Evidence map›Paper›PMID 25574024›Full record

ArticleScience (New York, N.Y.)2015

Structural biology. Division of labor in transhydrogenase by alternating proton translocation and hydride transfer.

Josephine H Leung, Lici A Schurig-Briccio, Mutsuo Yamaguchi, Arne Moeller, Jeffrey A Speir, Robert B Gennis, Charles D Stout

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

21 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Redox regulation of the immune response.Cellular & molecular immunology · 2022
    Review
  7. Ligand binding and conformational dynamics of theComputational and structural biotechnology journal · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Purification of AdultThe Journal of parasitology · 2019
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Josephine H LeungDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Lici A Schurig-BriccioDepartment of Biochemistry, University of Illinois, Urbana, IL 61801, USA.
Mutsuo YamaguchiDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Arne MoellerNational Resource for Automated Molecular Microscopy, The Scripps Research Institute, La Jolla, CA 92037, USA.
Jeffrey A SpeirNational Resource for Automated Molecular Microscopy, The Scripps Research Institute, La Jolla, CA 92037, USA.
Robert B GennisDepartment of Biochemistry, University of Illinois, Urbana, IL 61801, USA.
Charles D StoutDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. dave@scripps.edu.
Scripps Research Institute · USUniversity of Illinois Urbana-Champaign · US

Funding

JCSG Center:Innovative Membrane Protein Technology (RMI)P50GM073197 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI STEVENS, RAYMOND C · 2004 to 2013
$26.8M
TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
STRUCTURE, FUNCTION AND DYNAMICS OF TRANSHYDROGENASER01GM061545 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI STOUT, CHARLES DAVID · 2000 to 2007
$3.2M
Transhydrogenase: Structure, Dynamics, and MechanismR01GM103838 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI ZHANG, QINGHAI · 2014 to 2017
$1.5M
Using extreme thermophiles for the homologous expression of membrane proteinsR01GM095600 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI GENNIS, ROBERT B · 2010 to 2013
$1.1M
NIGMS NIH HHS 1R01GM103838-01A1NIGMS NIH HHS 5R01GM061545NIGMS NIH HHS GM073197NIGMS NIH HHS GM095600NIGMS NIH HHS P41 GM103310NIGMS NIH HHS P41GM103310NIGMS NIH HHS P50 GM073197NIGMS NIH HHS R01 GM061545NIGMS NIH HHS R01 GM095600NIGMS NIH HHS R01 GM103838
6 · The paper itself

Abstract

NADPH/NADP(+) (the reduced form of NADP(+)/nicotinamide adenine dinucleotide phosphate) homeostasis is critical for countering oxidative stress in cells. Nicotinamide nucleotide transhydrogenase (TH), a membrane enzyme present in both bacteria and mitochondria, couples the proton motive force to the generation of NADPH. We present the 2.8 Å crystal structure of the transmembrane proton channel domain of TH from Thermus thermophilus and the 6.9 Å crystal structure of the entire enzyme (holo-TH). The membrane domain crystallized as a symmetric dimer, with each protomer containing a putative proton channel. The holo-TH is a highly asymmetric dimer with the NADP(H)-binding domain (dIII) in two different orientations. This unusual arrangement suggests a catalytic mechanism in which the two copies of dIII alternatively function in proton translocation and hydride transfer.

Indexed as

ProtonsAmino Acid SequenceCrystallography, X-RayMolecular Sequence DataNADP TranshydrogenasesProtein MultimerizationProtein Structure, TertiaryThermus thermophilusNADP TranshydrogenasesProtons

Identifiers

PMID25574024
PMCPMC4479213
OpenAlexW2054607716

What OpenQuestion holds

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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.