Evidence map›Paper›PMID 39868159›Full record

ArticlebioRxiv : the preprint server for biology2025

Overcoming Fluorescence Loss in mEOS-based AAA+ Unfoldase Reporters Through Covalent Linkage.

Isabella R Walter, Baylee A Smith, Dominic Castanzo, Matthew L Wohlever

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 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

5 · Who and what money

Authors and funding

4 authors.

Isabella R WalterDepartment of Chemistry & Biochemistry, University of Toledo, Toledo, OH 43606.
Baylee A SmithDepartment of Chemistry & Biochemistry, University of Toledo, Toledo, OH 43606.
Dominic CastanzoDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720.
Matthew L WohleverDepartment of Chemistry & Biochemistry, University of Toledo, Toledo, OH 43606.ORCID 0000-0002-9406-3410

Funding

Mechanistic Investigation of Proteostasis at the Outer Mitochondrial MembraneR35GM137904 · NIGMS · UNIVERSITY OF TOLEDO · PI Matthew Lee Wohlever · 2020 to 2026
$2.6M
NIGMS NIH HHS R35 GM137904
6 · The paper itself

Abstract

Recent work has demonstrated that the soluble photoconvertable fluorescent protein mEOS can be a reporter for AAA+ (ATPases Associated with diverse cellular Activities) unfoldase activity. Given that many AAA+ proteins process membrane proteins, we sought to adapt mEOS for use with membrane protein substrates. However, direct genetic fusion of mEOS to a membrane protein completely abolished fluorescence, severely limiting the utility of mEOS for studying AAA+ proteins. To circumvent this challenge, we separately purified mEOS and a AAA+ degron, covalently linked them via Sortase, and photoconverted the linked construct. This innovative approach preserves fluorescence and enables functional analysis, offering a broadly applicable platform for the study of membrane associated AAA+ proteins.

Indexed as

AAA+ proteinfluorescent proteinmembrane proteinprotein engineeringproteostasis

Identifiers

PMID39868159
PMCPMC11761053

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.