gradient across membranes to drive the production of NADPH. The enzyme plays an important role in maintaining the redox balance of cells with implications in aging and a number of human diseases. TH exists as a homodimer with each protomer containing a proton-translocating transmembrane domain and two soluble nucleotide binding domains that mediate hydride transfer between NAD(H) and NADP(H). The three-domain architecture of TH is conserved across species but polypeptide composition differs substantially. The complex domain coupling mechanism of TH is not fully understood despite extensive biochemical and structural characterizations. Herein the progress is reviewed, focusing mainly on structural findings from 3D crystallization of isolated soluble domains and more recently of the transmembrane domain and the holo-enzyme from Thermus thermophilus. A structural perspective and impeding challenges in further elucidating the mechanism of TH are discussed.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 25 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 25 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 9 36%
Student > Doctoral Student 2 8%
Student > Bachelor 2 8%
Student > Master 2 8%
Researcher 2 8%
Other 2 8%
Unknown 6 24%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 8 32%
Agricultural and Biological Sciences 2 8%
Immunology and Microbiology 2 8%
Chemistry 2 8%
Medicine and Dentistry 1 4%
Other 1 4%
Unknown 9 36%
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 28 December 2017.
All research outputs
#20,456,235
of 23,012,811 outputs
Outputs from Frontiers in Physiology
#9,480
of 13,770 outputs
Outputs of similar age
#376,076
of 440,404 outputs
Outputs of similar age from Frontiers in Physiology
#194
of 296 outputs
Altmetric has tracked 23,012,811 research outputs across all sources so far. This one is in the 1st percentile – i.e., 1% of other outputs scored the same or lower than it.
So far Altmetric has tracked 13,770 research outputs from this source. They typically receive more attention than average, with a mean Attention Score of 7.6. This one is in the 1st percentile – i.e., 1% of its peers scored the same or lower than it.
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We're also able to compare this research output to 296 others from the same source and published within six weeks on either side of this one. This one is in the 1st percentile – i.e., 1% of its contemporaries scored the same or lower than it.