Evidence map›Paper›PMID 20858425›Full record

ArticleBiophysical journal2010

Assembly of the m2 tetramer is strongly modulated by lipid chain length.

Sandra Schick, Lirong Chen, Edwin Li, Janice Lin, Ingo Köper, Kalina Hristova

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

23 citing papers in PubMed, 31 citations in OpenAlex.

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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 2 institutions in 3 countries.

Sandra SchickDepartment of Materials Science and Engineering, The Johns Hopkins University, Baltimore, Maryland, USA.
Lirong Chen
Edwin Li
Janice Lin
Ingo Köper
Kalina Hristova
Johns Hopkins University · USMax Planck Institute for Polymer Research · DE

Funding

NIGMS NIH HHS GM68609
6 · The paper itself

Abstract

The influenza virus matrix protein 2 (M2) assembles into a tetramer in the host membrane during viral uncoating and maturation. It has been used as a model system to understand the relative contributions of protein-lipid and protein-protein interactions to membrane protein structure and association. Here we investigate the effect of lipid chain length on the association of the M2 transmembrane domain into tetramers using Förster resonance energy transfer. We observe that the interactions between the M2 helices are much stronger in 1,2-dilauroyl-sn-glycero-3-phosphocholine than in 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine bilayers. Thus, lipid chain length and bilayer thickness not only modulate peptide interactions, but could also be a major determinant of the association of transmembrane helices into functional membrane protein oligomers.

Indexed as

Protein MultimerizationAmino Acid SequenceCell MembraneFluorescence Resonance Energy TransferInfluenza A virusLipid BilayersMolecular Sequence DataPhosphatidylcholinesProtein ConformationViral Matrix ProteinsViroporin Proteins1,2-linoleoylphosphatidylcholine1-palmitoyl-2-oleoylphosphatidylcholineLipid BilayersM2 protein, Influenza A virusPhosphatidylcholinesViral Matrix ProteinsViroporin Proteins

Identifiers

PMID20858425
PMCPMC2941016
OpenAlexW1993408352

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.