Evidence map›Paper›PMID 41551578›Full record

ArticleBiophysica2025

Membrane Depth Measurements of E Protein by

Andrew K Morris, Robert M McCarrick, Gary A Lorigan

Abstract read
In one paragraph

Article in Biophysica, 2025. 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.

No citing paper in PubMed yet.

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

3 authors.

Andrew K MorrisDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA.
Robert M McCarrickDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA.
Gary A LoriganDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA.

Funding

EPR Spectroscopic Studies of Membrane Proteins-Diversity SupplementR35GM126935 · NIGMS · MIAMI UNIVERSITY OXFORD · PI GARY A LORIGAN · 2018 to 2026
$3.3M
NIGMS NIH HHS R35 GM126935
6 · The paper itself

Abstract

A topological analysis was performed by taking ESEEM measurements of site-specifically labeled E protein from SARS-CoV-2. The intensity of deuterium modulation arising from either deuterated solvent or deuterated lipid acyl chains revealed exposure to solvent or the bilayer hydrophobic region. Spin-labeled lipids and soluble spin labels were used as points of comparison. The data indicate that spin labels placed along the transmembrane helix of the E protein showed close contact with lipid acyl chains, but also substantial contact with solvent, while those placed on the C-terminal domain showed substantial but lower exposure to lipid acyl chains, with comparable solvent exposure. The results support the view that the C-terminal domain is in contact with the bilayer surface.

Indexed as

envelope proteinEPRESEEM

Identifiers

PMID41551578
PMCPMC12807508

What OpenQuestion holds

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LicenceCC BY
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.