Evidence map›Paper›PMID 40947943›Full record

ArticleJournal of peptide science : an official publication of the European Peptide Society2025

Plant Hormone Cytokinin as Aggregation Modulator of Gelsolin Amyloidosis.

Dev Seneviratne, Naomi Stock, Tyra Lewis, R J Neil Emery, Sanela Martic

Abstract read
In one paragraph

Article in Journal of peptide science : an official publication of the European Peptide Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. Plant Hormone Cytokinin as Aggregation Modulator of Gelsolin Amyloidosis.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Article
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

5 authors.

Dev SeneviratneEnvironmental and Life Sciences Program, Trent University, Peterborough, Ontario, Canada.
Naomi StockWater Quality Center, Trent University, Peterborough, Ontario, Canada.ORCID https://orcid.org/0000-0002-3472-9284
Tyra LewisEnvironmental and Life Sciences Program, Trent University, Peterborough, Ontario, Canada.
R J Neil EmeryEnvironmental and Life Sciences Program, Trent University, Peterborough, Ontario, Canada.ORCID https://orcid.org/0000-0003-1304-6430
Sanela MarticEnvironmental and Life Sciences Program, Trent University, Peterborough, Ontario, Canada.ORCID https://orcid.org/0000-0001-6642-2298

Funding

Natural Sciences and Engineering Research Council RGPIN49842020
6 · The paper itself

Abstract

Amyloidosis, a self-assembly of proteins or peptides, is associated with numerous degenerative diseases, such as gelsolin amyloidosis, which remain without a cure. Gelsolin protein is an actin-binding protein, but when aggregated in a diseased state, it is a potential drug target. Specifically, gelsolin mutations, N184K and D187Y, have been linked to renal amyloidosis and systemic progressive deposition of amyloids, respectively. Understanding how such mutations mitigate gelsolin aggregation and how this process can be prevented through small molecule inhibitors is of interest. Herein, we explored the efficacies of plant-based naturally occurring cytokinin (CK) molecules as aggregation modulators in vitro. Using various biophysical methods, such as spectroscopy and microscopy, the aggregation of wild-type gelsolin peptide 184NNGDCFILDL193 and its mutants (N184K, D187Y) was investigated. The mutations significantly promoted aggregation, which is of biological significance. The CK trans-zeatin (tZ) was a more effective disaggregation promoter compared with kinetin (Kin). The experimentally determined IC

Indexed as

AmyloidosisCytokininsGelsolinPlant Growth RegulatorsHumansMutationProtein AggregatesCytokininsGelsolinPlant Growth RegulatorsProtein Aggregatesaggregationamyloidcytokiningelsolin

Identifiers

PMID40947943
PMCPMC12434452

What OpenQuestion holds

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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.