Evidence map›Paper›PMID 20798065›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Functional interactions between membrane-bound transporters and membranes.

Linda Näsvik Ojemyr, Hyun Ju Lee, Robert B Gennis, Peter Brzezinski

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. ATP synthase activity boosts membrane proton acceptance and lateral diffusion.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Kinetic coupling of the respiratory chain with ATP synthase, but not proton gradients, drives ATP production in cristae membranes.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Review
  7. Exploring fast proton transfer events associated with lateral proton diffusion on the surface of membranes.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Structure of a functional obligate complex IIINature structural & molecular biology · 2018
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Superresolution microscopy reveals spatial separation of UCP4 and F0F1-ATP synthase in neuronal mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Review
  19. Article
  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

4 authors at 1 institution in 2 countries.

Linda Näsvik OjemyrDepartment of Biochemistry and Biophysics, Stockholm University, Sweden.
Hyun Ju Lee
Robert B Gennis
Peter Brzezinski
Stockholm University · SE

Funding

PROTEIN/LIPID INTERACTIONSR01HL016101 · NHLBI · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GENNIS, ROBERT B · 1985 to 2015
$6.8M
NHLBI NIH HHS R01 HL016101
6 · The paper itself

Abstract

One key role of many cellular membranes is to hold a transmembrane electrochemical ion gradient that stores free energy, which is used, for example, to generate ATP or to drive transmembrane transport processes. In mitochondria and many bacteria, the gradient is maintained by proton-transport proteins that are part of the respiratory (electron-transport) chain. Even though our understanding of the structure and function of these proteins has increased significantly, very little is known about the specific role of functional protein-membrane and membrane-mediated protein-protein interactions. Here, we have investigated the effect of membrane incorporation on proton-transfer reactions within the membrane-bound proton pump cytochrome c oxidase. The results show that the membrane acts to accelerate proton transfer into the enzyme's catalytic site and indicate that the intramolecular proton pathway is wired via specific amino acid residues to the two-dimensional space defined by the membrane surface. We conclude that the membrane not only acts as a passive barrier insulating the interior of the cell from the exterior solution, but also as a component of the energy-conversion machinery.

Indexed as

Catalytic DomainCell MembraneMembrane Transport ProteinsModels, MolecularProtein BindingMembrane Transport Proteins

Identifiers

PMID20798065
PMCPMC2936589
OpenAlexW2025890541

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.