Evidence map›Paper›PMID 42283461›Full record

ArticleJournal of virology2026

A highly conserved basic motif in the wing domain of portal protein is necessary for oligomerization and incorporation in phage P22.

Makayla N Leroux, Lohra M Young, Martin F Jarrold, Carolyn M Teschke

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of virology, 2026. 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

4 authors.

Makayla N LerouxDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut, USA.ORCID 0000-0002-0009-3628
Lohra M YoungMegadalton Solutions, Bloomington, Indiana, USA.
Martin F JarroldMegadalton Solutions, Bloomington, Indiana, USA.ORCID 0000-0001-7084-176X
Carolyn M TeschkeDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut, USA.ORCID 0000-0001-6420-4895

Funding

Understanding the Protein:Protein Interactions Required for Virus AssemblyR01GM076661 · NIGMS · UNIVERSITY OF CONNECTICUT STORRS · PI TESCHKE, CAROLYN M · 2007 to 2022
$7.2M
Phages as Lenses to Study Virus Assembly and Virus: Host InteractionsR35GM156358 · NIGMS · UNIVERSITY OF CONNECTICUT STORRS · PI CAROLYN M TESCHKE · 2025 to 2026
$1.2M
NIGMS NIH HHS F31GM14795NIGMS NIH HHS R01 GM076661NIGMS NIH HHS R01GM076661NIGMS NIH HHS R35 GM156358NIGMS NIH HHS R35GM156358
6 · The paper itself

Abstract

The dodecameric portal ring complex plays a critical role in the assembly of most double-stranded DNA (dsDNA) viruses and bacteriophages. The fidelity of ring oligomerization and incorporation of a single 12-mer portal ring is driven by interactions with a viral scaffolding protein. Structural evidence indicates that the wing domain of the portal is a crucial site for scaffolding protein interactions. In this study, the functional significance of the highly conserved

Indexed as

Bacteriophage P22Capsid ProteinsProtein MultimerizationVirus AssemblyAmino Acid MotifsAmino Acid SequenceModels, MolecularCapsid Proteinsportal protein, bacteriophage P22DNA packagingportal proteinscaffolding proteinvirus assembly

Identifiers

PMID42283461
PMCPMC13386823

What OpenQuestion holds

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Registered trials

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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.