Evidence map›Paper›PMID 37645758›Full record

ArticlebioRxiv : the preprint server for biology2023

Differences in Oligomerization of the SARS-CoV-2 Envelope Protein, Poliovirus VP4, and HIV Vpu.

Julia A Townsend, Oluwaseun Fapohunda, Zhihan Wang, Hieu Pham, Michael T Taylor, Brian Kloss, Sang Ho Park, Stanley Opella, Craig A Aspinwall, Michael T Marty

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Julia A TownsendDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Oluwaseun FapohundaDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Zhihan WangDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Hieu PhamDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Michael T TaylorDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Brian KlossNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, New York, NY 10027, USA.
Sang Ho ParkDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA.
Stanley OpellaDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA.
Craig A AspinwallDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
Michael T MartyDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
University of Arizona · USUniversity of California San Diego · USNew York Structural Biology Center · US

Funding

Training (303-338)P41GM116799 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI HENDRICKSON, WAYNE A. · 2016 to 2020
$7.1M
CHEMISTRY-BIOLOGY INTERFACE TRAINING PROGRAMT32GM008804 · NIGMS · UNIVERSITY OF ARIZONA · PI MONTFORT, WILLIAM R. · 2003 to 2023
$3.9M
Unravelling Membrane Protein-Lipid Interactions using Nanodiscs and Mass SpectrometryR35GM128624 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Michael T Marty · 2018 to 2026
$3.6M
Structures, Dynamics, and Functions of Membrane ProteinsR35GM122501 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2017 to 2021
$2.5M
New Chemical Tools for Optically Controlled Protein ModificationR35GM143120 · NIGMS · UNIVERSITY OF WYOMING · PI TAYLOR, MICHAEL T · 2021 to 2025
$1.6M
NIGMS NIH HHS P41 GM116799NIGMS NIH HHS R35 GM122501NIGMS NIH HHS R35 GM128624NIGMS NIH HHS R35 GM143120NIGMS NIH HHS T32 GM008804
6 · The paper itself

Abstract

Viroporins constitute a class of viral membrane proteins with diverse roles in the viral life cycle. They can self-assemble and form pores within the bilayer that transport substrates, such as ions and genetic material, that are critical to the viral infection cycle. However, there is little known about the oligomeric state of most viroporins. Here, we use native mass spectrometry (MS) in detergent micelles to uncover the patterns of oligomerization of the full-length SARS-CoV-2 envelope (E) protein, poliovirus VP4, and HIV Vpu. Our data suggest that the E protein is a specific dimer, VP4 is exclusively monomeric, and Vpu assembles into a polydisperse mixture of oligomers under these conditions. Overall, these results revealed the diversity in the oligomerization of viroporins, which has implications for mechanisms of their biological functions as well as their potential as therapeutic targets.

Indexed as

HIV Vpunative mass spectrometryoligomerizationpolio VP4SARS-CoV-2 Envelope proteinViroporins

Identifiers

PMID37645758
PMCPMC10462163
OpenAlexW4386029779

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.