Evidence map›Paper›PMID 38358134›Full record

ArticleProtein science : a publication of the Protein Society2024

The effects of biological crowders on fibrillization, structure, diffusion, and conformational dynamics of α-synuclein.

Sina Heravi, Jude Vincent Dobbin Power, Anand Yethiraj, Valerie Booth

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. 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. 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.

Sina HeraviDepartment of Biochemistry, Memorial University of Newfoundland, St. John's, Newfoundland and Labrador, Canada.ORCID 0000-0002-8435-699X
Jude Vincent Dobbin PowerDepartment of Biochemistry, Memorial University of Newfoundland, St. John's, Newfoundland and Labrador, Canada.
Anand YethirajDepartment of Physics and Physical Oceanography, Memorial University of Newfoundland, St. John's, Newfoundland and Labrador, Canada.ORCID 0000-0003-1293-2801
Valerie BoothDepartment of Biochemistry, Memorial University of Newfoundland, St. John's, Newfoundland and Labrador, Canada.ORCID 0000-0001-9342-9217

Funding

National Research Council of Canada 204040National Research Council of Canada 204115
6 · The paper itself

Abstract

α-synuclein is an intrinsically disordered protein (IDP) whose aggregation in presynaptic neuronal cells is a pathological hallmark of Lewy body formation and Parkinson's disease. This aggregation process is likely affected by the crowded macromolecular cellular environment. In this study, α-synuclein was studied in the presence of both a synthetic crowder, Ficoll70, and a biological crowder composed of lysed cells that better mimics the biocomplexity of the cellular environment.

Indexed as

Intrinsically Disordered ProteinsParkinson Diseasealpha-SynucleinHumansMacromolecular SubstancesProtein Conformationalpha-SynucleinIntrinsically Disordered ProteinsMacromolecular Substancesintrinsically disordered proteinmacromolecular crowdingNMRrelaxationtranslational diffusionα-synuclein

Identifiers

PMID38358134
PMCPMC10868423

What OpenQuestion holds

Textmetadata
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.