Evidence map›Paper›PMID 42204260›Full record

ArticleScientific reports2026

Liquid-liquid phase separation and the formation of amyloid fibrils from DcpS scavenger enzymes.

Aleksandra Ferenc-Mrozek, Maria Winiewska-Szajewska, Hanna Nieznańska, Anna Anielska-Mazur, Marek Warzecha, Wojciech Dzwolak, Maciej Łukaszewicz

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Article in Scientific reports, 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

7 authors.

Aleksandra Ferenc-MrozekDivision of Biophysics, Faculty of Physics, University of Warsaw, Pasteura 5, 02-093, Warsaw, Poland.
Maria Winiewska-SzajewskaDivision of Biophysics, Faculty of Physics, University of Warsaw, Pasteura 5, 02-093, Warsaw, Poland.
Hanna NieznańskaLaboratory of Electron Microscopy, Nencki Institute of Experimental Biology PAS, Pasteura 3, 02-093, Warsaw, Poland.
Anna Anielska-MazurInstitute of Biochemistry and Biophysics PAS, Pawinskiego 5a, 02-106, Warsaw, Poland.
Marek WarzechaDivision of Biophysics, Faculty of Physics, University of Warsaw, Pasteura 5, 02-093, Warsaw, Poland.
Wojciech DzwolakFaculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, Pasteura 1, 02-093, Warsaw, Poland. wdzwolak@chem.uw.edu.pl.
Maciej ŁukaszewiczDivision of Biophysics, Faculty of Physics, University of Warsaw, Pasteura 5, 02-093, Warsaw, Poland. Maciej.Lukaszewicz@fuw.edu.pl.

Funding

Narodowe Centrum Nauki UMO/2017/27/B/NZ1/01859
6 · The paper itself

Abstract

Decapping Scavenger (DcpS) enzyme was initially identified by its ability to hydrolyze the cap structure resulting from mRNA decay. Human DcpS is an established target for acute myeloid leukemia (AML) and hepatic metastasis. Recently, the protein has been linked to neuronal development regulation and implicated in certain developmental neurological disorders. Here we demonstrate for the first time that DcpS of the human and C. elegans nematode origin undergoes misfolding in vitro, leading to the formation of amyloid-like fibrils. Additionally, the DcpS

Indexed as

AmyloidCaenorhabditis elegans ProteinsAnimalsCaenorhabditis elegansHumansKineticsPhase SeparationPhase TransitionProtein AggregatesProtein FoldingAmyloidCaenorhabditis elegans ProteinsProtein AggregatesAmyloid fibrilsDcpSDecappingLLPS

Identifiers

PMID42204260
PMCPMC13444105

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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.