Evidence map›Paper›PMID 29312000›Full record

ReviewFrontiers in physiology2017

Proton-Translocating Nicotinamide Nucleotide Transhydrogenase: A Structural Perspective.

Qinghai Zhang, Pius S Padayatti, Josephine H Leung

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Changes in the brain [NADFrontiers in aging neuroscience · 2026
    Review
  4. LPS-DephosphorylatingMicroorganisms · 2024
    Article
  5. Review
  6. Reduced Nucleotides, Thiols and OAntioxidants (Basel, Switzerland) · 2022
    Review
  7. Article
  8. Ligand binding and conformational dynamics of theComputational and structural biotechnology journal · 2022
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Qinghai ZhangDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, United States.
Pius S PadayattiDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, United States.
Josephine H LeungDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, United States.
Scripps Research Institute · US

Funding

Transhydrogenase: Structure, Dynamics, and MechanismR01GM103838 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI ZHANG, QINGHAI · 2014 to 2017
$1.5M
NIGMS NIH HHS R01 GM103838
6 · The paper itself

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

Indexed as

hydride transferlipidic cubic phasemembrane proteinNADPHnucleotide bindingproton channeltranshydrogenaseX-ray crystallography

Identifiers

PMID29312000
PMCPMC5742237
OpenAlexW2776746901

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.