Yeasts as Complementary Model Systems for the Study of the Pathological Repercussions of Enhanced Synphilin-1 Glycation and Oxidation.

David Seynnaeve, Daniel P Mulvihill, Joris Winderickx, Vanessa Franssens

Open access · goldAbstract read

In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.1field-weighted citation impact, top 56% of its field

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

1 citing paper in PubMed, 2 citations in OpenAlex.

Yeast Models and Molecular Mechanisms of Neurodegenerative Diseases.International journal of molecular sciences · 2021
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

4 authors at 2 institutions in 2 countries.

David SeynnaeveFunctional Biology, Division of Molecular Physiology of Plants & Microorganisms, KU Leuven, 3000 Leuven, Belgium.ORCID 0000-0002-2598-3934

Daniel P MulvihillSchool of Biosciences, Ingram Building, Room 424, University of Kent, Canterbury, Kent CT2 7NH, UK.ORCID 0000-0003-2502-5274

Joris WinderickxFunctional Biology, Division of Molecular Physiology of Plants & Microorganisms, KU Leuven, 3000 Leuven, Belgium.ORCID 0000-0003-3133-7733

Vanessa FranssensFunctional Biology, Division of Molecular Physiology of Plants & Microorganisms, KU Leuven, 3000 Leuven, Belgium.

Physiol (Belgium) · BEUniversity of Kent · GB

Funding

Fonds Wetenschappelijk Onderzoek 1287517N, 1101317N, S006617N, G0A6315NKU Leuven C14/17/063

6 · The paper itself

Abstract

Synphilin-1 has previously been identified as an interaction partner of α-Synuclein (αSyn), a primary constituent of neurodegenerative disease-linked Lewy bodies. In this study, the repercussions of a disrupted glyoxalase system and aldose reductase function on Synphilin-1 inclusion formation characteristics and cell growth were investigated. To this end, either fluorescent dsRed-tagged or non-tagged human

Indexed as

Oxidative StressAlcohol OxidoreductasesAldehyde ReductaseCarrier ProteinsGlycosylationHumansInclusion BodiesLactoylglutathione LyaseNerve Tissue ProteinsOxidation-ReductionSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAlcohol OxidoreductasesAldehyde ReductaseCarrier Proteinsgluconolactone oxidaseLactoylglutathione LyaseNerve Tissue ProteinsSaccharomyces cerevisiae ProteinsSNCAIP protein, humanglycationneurodegenerationoxidationParkinson’s diseaseprotein aggregationSynphilin-1yeast

Identifiers

PMID33562355

DOI10.3390/ijms22041677

PMCPMC7915245

OpenAlexW3129047769

What OpenQuestion holds

Textmetadata

LicenceCC BY

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.