Evidence map›Paper›PMID 19266309›Full record

ArticlePhotosynthesis research

Atomic force microscopy of the bacterial photosynthetic apparatus: plain pictures of an elaborate machinery.

Simon Scheuring, James N Sturgis

Abstract read
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In one paragraph

Article in Photosynthesis research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
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  6. Review
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  11. Optimal fold symmetry of LH2 rings on a photosynthetic membrane.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  12. Article
  13. Review
  14. Article
  15. Forces guiding assembly of light-harvesting complex 2 in native membranes.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  16. Article
  17. Förster energy transfer theory as reflected in the structures of photosynthetic light-harvesting systems.Chemphyschem : a European journal of chemical physics and physical chemistry · 2011
    Review
  18. Review
  19. Review
  20. Article
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

2 authors at 2 institutions in 1 country.

Simon ScheuringInstitut Curie, UMR168-CNRS, 26 Rue d’Ulm, 75248 Paris, France. simon.scheuring@curie.fr
James N Sturgis
Institut Curie · FRLaboratoire de Mécanique et d’Acoustique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosynthesis both in the past and present provides the vast majority of the energy used on the planet. The purple photosynthetic bacteria are a group of organisms that are able to perform photosynthesis using a particularly simple system that has been much studied. The main molecular constituents required for photosynthesis in these organisms are a small number of transmembrane pigment-protein complexes. These are able to function together with a high quantum efficiency (about 95%) to convert light energy into chemical potential energy. While the structure of the various proteins have been solved for several years, direct studies of the supramolecular assembly of these complexes in native membranes needed maturity of the atomic force microscope (AFM). Here, we review the novel findings and the direct conclusions that could be drawn from high-resolution AFM analysis of photosynthetic membranes. These conclusions rely on the possibility that the AFM brings of obtaining molecular resolution images of large membrane areas and thereby bridging the resolution gap between atomic structures and cellular ultrastructure.

Indexed as

PhotosynthesisBacteriaElectron Transport Complex IIILightLight-Harvesting Protein ComplexesMembrane ProteinsMicroscopy, Atomic ForceModels, MolecularProtonsSpecies SpecificityElectron Transport Complex IIILight-Harvesting Protein ComplexesMembrane ProteinsProtons

Identifiers

PMID19266309
OpenAlexW2020067402

What OpenQuestion holds

Textmetadata
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.