Evidence map›Paper›PMID 33454006›Full record

ArticleThe Journal of biological chemistry2020

AggreCount: an unbiased image analysis tool for identifying and quantifying cellular aggregates in a spatially defined manner.

Jacob Aaron Klickstein, Sirisha Mukkavalli, Malavika Raman

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 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
–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

33 citing papers in PubMed.

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  5. ACS omega · 2025
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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

3 authors.

Jacob Aaron KlicksteinDepartment of Developmental Molecular and Chemical Biology, Tufts University School of Medicine, Boston, Massachusetts, USA.
Sirisha MukkavalliDepartment of Developmental Molecular and Chemical Biology, Tufts University School of Medicine, Boston, Massachusetts, USA.
Malavika RamanDepartment of Developmental Molecular and Chemical Biology, Tufts University School of Medicine, Boston, Massachusetts, USA. Electronic address: malavika.raman@tufts.edu.

Funding

“Regulation of Protein Quality Control by the VCP AAA-ATPase”R01GM127557 · NIGMS · TUFTS UNIVERSITY BOSTON · PI Malavika Raman · 2018 to 2026
$3.5M
NIGMS NIH HHS R01 GM127557
6 · The paper itself

Abstract

Protein quality control is maintained by a number of integrated cellular pathways that monitor the folding and functionality of the cellular proteome. Defects in these pathways lead to the accumulation of misfolded or faulty proteins that may become insoluble and aggregate over time. Protein aggregates significantly contribute to the development of a number of human diseases such as amyotrophic lateral sclerosis, Huntington's disease, and Alzheimer's disease. In vitro, imaging-based, cellular studies have defined key biomolecular components that recognize and clear aggregates; however, no unifying method is available to quantify cellular aggregates, limiting our ability to reproducibly and accurately quantify these structures. Here we describe an ImageJ macro called AggreCount to identify and measure protein aggregates in cells. AggreCount is designed to be intuitive, easy to use, and customizable for different types of aggregates observed in cells. Minimal experience in coding is required to utilize the script. Based on a user-defined image, AggreCount will report a number of metrics: (i) total number of cellular aggregates, (ii) percentage of cells with aggregates, (iii) aggregates per cell, (iv) area of aggregates, and (v) localization of aggregates (cytosol, perinuclear, or nuclear). A data table of aggregate information on a per cell basis, as well as a summary table, is provided for further data analysis. We demonstrate the versatility of AggreCount by analyzing a number of different cellular aggregates including aggresomes, stress granules, and inclusion bodies caused by huntingtin polyglutamine expansion.

Indexed as

Protein AggregatesAdaptor Proteins, Signal TransducingAmyotrophic Lateral SclerosisArsenitesCytoplasmic GranulesFluorescent DyesHeLa CellsHumansHuntington DiseaseImage Processing, Computer-AssistedInclusion BodiesMicroscopy, FluorescenceProteinsPuromycinSodium CompoundsAdaptor Proteins, Signal TransducingArsenitesFluorescent DyesProtein AggregatesProteinsPuromycinsodium arseniteSodium CompoundsUBXN1 protein, humanaggregateaggregationaggresomeamyotrophic lateral sclerosis (ALS) (Lou Gehrig disease)Huntington diseaseimage-based analysisImageJinclusion bodymicroscopic imagingmisfolded proteinp97/valosin-containing proteinpolyQ inclusion bodypolyubiquitin chainprotein aggregationprotein misfolding p97/valosin-containing proteinprotein quality controlproteostasisstress granuleubiquitin

Identifiers

PMID33454006
PMCPMC7762942

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Registered trials

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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.