Evidence map›Paper›PMID 39912644›Full record

ArticleApplied and environmental microbiology2025

Effects of Sup35 overexpression on the formation, morphology, and physiological functions of intracellular Sup35 assemblies.

Jianhui Feng, Ekaterina Osmekhina, Jaakko V I Timonen, Markus B Linder

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Applied and environmental microbiology, 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

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.

Jianhui FengDepartment of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, Espoo, Finland.ORCID 0000-0001-6372-6245
Ekaterina OsmekhinaDepartment of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, Espoo, Finland.ORCID 0000-0002-5756-9877
Jaakko V I TimonenThe Center of Excellence in Life-Inspired Hybrid Materials (LIBER), Aalto University, Espoo, Finland.ORCID 0000-0002-5499-1482
Markus B LinderDepartment of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, Espoo, Finland.ORCID 0000-0002-7271-6441

Funding

Jenny and Antti Wihuri Foundation CyssNovo Nordisk Fonden (NNF) NNF20OC0061306Research Council of Finland (AKA) 346105, 364199Research Council of Finland (AKA) 346112
6 · The paper itself

Abstract

The yeast prion protein Sup35 is aggregation-prone at high concentrations. IMPORTANCE: The role of condensates in living cells is often studied by overexpression. For understanding their physiological role, this can be problematic. Overexpression can shift cellular functions, thereby changing the system under study, and overexpression can also affect the phase behavior of condensates by shifting the position of the system in the underlying phase diagram. Our detailed study of overexpression of Sup35 in

Indexed as

Peptide Termination FactorsPrionsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsProtein AggregatesPeptide Termination FactorsPrionsProtein AggregatesSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaebiomolecular condensatesstress responseSup35super-resolution radial fluctuations

Identifiers

PMID39912644
PMCPMC11921396

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.