ArticleFEMS microbiology letters2017
Autophagy participates in the unfolded protein response in Toxoplasma gondii.
Article in FEMS microbiology letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
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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.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Article
- The roles and mechanisms of endoplasmic reticulum stress-mediated autophagy in animal viral infections.Veterinary research · 2024Review
- Autophagy in protists and their hosts: When, how and why?Autophagy reports · 2023Article
- Glycosylation Analysis of Feline Small Intestine FollowingAnimals : an open access journal from MDPI · 2022Article
- Article
- Different Drugs, Same End: Ultrastructural Hallmarks of Autophagy in Pathogenic Protozoa.Frontiers in microbiology · 2022Review
- The Autophagy Machinery in Human-Parasitic Protists; Diverse Functions for Universally Conserved Proteins.Cells · 2021Review
- 17-AAG-Induced Activation of the Autophagic Pathway inMicroorganisms · 2021Article
- Endoplasmic Reticulum Stress, a Target for Drug Design and Drug Resistance in Parasitosis.Frontiers in microbiology · 2021Review
- Ubiquitin-Like Modifiers: Emerging Regulators of Protozoan Parasites.Biomolecules · 2020Review
- Phosphorylation of eukaryotic initiation factor-2α in response to endoplasmic reticulum and nitrosative stress in the human protozoan parasite, Entamoeba histolytica.Molecular and biochemical parasitology · 2019Article
- Characterisation of two Toxoplasma PROPPINs homologous to Atg18/WIPI suggests they have evolved distinct specialised functions.PloS one · 2018Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Environmental and genetic perturbations of endoplasmic reticulum (ER) function can lead to the accumulation of unfolded proteins. In these conditions, eukaryotic cells can activate a complex signaling network called the unfolded protein response (UPR) to reduce ER stress and restore cellular homeostasis. Autophagy, a degradation and recycling process, is part of this response. The parasitic protist Toxoplasma gondii is known to be able to activate the UPR upon ER stress, and we now show that this pathway leads to autophagy activation, supporting the idea of a regulated function for canonical autophagy as part of an integrated stress response in the parasites.
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Registered trials
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.