Evidence map›Paper›PMID 16415058›Full record

ArticleBiophysical journal2006

Molecular dynamics studies of the archaeal translocon.

James Gumbart, Klaus Schulten

Abstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Peptide Folding in Translocon-Like Pores.The Journal of membrane biology · 2015
    Article
  13. Article
  14. Direct simulation of early-stage Sec-facilitated protein translocation.Journal of the American Chemical Society · 2012
    Article
  15. Article
  16. Article
  17. Free energy of nascent-chain folding in the translocon.Journal of the American Chemical Society · 2011
    Article
  18. Probing the SecYEG translocation pore size with preproteins conjugated with sizable rigid spherical molecules.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  19. Free-energy cost for translocon-assisted insertion of membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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

2 authors.

James GumbartDepartment of Physics, University of Illinois at Urbana-Champaign and Beckman Institute for Advanced Science and Technology, Urbana, Illinois 61801, USA.
Klaus Schulten

Funding

WHOLE CELL SIMULATIONP41RR005969 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI LUTHEY-SCHULTEN, ZAIDA · 1990 to 2011
$19.8M
System-Level Simulation of a Bioenergetic MembraneR01GM067887 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2003 to 2018
$4.0M
NCRR NIH HHS 5-P41-RR05969NCRR NIH HHS P41 RR005969NIGMS NIH HHS 1-R01-GM067887NIGMS NIH HHS R01 GM067887
6 · The paper itself

Abstract

The translocon is a protein-conducting channel conserved over all domains of life that serves to translocate proteins across or into membranes. Although this channel has been well studied for many years, the recent discovery of a high-resolution crystal structure opens up new avenues of exploration. Taking advantage of this, we performed molecular dynamics simulations of the translocon in a fully solvated lipid bilayer, examining the translocation abilities of monomeric SecYEbeta by forcing two helices comprised of different amino acid sequences to cross the channel. The simulations revealed that the so-called plug of SecYEbeta swings open during translocation, closing thereafter. Likewise, it was established that the so-called pore ring region of SecYEbeta forms an elastic, yet tight, seal around the translocating oligopeptides. The closed state of the channel was found to block permeation of all ions and water molecules; in the open state, ions were blocked. Our results suggest that the SecYEbeta monomer is capable of forming an active channel.

Indexed as

AlanineArchaeaArchaeal ProteinsAsparagineBiophysicsComputer SimulationCytoplasmDatabases, ProteinDimerizationGlycineHistidineHydrogenIonsLeucineLipid BilayersLipids1-palmitoyl-2-oleoylphosphatidylcholineAlanineArchaeal ProteinsAsparagineGlycineHistidineHydrogenIonsLeucineLipid BilayersLipidsOligopeptidesPhosphatidylcholinesWater

Identifiers

PMID16415058
PMCPMC1403164

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.