Evidence map›Paper›PMID 41715294›Full record

ArticleFEBS letters2026

Protein disulfide isomerase dissolves and detoxifies oligomeric assemblies of amyloid beta peptide.

Antonio Mele, Albert Serrano, Maria C Zabala-Rodriguez, Baggio A Evangelista, Haley Lehew, Jasmina Kovacevic, Michael Taylor, Suren A Tatulian, Ken Teter

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 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

9 authors.

Antonio MeleBurnett School of Biomedical Sciences, University of Central Florida, Orlando, FL, USA.
Albert SerranoBurnett School of Biomedical Sciences, University of Central Florida, Orlando, FL, USA.
Maria C Zabala-RodriguezBurnett School of Biomedical Sciences, University of Central Florida, Orlando, FL, USA.
Baggio A EvangelistaBurnett School of Biomedical Sciences, University of Central Florida, Orlando, FL, USA.
Haley LehewBurnett School of Biomedical Sciences, University of Central Florida, Orlando, FL, USA.
Jasmina KovacevicBurnett School of Biomedical Sciences, University of Central Florida, Orlando, FL, USA.
Michael TaylorBurnett School of Biomedical Sciences, University of Central Florida, Orlando, FL, USA.
Suren A TatulianDepartment of Physics, University of Central Florida, Orlando, FL, USA.
Ken TeterBurnett School of Biomedical Sciences, University of Central Florida, Orlando, FL, USA.ORCID https://orcid.org/0000-0003-4176-9361

Funding

The Florida Department of Health, Ed and Ethel Moore Alzheimer's Disease Research Program 21A06The Florida Department of Health, Ed and Ethel Moore Alzheimer's Disease Research Program 8ZA12
6 · The paper itself

Abstract

Aggregated amyloid beta peptide (Aβ) contributes to Alzheimer's disease through neurotoxic effects and a prion-like mode of transmission. We report that protein disulfide isomerase (PDI) exhibits disaggregase activity against oligomeric but not fibrillar forms of Aβ. PDI did not bind monomeric Aβ, indicating its highly effective inhibition of fibril formation occurs through reversal of early-stage oligomers rather than prevention of the initial aggregate. Cells exposed to both PDI and oligomeric Aβ were protected from Aβ-induced toxicity. An S-nitrosylated form of PDI that is associated with neurodegeneration could not bind to oligomeric Aβ, thereby eliminating its neuroprotective disaggregase activity. Our observations suggest PDI could be used both physiologically and therapeutically to dissolve the oligomeric forms of Aβ.

Indexed as

Amyloid beta-PeptidesPeptide FragmentsProtein Disulfide-IsomerasesProtein MultimerizationAnimalsHumansAmyloid beta-PeptidesPeptide FragmentsProtein Disulfide-IsomerasesAlzheimer's diseasechaperoneconditional disorderdisaggregaseprotein disulfide isomerase

Identifiers

PMID41715294
PMCPMC13404157

What Socratic 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 Socratic graph.