Evidence map›Paper›PMID 19581593›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Insertion of short transmembrane helices by the Sec61 translocon.

Simon Jaud, Mónica Fernández-Vidal, Ingmarie Nilsson, Nadja M Meindl-Beinker, Nadja C Hübner, Douglas J Tobias, Gunnar von Heijne, Stephen H White

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Folding and Insertion of Transmembrane Helices at the ER.International journal of molecular sciences · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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

8 authors.

Simon JaudDepartment of Chemistry and the Center for Biomembrane Systems, University of California, Irvine, CA 92697-2025, USA.
Mónica Fernández-Vidal
Ingmarie Nilsson
Nadja M Meindl-Beinker
Nadja C Hübner
Douglas J Tobias
Gunnar von Heijne
Stephen H White

Funding

Membrane Protein Folding and AssemblyR01GM074637 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WHITE, STEPHEN H. · 2006 to 2020
$4.5M
FLUID BILAYER INTERACTIONS WITH PEPTIDESR01GM046823 · NIGMS · UNIVERSITY OF CALIFORNIA IRVINE · PI WHITE, STEPHEN H. · 1992 to 2004
$1.3M
Concerted membrane diffraction and simulation studiesR01GM068002 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WHITE, STEPHEN H. · 2003 to 2006
$989k
NIGMS NIH HHS GM46823NIGMS NIH HHS GM68002NIGMS NIH HHS GM74637NIGMS NIH HHS R01 GM046823NIGMS NIH HHS R01 GM068002NIGMS NIH HHS R01 GM074637
6 · The paper itself

Abstract

The insertion efficiency of transmembrane (TM) helices by the Sec61 translocon depends on helix amino acid composition, the positions of the amino acids within the helix, and helix length. We have used an in vitro expression system to examine systematically the insertion efficiency of short polyleucine segments (L(n), n = 4 ... 12) flanked at either end by 4-residue sequences of the form XXPX-L(n)-XPXX with X = G, N, D, or K. Except for X = K, insertion efficiency (p) is <10% for n < 8, but rises steeply to 100% for n = 12. For X = K, p is already close to 100% for n = 10. A similar pattern is observed for synthetic peptides incorporated into oriented phospholipid bilayer arrays, consistent with the idea that recognition of TM segments by the translocon critically involves physical partitioning of nascent peptide chains into the lipid bilayer. Molecular dynamics simulations suggest that insertion efficiency is determined primarily by the energetic cost of distorting the bilayer in the vicinity of the TM helix. Very short lysine-flanked leucine segments can reduce the energetic cost by extensive hydrogen bonding with water and lipid phosphate groups (snorkeling) and by partial unfolding.

Indexed as

Models, BiologicalComputer SimulationHydrogen BondingLipid BilayersMembrane ProteinsPeptidesSEC Translocation ChannelsLipid BilayersMembrane ProteinsPeptidespolyleucineSEC Translocation Channels

Identifiers

PMID19581593
PMCPMC2710650

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.