Evidence map›Paper›PMID 36594740›Full record

ArticleAutophagy2023

The chaperone-assisted selective autophagy complex dynamics and dysfunctions.

Barbara Tedesco, Leen Vendredy, Vincent Timmerman, Angelo Poletti

Open access · hybridAbstract read
In one paragraph

Article in Autophagy, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
21.7field-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

65 citing papers in PubMed, 101 citations in OpenAlex.

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  14. Links Between Autophagy and Healthy Aging.Journal of molecular biology · 2026
    Review
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  16. Article
  17. Article
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  19. Article
  20. Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026
    Review

5 more citing papers are in PubMed but not listed here.

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.

Barbara TedescoLaboratory of Experimental Biology, Dipartimento di Scienze Farmacologiche e Biomolecolari, Dipartimento di Eccellenza 2018-2027, Università degli studi di Milano, Milan, Italy.ORCID 0000-0002-7077-3696
Leen VendredyPeripheral Neuropathy Research Group, Department of Biomedical Sciences, Institute Born Bunge, University of Antwerp, Antwerpen, Belgium.ORCID 0000-0002-7643-517X
Vincent TimmermanPeripheral Neuropathy Research Group, Department of Biomedical Sciences, Institute Born Bunge, University of Antwerp, Antwerpen, Belgium.ORCID 0000-0002-2162-0933
Angelo PolettiLaboratory of Experimental Biology, Dipartimento di Scienze Farmacologiche e Biomolecolari, Dipartimento di Eccellenza 2018-2027, Università degli studi di Milano, Milan, Italy.ORCID 0000-0002-8883-0468
University of Antwerp · BEUniversity of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Each protein must be synthesized with the correct amino acid sequence, folded into its native structure, and transported to a relevant subcellular location and protein complex. If any of these steps fail, the cell has the capacity to break down aberrant proteins to maintain protein homeostasis (also called proteostasis). All cells possess a set of well-characterized protein quality control systems to minimize protein misfolding and the damage it might cause. Autophagy, a conserved pathway for the degradation of long-lived proteins, aggregates, and damaged organelles, was initially characterized as a bulk degradation pathway. However, it is now clear that autophagy also contributes to intracellular homeostasis by selectively degrading cargo material. One of the pathways involved in the selective removal of damaged and misfolded proteins is chaperone-assisted selective autophagy (CASA). The CASA complex is composed of three main proteins (HSPA, HSPB8 and BAG3), essential to maintain protein homeostasis in muscle and neuronal cells. A failure in the CASA complex, caused by mutations in the respective coding genes, can lead to (cardio)myopathies and neurodegenerative diseases. Here, we summarize our current understanding of the CASA complex and its dynamics. We also briefly discuss how CASA complex proteins are involved in disease and may represent an interesting therapeutic target.

Indexed as

AutophagyNF-E2-Related Factor 2Heat-Shock ProteinsIntracellular Signaling Peptides and ProteinsKelch-Like ECH-Associated Protein 1Molecular ChaperonesUbiquitinsHeat-Shock ProteinsIntracellular Signaling Peptides and ProteinsKelch-Like ECH-Associated Protein 1Molecular ChaperonesNF-E2-Related Factor 2UbiquitinsAggresomeBAG3HSPAHSPB8misfoldingmyopathyneurodegenerative diseasesneuropathyproteostasisSQSTM1STUB1

Identifiers

PMID36594740
PMCPMC10262806
OpenAlexW4313446499

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.