Evidence map›Paper›PMID 23756419›Full record

ArticleNature communications2013

Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation.

Carla Schmidt, Min Zhou, Hazel Marriott, Nina Morgner, Argyris Politis, Carol V Robinson

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
9.9field-weighted citation impact, top 1% 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

66 citing papers in PubMed, 141 citations in OpenAlex.

  1. Article
  2. Review
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  4. Review
  5. Review
  6. Review
  7. Article
  8. Crosslinking mass spectrometry: A link between structural biology and systems biology.Protein science : a publication of the Protein Society · 2021
    Review
  9. Review
  10. NaGenomics, proteomics & bioinformatics · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Capturing Biology in Flight.Journal of the American Society for Mass Spectrometry · 2019
    Article
  18. Article
  19. Review
  20. Review

6 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Carla SchmidtDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, UK.
Min Zhou
Hazel Marriott
Nina Morgner
Argyris Politis
Carol V Robinson
University of Oxford · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

F-type ATPases are highly conserved enzymes used primarily for the synthesis of ATP. Here we apply mass spectrometry to the F1FO-ATPase, isolated from spinach chloroplasts, and uncover multiple modifications in soluble and membrane subunits. Mass spectra of the intact ATPase define a stable lipid 'plug' in the FO complex and reveal the stoichiometry of nucleotide binding in the F1 head. Comparing complexes formed in solution from an untreated ATPase with one incubated with a phosphatase reveals that the dephosphorylated enzyme has reduced nucleotide occupancy and decreased stability. By contrasting chemical cross-linking of untreated and dephosphorylated forms we show that cross-links are retained between the head and base, but are significantly reduced in the head, stators and stalk. Conformational changes at the catalytic interface, evidenced by changes in cross-linking, provide a rationale for reduced nucleotide occupancy and highlight a role for phosphorylation in regulating nucleotide binding and stability of the chloroplast ATPase.

Indexed as

ChloroplastsCross-Linking ReagentsEnzyme StabilityMass SpectrometryNucleotidesPhosphorylationProtein BindingProtein ConformationProtein SubunitsProton-Translocating ATPasesSpinacia oleraceaCross-Linking ReagentsNucleotidesProtein SubunitsProton-Translocating ATPases

Identifiers

PMID23756419
PMCPMC3709506
OpenAlexW2007188470

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.