Evidence map›Paper›PMID 20637421›Full record

ArticleStructure (London, England : 1993)2010

Dynamics of SecY translocons with translocation-defective mutations.

Ana-Nicoleta Bondar, Coral del Val, J Alfredo Freites, Douglas J Tobias, Stephen H White

Open access · bronzeAbstract 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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.8field-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

27 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. DynamicsProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Channel crossing: how are proteins shipped across the bacterial plasma membrane?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015
    Review
  11. Review
  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. Article
  14. Exploring the nature of the translocon-assisted protein insertion.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Direct simulation of early-stage Sec-facilitated protein translocation.Journal of the American Chemical Society · 2012
    Article
  20. The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
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

5 authors at 3 institutions in 2 countries.

Ana-Nicoleta BondarDepartment of Physiology and Biophysics, University of California at Irvine, Irvine, CA 92697-4560, USA.
Coral del Val
J Alfredo Freites
Douglas J Tobias
Stephen H White
University of California, Irvine · USInterface (United States) · USUniversidad de Granada · ES

Funding

Project 3: Structural Studies of Voltage-Gated Potassium Channels as FunctionP01GM086685 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WHITE, STEPHEN H. · 2009 to 2013
$6.7M
Membrane Protein Folding and AssemblyR01GM074637 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WHITE, STEPHEN H. · 2006 to 2020
$4.5M
NIGMS NIH HHS GM-74637NIGMS NIH HHS GM86685NIGMS NIH HHS P01 GM086685NIGMS NIH HHS R01 GM074637
6 · The paper itself

Abstract

The SecY/Sec61 translocon complex, located in the endoplasmic reticulum membrane of eukaryotes (Sec61) or the plasma membrane of prokaryotes (SecY), mediates the transmembrane secretion or insertion of nascent proteins. Mutations that permit the secretion of nascent proteins with defective signal sequences (Prl-phenotype), or interfere with the transmembrane orientation of newly synthesized protein segments, can affect protein topogenesis. The crystallographic structure of SecYEbeta from Methanococcus jannaschii revealed widespread distribution of mutations causing topogenesis defects, but not their molecular mechanisms. Based upon prolonged molecular dynamics simulations of wild-type M. jannaschii SecYEbeta and an extensive sequence-conservation analysis, we show that the closed state of the translocon is stabilized by hydrogen-bonding interactions of numerous highly conserved amino acids. Perturbations induced by mutation at various locations are rapidly relayed to the plug segment that seals the wild-type closed-state translocon, leading to displacement and increased hydration of the plug.

Indexed as

Models, MolecularProtein ConformationAmino AcidsAmino Acid SequenceComputational BiologyHydrogen BondingMembrane Transport ProteinsMethanococcusMolecular Sequence DataMutationProtein TransportSequence AlignmentAmino AcidsMembrane Transport Proteins

Identifiers

PMID20637421
PMCPMC2909450
OpenAlexW2073990689

What OpenQuestion holds

Textmetadata
LicenceTDM
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.