Evidence map›Paper›PMID 16214859›Full record

ArticleBiophysical journal2006

Transmembrane peptides stabilize inverted cubic phases in a biphasic length-dependent manner: implications for protein-induced membrane fusion.

D P Siegel, V Cherezov, D V Greathouse, R E Koeppe, J Antoinette Killian, M Caffrey

Open access · bronzeAbstract 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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
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  12. Micron-scale holes terminate the phage infection cycle.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  13. Article
  14. Membrane fusion.Nature structural & molecular biology · 2008
    Review
  15. Article
  16. Article
  17. 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

6 authors at 4 institutions in 4 countries.

D P SiegelGivaudan Inc., Cincinnati, Ohio, USA. david.siegel@givaudan.com
V Cherezov
D V Greathouse
R E Koeppe
J Antoinette Killian
M Caffrey
The Ohio State University · USUniversity of Arkansas at Fayetteville · USGivaudan (Switzerland) · CHUtrecht University · NL

Funding

Structure based drug discoveryP20RR015569 · NCRR · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI MILLETT, FRANCIS S · 2000 to 2009
$21.4M
MEMBRANE PROTEIN STRUCTURE : USE OF LIPIDIC MESOPHASESR01GM061070 · NIGMS · OHIO STATE UNIVERSITY · PI CAFFREY, MARTIN D. · 2001 to 2004
$928k
MECHANISM OF ION TRANSPORT THROUGH MEMBRANE CHANNELSR01GM034968 · NIGMS · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI KOEPPE, ROGER E · 1985 to 2001
$301k
KINETICS &MECHANISM OF LIPID PHASE TRANSITIONSR01DK036849 · NIDDK · OHIO STATE UNIVERSITY · PI CAFFREY, MARTIN D. · 1990 to 1992
–
KINETICS AND MECHANISM OF LIPID PHASE TRANSITIONSR23DK036849 · NIDDK · OHIO STATE UNIVERSITY · PI CAFFREY, MARTIN D. · 1986 to 1988
–
NCRR NIH HHS P20 RR015569NCRR NIH HHS RR15569NIDDK NIH HHS DK36849NIDDK NIH HHS DK46295NIGMS NIH HHS GM34968NIGMS NIH HHS GM61070NIGMS NIH HHS R01 GM061070
6 · The paper itself

Abstract

WALP peptides consist of repeating alanine-leucine sequences of different lengths, flanked with tryptophan "anchors" at each end. They form membrane-spanning alpha-helices in lipid membranes, and mimic protein transmembrane domains. WALP peptides of increasing length, from 19 to 31 amino acids, were incorporated into N-monomethylated dioleoylphosphatidylethanolamine (DOPE-Me) at concentrations up to 0.5 mol % peptide. When pure DOPE-Me is heated slowly, the lamellar liquid crystalline (L(alpha)) phase first forms an inverted cubic (Q(II)) phase, and the inverted hexagonal (H(II)) phase at higher temperatures. Using time-resolved x-ray diffraction and slow temperature scans (1.5 degrees C/h), WALP peptides were shown to decrease the temperatures of Q(II) and H(II) phase formation (T(Q) and T(H), respectively) as a function of peptide concentration. The shortest and longest peptides reduced T(Q) the most, whereas intermediate lengths had weaker effects. These findings are relevant to membrane fusion because the first step in the L(alpha)/Q(II) phase transition is believed to be the formation of fusion pores between pure lipid membranes. These results imply that physiologically relevant concentrations of these peptides could increase the susceptibility of biomembrane lipids to fusion through an effect on lipid phase behavior, and may explain one role of the membrane-spanning domains in the proteins that mediate membrane fusion.

Indexed as

Membrane FusionAmino AcidsLipid BilayersLipidsLiposomesModels, MolecularMolecular ConformationPeptidesPhase TransitionPhosphatidylethanolaminesProteinsProtein Structure, SecondaryRecombinant Fusion ProteinsSynchrotronsTemperatureThermodynamics1,2-dioleoyl-glycero-3-phosphatidyl ethanolamineAmino AcidsLipid BilayersLipidsLiposomesPeptidesPhosphatidylethanolaminesProteinsRecombinant Fusion Proteins

Identifiers

PMID16214859
PMCPMC1367019
OpenAlexW2144804038

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.