Evidence map›Paper›PMID 20541505›Full record

ArticleStructure (London, England : 1993)2010

Three-dimensional structure of TspO by electron cryomicroscopy of helical crystals.

Vladimir M Korkhov, Carsten Sachse, Judith M Short, Christopher G Tate

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed, 1 pooled it
3.7field-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

45 citing papers in PubMed, 1 synthesis or guideline pooled it, 103 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Cellular sources of TSPO expression in healthy and diseased brain.European journal of nuclear medicine and molecular imaging · 2021
    Review
  5. TSPO protein binding partners in bacteria, animals, and plants.Journal of bioenergetics and biomembranes · 2021
    Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. TSPO: An Evolutionarily Conserved Protein with Elusive Functions.International journal of molecular sciences · 2018
    Review
  13. Review
  14. In vivo PET imaging of neuroinflammation in Alzheimer's disease.Journal of neural transmission (Vienna, Austria : 1996) · 2018
    Review
  15. Applications of sequence coevolution in membrane protein biochemistry.Biochimica et biophysica acta. Biomembranes · 2018
    Review
  16. Review
  17. Article
  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

4 authors at 2 institutions in 1 country.

Vladimir M KorkhovMedical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK. volodymyr.korkhov@mol.biol.ethz.ch <volodymyr.korkhov@mol.biol.ethz.ch>
Carsten Sachse
Judith M Short
Christopher G Tate
Medical Research Council · GBMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184308Medical Research Council MC_U105184322Medical Research Council MC_U105197215
6 · The paper itself

Abstract

The 18 kDa TSPO protein is a polytopic mitochondrial outer membrane protein involved in a wide range of physiological functions and pathologies, including neurodegeneration and cancer. The pharmacology of TSPO has been extensively studied, but little is known about its biochemistry, oligomeric state, and structure. We have expressed, purified, and characterized a homologous protein, TspO from Rhodobacter sphaeroides, and reconstituted it as helical crystals. Using electron cryomicroscopy and single-particle helical reconstruction, we have determined a three-dimensional structure of TspO at 10 A resolution. The structure suggests that monomeric TspO comprises five transmembrane alpha helices that form a homodimer, which is consistent with the dimeric state observed in detergent solution. Furthermore, the arrangement of transmembrane domains of individual TspO subunits indicates a possibility of two substrate translocation pathways per dimer. The structure provides the first insight into the molecular architecture of TSPO/PBR protein family that will serve as a framework for future studies.

Indexed as

Cryoelectron MicroscopyDetergentsMembrane ProteinsMitochondrial MembranesProtein Structure, SecondaryRhodobacter sphaeroidesDetergentsMembrane Proteins

Identifiers

PMID20541505
PMCPMC2911597
OpenAlexW2048659521

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.