Evidence map›Paper›PMID 19933108›Full record

ArticleScience (New York, N.Y.)2009

Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome.

Thomas Becker, Shashi Bhushan, Alexander Jarasch, Jean-Paul Armache, Soledad Funes, Fabrice Jossinet, James Gumbart, Thorsten Mielke, Otto Berninghausen, Klaus Schulten and 4 more

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed
–field-weighted citation impact
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

150 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Mechanism of Protein Translocation by the Sec61 Translocon Complex.Cold Spring Harbor perspectives in biology · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors.

Thomas BeckerGene Center Munich and Center for Integrated Protein Science, Department of Chemistry and Biochemistry, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.
Shashi Bhushan
Alexander Jarasch
Jean-Paul Armache
Soledad Funes
Fabrice Jossinet
James Gumbart
Thorsten Mielke
Otto Berninghausen
Klaus Schulten
Eric Westhof
Reid Gilmore
Elisabet C Mandon
Roland Beckmann

Funding

WHOLE CELL SIMULATIONP41RR005969 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI LUTHEY-SCHULTEN, ZAIDA · 1990 to 2011
$19.8M
PROTEIN TRANSLOCATION ACROSS THE ENDOPLASMIC RETICULUMR01GM035687 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GILMORE, JAMES REID · 1985 to 2019
$5.9M
System-Level Simulation of a Bioenergetic MembraneR01GM067887 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2003 to 2018
$4.0M
NCRR NIH HHS P41 RR005969NCRR NIH HHS P41-RR05969NIGMS NIH HHS GM35687NIGMS NIH HHS R01 GM035687NIGMS NIH HHS R01 GM067887NIGMS NIH HHS R01-GM067887
6 · The paper itself

Abstract

The trimeric Sec61/SecY complex is a protein-conducting channel (PCC) for secretory and membrane proteins. Although Sec complexes can form oligomers, it has been suggested that a single copy may serve as an active PCC. We determined subnanometer-resolution cryo-electron microscopy structures of eukaryotic ribosome-Sec61 complexes. In combination with biochemical data, we found that in both idle and active states, the Sec complex is not oligomeric and interacts mainly via two cytoplasmic loops with the universal ribosomal adaptor site. In the active state, the ribosomal tunnel and a central pore of the monomeric PCC were occupied by the nascent chain, contacting loop 6 of the Sec complex. This provides a structural basis for the activity of a solitary Sec complex in cotranslational protein translocation.

Indexed as

Protein BiosynthesisProtein TransportAnimalsBinding SitesCryoelectron MicroscopyDogsImage Processing, Computer-AssistedMembrane ProteinsModels, MolecularProtein ConformationProtein MultimerizationProteinsProtein Structure, SecondaryRibosomesSaccharomyces cerevisiae ProteinsMembrane ProteinsProteinsSaccharomyces cerevisiae ProteinsSSH1 protein, S cerevisiae

Identifiers

PMID19933108
PMCPMC2920595

What OpenQuestion holds

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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.