Evidence map›Paper›PMID 26818841›Full record

ArticleJournal of cell science2016

Distinguishing aggregate formation and aggregate clearance using cell-based assays.

Evelien Eenjes, Joanna M Dragich, Harm H Kampinga, Ai Yamamoto

Open access · bronzeAbstract readEvaluation Study
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
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  12. Autophagy Modulation as a Treatment of Amyloid Diseases.Molecules (Basel, Switzerland) · 2019
    Review
  13. Article
  14. A role for autophagy in Huntington's disease.Neurobiology of disease · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. 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 at 2 institutions in 2 countries.

Evelien EenjesColumbia University, Department of Neurology, New York, NY 10032, USA University Medical Center Groningen, University of Groningen, Department of Cell Biology, Groningen 9713, The Netherlands.
Joanna M DragichColumbia University, Department of Neurology, New York, NY 10032, USA.
Harm H KampingaUniversity Medical Center Groningen, University of Groningen, Department of Cell Biology, Groningen 9713, The Netherlands.
Ai YamamotoColumbia University, Department of Neurology, New York, NY 10032, USA Columbia University, Department of Pathology and Cell Biology, New York, NY 10032, USA ay46@cumc.columbia.edu.
Columbia University · USUniversity Medical Center Groningen · NL

Funding

Modulating selective autophagy to modify Huntington's diseaseR01NS077111 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Ai Yamamoto · 2012 to 2026
$4.3M
Autophagy and NeurodegenerationR01NS063973 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI MELIA, THOMAS JAMES, YAMAMOTO, AI · 2008 to 2019
$3.8M
NINDS NIH HHS R01 NS063973NINDS NIH HHS R01 NS077111NINDS NIH HHS R01NS077111
6 · The paper itself

Abstract

The accumulation of ubiquitylated proteinaceous inclusions represents a complex process, reflecting the disequilibrium between aggregate formation and aggregate clearance. Although decreasing aggregate formation or augmenting aggregate clearance will ultimately lead to a diminished aggregate burden, in terms of disease pathogenesis, the different approaches can have distinct outcomes. Using a novel cell-based assay that can distinguish newly formed versus preformed inclusions, we demonstrate that two proteins previously implicated in the autophagic clearance of expanded polyglutamine inclusions, HspB7 and Alfy (also known as WDFY3), actually affect very distinct cellular processes to affect aggregate burden. Using this cell-based assay, we also establish that constitutive expression of the aggregation-prone protein can measurably slow the elimination of protein aggregates, given that not all aggregates appear to be available for degradation. This new assay can therefore not only determine at what step a modifier might influence aggregate burden, but also can be used to provide new insights into how protein aggregates are targeted for degradation.

Indexed as

Protein AggregatesAdaptor Proteins, Signal TransducingAnimalsAutophagyAutophagy-Related ProteinsBiochemistryHeLa CellsHSP27 Heat-Shock ProteinsHumansInclusion BodiesMembrane ProteinsMiceProteolysisTranscription FactorsAdaptor Proteins, Signal TransducingAutophagy-Related ProteinsHSP27 Heat-Shock ProteinsHSPB7 protein, humanMembrane ProteinsProtein AggregatesTranscription FactorsWDFY3 protein, humanAutophagyChaperonePolyglutamine proteinProtein aggregation

Identifiers

PMID26818841
PMCPMC4813294
OpenAlexW2279862680

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.