Evidence map›Paper›PMID 22852862›Full record

ArticleJournal of the American Chemical Society2012

Direct simulation of early-stage Sec-facilitated protein translocation.

Bin Zhang, Thomas F Miller

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. 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
–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

20 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Anomalous behavior of water inside the SecY translocon.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Peptide Folding in Translocon-Like Pores.The Journal of membrane biology · 2015
    Article
  14. Article
  15. Article
  16. Functional asymmetry within the Sec61p translocon.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. Native states of fast-folding proteins are kinetic traps.Journal of the American Chemical Society · 2013
    Article
  18. Article
  19. Exploring the nature of the translocon-assisted protein insertion.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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.

Bin ZhangDivision of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, Pasadena, California 91125, USA.
Thomas F Miller

Funding

Innovative Supercomputing for Breakthrough Molecular DynamicsRC2GM093307 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI DITTRICH, MARKUS · 2009 to 2010
$2.7M
NIGMS NIH HHS RC2 GM093307
6 · The paper itself

Abstract

Direct simulations reveal key mechanistic features of early-stage protein translocation and membrane integration via the Sec-translocon channel. We present a novel computational protocol that combines non-equilibrium growth of the nascent protein with microsecond timescale molecular dynamics trajectories. Analysis of multiple, long timescale simulations elucidates molecular features of protein insertion into the translocon, including signal-peptide docking at the translocon lateral gate (LG), large lengthscale conformational rearrangement of the translocon LG helices, and partial membrane integration of hydrophobic nascent-protein sequences. Furthermore, the simulations demonstrate the role of specific molecular interactions in the regulation of protein secretion, membrane integration, and integral membrane protein topology. Salt-bridge contacts between the nascent-protein N-terminus, cytosolic translocon residues, and phospholipid head groups are shown to favor conformations of the nascent protein upon early-stage insertion that are consistent with the Type II (N(cyt)/C(exo)) integral membrane protein topology, and extended hydrophobic contacts between the nascent protein and the membrane lipid bilayer are shown to stabilize configurations that are consistent with the Type III (N(exo)/C(cyt)) topology. These results provide a detailed, mechanistic basis for understanding experimentally observed correlations between integral membrane protein topology, translocon mutagenesis, and nascent-protein sequence.

Indexed as

Molecular Dynamics SimulationBacterial ProteinsHydrophobic and Hydrophilic InteractionsProtein ConformationProtein TransportThermotoga maritimaBacterial Proteins

Identifiers

PMID22852862
PMCPMC3431202

What OpenQuestion holds

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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.