Evidence map›Paper›PMID 40453094›Full record

ArticleFrontiers in immunology2025

Engineered sequestrins inhibit aggregation of pathogenic alpha-synuclein mutants.

Linnea Charlotta Hjelm, Wojciech Paslawski, Christofer Lendel, Siri Flemming Svedmark, Per Svenningsson, Stefan Ståhl, Hanna Lindberg, John Löfblom

Abstract read
In one paragraph

Article in Frontiers in immunology, 2025. 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
–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

1 citing paper in PubMed.

  1. Review
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

8 authors.

Linnea Charlotta HjelmDepartment of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, Stockholm, Sweden.
Wojciech PaslawskiDepartment of Clinical Neuroscience, Karolinska Institute, Stockholm, Sweden.
Christofer LendelDepartment of Chemistry, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, Stockholm, Sweden.
Siri Flemming SvedmarkDepartment of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, Stockholm, Sweden.
Per SvenningssonDepartment of Clinical Neuroscience, Karolinska Institute, Stockholm, Sweden.
Stefan StåhlDepartment of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, Stockholm, Sweden.
Hanna LindbergDepartment of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, Stockholm, Sweden.
John LöfblomDepartment of Protein Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, Stockholm, Sweden.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Misfolding and aggregation of the neuronal protein alpha-synuclein (aSyn) has been identified as a hallmark of Parkinson's disease (PD) pathology and other synucleinopathies. Preventing formation of intracellular aSyn accumulations constitutes a therapeutic strategy against disease development. We recently reported on a new type of affinity protein, denoted

Indexed as

alpha-SynucleinMutationProtein Aggregation, PathologicalHumansParkinson DiseasePeptide LibraryProtein AggregatesProtein BindingProtein Engineeringalpha-SynucleinPeptide LibraryProtein Aggregatesaffibody moleculealpha-synucleindirected evolutionParkinson’s diseasephage displaysequestrin

Identifiers

PMID40453094
PMCPMC12122515

What OpenQuestion holds

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LicenceCC BY
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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.