Evidence map›Paper›PMID 30819568›Full record

ArticleBiophysical journal2019

Influenza A M2 Channel Clustering at High Protein/Lipid Ratios: Viral Budding Implications.

Joana Paulino, Xiaodong Pang, Ivan Hung, Huan-Xiang Zhou, Timothy A Cross

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2019. 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
3.2field-weighted citation impact, top 7% 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, 41 citations in OpenAlex.

  1. Article
  2. Journal of the American Chemical Society · 2025
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  3. Article
  4. The Role of Cholesterol in M2 Clustering and Viral Budding Explained.Journal of chemical theory and computation · 2025
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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

5 authors at 3 institutions in 1 country.

Joana PaulinoInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida; National High Magnetic Field Laboratory, Tallahassee, Florida.
Xiaodong PangInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida.
Ivan HungNational High Magnetic Field Laboratory, Tallahassee, Florida.
Huan-Xiang ZhouInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida; Department of Chemistry and Department of Physics, University of Illinois at Chicago, Chicago, Illinois.
Timothy A CrossInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida; National High Magnetic Field Laboratory, Tallahassee, Florida; Department of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida. Electronic address: cross@magnet.fsu.edu.
Florida State University · USNational High Magnetic Field Laboratory · USUniversity of Illinois Chicago · US

Funding

TR&D3-SCHP41GM122698 · NIGMS · FLORIDA STATE UNIVERSITY · PI BREY, WILLIAM W, CROSS, TIMOTHY A · 2017 to 2021
$6.7M
DYNAMIC AND STRUCTURAL ELUCIDATION OF GRAMICIDIN A'R01AI023007 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 1987 to 2014
$5.1M
Membrane Protein Structures and Interactions in the M. tuberculosis DivisomeR01AI119178 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 2015 to 2019
$3.6M
NIAID NIH HHS R01 AI023007NIAID NIH HHS R01 AI119178NIGMS NIH HHS P41 GM122698
6 · The paper itself

Abstract

Protein dynamics in crowded environments is important for understanding protein functions in vivo and is especially relevant for membrane proteins because of the roles of protein-protein interactions in membrane protein functions and their regulation. Here, using solid-state NMR spectroscopy in combination with coarse-grained molecular dynamics simulations, we report that the rotational correlation time for the transmembrane domain of the influenza A M2 proton channel in lipid bilayers increases dramatically at an elevated protein/lipid ratio. This increase is attributable to persistent protein-protein interactions, thus revealing for the first time, to the best of our knowledge, extensive cluster formation of the M2 tetrameric channel. Such clustering appears to have direct biological relevance during budding of the nascent influenza virus, which does not use the endosomal sorting complexes required for transport machinery. Indeed, initial coarse-grained molecular dynamics simulations of the longer M2 construct known as the conductance domain suggest clustering-induced membrane curvature formation.

Indexed as

Lipid MetabolismVirus ReleaseAmino Acid SequenceDiffusionInfluenza A virusModels, MolecularProtein ConformationRotationViral Matrix ProteinsViroporin ProteinsM2 protein, Influenza A virusViral Matrix ProteinsViroporin Proteins

Identifiers

PMID30819568
PMCPMC6428927
OpenAlexW2911785287

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.