Evidence map›Paper›PMID 32915553›Full record

ArticleJournal of the American Chemical Society2020

AggFluor: Fluorogenic Toolbox Enables Direct Visualization of the Multi-Step Protein Aggregation Process in Live Cells.

Charles H Wolstenholme, Hang Hu, Songtao Ye, Brian E Funk, Divya Jain, Chia-Heng Hsiung, Gang Ning, Yu Liu, Xiaosong Li, Xin Zhang

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

33 citing papers in PubMed, 145 citations in OpenAlex.

  1. A New Soaking Protocol to Live StainbioRxiv : the preprint server for biology · 2026
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  20. Monitoring amyloid aggregationChemical science · 2023
    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

10 authors at 2 institutions in 1 country.

Charles H Wolstenholme
Hang Hu
Songtao Ye
Brian E Funk
Divya Jain
Chia-Heng Hsiung
Gang Ning
Yu Liu
Pennsylvania State University · USUniversity of Washington · US

Funding

Chemically Probing and Regulating Misfolding and Aggregation of Intrinsically Disordered Proteins in Membraneless OrganellesR35GM133484 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI ZHANG, XIN · 2019 to 2021
$1.2M
NIGMS NIH HHS R35 GM133484
6 · The paper itself

Abstract

Aberrantly processed or mutant proteins misfold and assemble into a variety of soluble oligomers and insoluble aggregates, a process that is associated with an increasing number of diseases that are not curable or manageable. Herein, we present a chemical toolbox, AggFluor, that allows for live cell imaging and differentiation of complex aggregated conformations in live cells. Based on the chromophore core of green fluorescent proteins, AggFluor is comprised of a series of molecular rotor fluorophores that span a wide range of viscosity sensitivity. As a result, these compounds exhibit differential turn-on fluorescence when incorporated in either soluble oligomers or insoluble aggregates. This feature allows us to develop, for the first time, a dual-color imaging strategy to distinguish unfolded protein oligomers from insoluble aggregates in live cells. Furthermore, we have demonstrated how small molecule proteostasis regulators can drive formation and disassembly of protein aggregates in both conformational states. In summary, AggFluor is the first set of rationally designed molecular rotor fluorophores that evenly cover a wide range of viscosity sensitivities. This set of fluorescent probes not only change the status quo of current imaging methods to visualize protein aggregation in live cells but also can be generally applied to study other biological processes that involve local viscosity changes with temporal and spatial resolutions.

Indexed as

Fluorescent DyesGreen Fluorescent ProteinsHEK293 CellsHumansOptical ImagingProtein AggregatesProtein ConformationProtein FoldingSolventsSpectrometry, FluorescenceViscosityFluorescent DyesGreen Fluorescent ProteinsProtein AggregatesSolvents

Identifiers

PMID32915553
PMCPMC8088285
OpenAlexW3086592412

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.