Evidence map›Paper›PMID 26492083›Full record

ArticleACS chemical biology2016

Self-Assembling NanoLuc Luciferase Fragments as Probes for Protein Aggregation in Living Cells.

Jia Zhao, Travis J Nelson, Quyen Vu, Tiffany Truong, Cliff I Stains

Abstract read
In one paragraph

Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 58 citations in OpenAlex.

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  17. Dynamic monitoring of STAT3 activation in live cells using a novel STAT3 Phospho-BRET sensor.American journal of nuclear medicine and molecular imaging · 2019
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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

5 authors at 1 institution in 1 country.

Jia ZhaoDepartment of Chemistry, University of Nebraska-Lincoln , Lincoln, Nebraska 68588, United States.
Travis J NelsonDepartment of Chemistry, University of Nebraska-Lincoln , Lincoln, Nebraska 68588, United States.
Quyen VuDepartment of Chemistry, University of Nebraska-Lincoln , Lincoln, Nebraska 68588, United States.
Tiffany TruongDepartment of Chemistry, University of Nebraska-Lincoln , Lincoln, Nebraska 68588, United States.
Cliff I StainsDepartment of Chemistry, University of Nebraska-Lincoln , Lincoln, Nebraska 68588, United States.
University of Nebraska–Lincoln · US

Funding

Molecular Mechanisms of DiseaseT32GM107001 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI BECKER, DONALD F, BLACK, PAUL N. · 2015 to 2019
$1.0M
NIGMS NIH HHS T32 GM107001NIGMS NIH HHS T32GM107001
6 · The paper itself

Abstract

Given the clear role of protein aggregation in human disease, there is a critical need for assays capable of quantifying protein aggregation in living systems. We hypothesized that the inherently low background and biocompatibility of luminescence signal readouts could provide a potential solution to this problem. Herein, we describe a set of self-assembling NanoLuc luciferase (Nluc) fragments that produce a tunable luminescence readout that is dependent upon the solubility of a target protein fused to the N-terminal Nluc fragment. To demonstrate this approach, we employed this assay in bacteria to assess mutations known to disrupt amyloid-beta (Aβ) aggregation as well as disease-relevant mutations associated with familial Alzheimer's diseases. The luminescence signal from these experiments correlates with the reported aggregation potential of these Aβ mutants and reinforces the increased aggregation potential of disease-relevant mutations in Aβ1-42. To further demonstrate the utility of this approach, we show that the effect of small molecule inhibitors on Aβ aggregation can be monitored using this system. In addition, we demonstrate that aggregation assays can be ported into mammalian cells. Taken together, these results indicate that this platform could be used to rapidly screen for mutations that influence protein aggregation as well as inhibitors of protein aggregation. This method offers a novel, genetically encodable luminescence readout of protein aggregation in living cells.

Indexed as

Amyloid beta-PeptidesAnimalsBacteriaBiological AssayBlotting, WesternCloning, MolecularHumansLuciferasesMiceMutationNIH 3T3 CellsPeptide FragmentsProtein Aggregation, PathologicalProtein BindingAmyloid beta-PeptidesLuciferasesPeptide Fragments

Identifiers

PMID26492083
PMCPMC5110118
OpenAlexW2300242283

What OpenQuestion holds

Textmetadata
LicenceTDM
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.