Evidence map›Paper›PMID 32489651›Full record

ArticleRSC advances2020

A luminescence-based assay for monitoring changes in alpha-synuclein aggregation in living cells.

Travis J Nelson, Tiffany Truong, BaoLong Truong, Camden V Bilyeu, Jia Zhao, Cliff I Stains

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. 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

6 authors.

Travis J NelsonDepartment of Chemistry, University of Nebraska - Lincoln, Lincoln, NE 68588, USA.
Tiffany TruongDepartment of Chemistry, University of Nebraska - Lincoln, Lincoln, NE 68588, USA.
BaoLong TruongDepartment of Chemistry, University of Nebraska - Lincoln, Lincoln, NE 68588, USA.
Camden V BilyeuDepartment of Chemistry, University of Nebraska - Lincoln, Lincoln, NE 68588, USA.
Jia ZhaoDepartment of Chemistry, University of Nebraska - Lincoln, Lincoln, NE 68588, USA.
Cliff I StainsDepartment of Chemistry, University of Nebraska - Lincoln, Lincoln, NE 68588, USA.ORCID 0000-0002-3165-4539

Funding

Chemical Approaches for Interrogating Fundamental Biomedical ProcessesR35GM119751 · NIGMS · UNIVERSITY OF VIRGINIA · PI STAINS, CLIFF I · 2016 to 2020
$1.8M
NIGMS NIH HHS R35 GM119751
6 · The paper itself

Abstract

Parkinson's disease is characterized by the accumulation of protein aggregates in the brain, termed Lewy bodies. Lewy bodies are predominantly composed of α-synuclein and mutations that increase the aggregation potential of α-synuclein have been associated with early on-set disease. Assays capable of reporting on the solubility of α-synuclein in living cells could provide a means to interrogate the influence of mutations on aggregation as well as identify small molecules capable of modulating the aggregation of α-synuclein. Herein, we repurpose our previously reported self-assembling NanoLuc luciferase fragments to engineer a platform for detecting α-synuclein solubility in living cells. This new assay is capable of reporting on changes in α-synuclein solubility caused by disease-relevant mutations as well as inhibitors of aggregation. In the long term, this new assay platform provides a means to investigate the influence of mutations on α-synuclein solubility as well as identify potential tool compounds capable of modulating α-synuclein aggregation.

Identifiers

PMID32489651
PMCPMC7266166

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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.