Evidence map›Paper›PMID 20039094›Full record

ReviewCellular and molecular life sciences : CMLS2010

Helix insertion into bilayers and the evolution of membrane proteins.

Robert Renthal

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2010. 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
1.9field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. The big BAM theory: An open and closed case?Biochimica et biophysica acta. Biomembranes · 2020
    Review
  8. Article
  9. pHLIP Peptide Interaction with a Membrane Monitored by SAXS.The journal of physical chemistry. B · 2016
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  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

1 author at 1 institution in 1 country.

Robert RenthalDepartment of Biology, University of Texas at San Antonio, 1 UTSA Circle, San Antonio, TX, 78249, USA. Robert.Renthal@UTSA.edu
The University of Texas at San Antonio · US

Funding

STRUCTURAL VISUALIZATION IN BIOINFORMATICSG12RR013646 · NCRR · UNIVERSITY OF TEXAS SAN ANTONIO · PI WENK, CAROLA · 1998 to 2011
$19.6M
Conformations and interactions of insect olfactory receptor proteinsR21DC010071 · NIDCD · UNIVERSITY OF TEXAS SAN ANTONIO · PI RENTHAL, ROBERT D · 2009 to 2010
$390k
NCRR NIH HHS G12 RR013646NIDCD NIH HHS R21 DC010071
6 · The paper itself

Abstract

Polytopic alpha-helical membrane proteins cannot spontaneously insert into lipid bilayers without assistance from polytopic alpha-helical membrane proteins that already reside in the membrane. This raises the question of how these proteins evolved. Our current knowledge of the insertion of alpha-helices into natural and model membranes is reviewed with the goal of gaining insight into the evolution of membrane proteins. Topics include: translocon-dependent membrane protein insertion, antibiotic peptides and proteins, in vitro insertion of membrane proteins, chaperone-mediated insertion of transmembrane helices, and C-terminal tail-anchored (TA) proteins. Analysis of the E. coli genome reveals several predicted C-terminal TA proteins that may be descendents of proteins involved in pre-cellular membrane protein insertion. Mechanisms of pre-translocon polytopic alpha-helical membrane protein insertion are discussed.

Indexed as

Amino Acid SequenceBacteriocinsCalcium-Binding ProteinsCell MembraneEvolution, MolecularLipid BilayersMembrane GlycoproteinsMembrane ProteinsMolecular ChaperonesMolecular Sequence DataProtein Structure, SecondaryReceptors, Cytoplasmic and NuclearReceptors, PeptideBacteriocinsCalcium-Binding ProteinsLipid BilayersMembrane GlycoproteinsMembrane ProteinsMolecular ChaperonesReceptors, Cytoplasmic and NuclearReceptors, Peptidesignal sequence receptorBacteriocinsChaperonesTail-anchored proteinsTransloconsα-Helical membrane proteins

Identifiers

PMID20039094
PMCPMC2862650
OpenAlexW2046328704

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.