ArticleThe Journal of biological chemistry2012
Failure of prion protein oxidative folding guides the formation of toxic transmembrane forms.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 6 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Crosstalk Between Oxidative Stress and Endoplasmic Reticulum (ER) Stress in Endothelial Dysfunction and Aberrant Angiogenesis Associated With Diabetes: A Focus on the Protective Roles of Heme Oxygenase (HO)-1.Frontiers in physiology · 2019Review
- Protective effects of Danshen injection against erectile dysfunction via suppression of endoplasmic reticulum stress activation in a streptozotocin-induced diabetic rat model.BMC complementary and alternative medicine · 2018Article
- Endoplasmic Reticulum Stress, NRF2 Signalling and Cardiovascular Diseases in a Nutshell.Current atherosclerosis reports · 2017Review
- PrP charge structure encodes interdomain interactions.Scientific reports · 2015Article
- Polar substitutions in helix 3 of the prion protein produce transmembrane isoforms that disturb vesicle trafficking.Human molecular genetics · 2013Article
- An involvement of oxidative stress in endoplasmic reticulum stress and its associated diseases.International journal of molecular sciences · 2012Review
Corrections and comments
- Retraction · 2017-12-08Duplication of/in Image · Manipulation of Images ·
- Retracted
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The mechanism by which pathogenic mutations in the globular domain of the cellular prion protein (PrP(C)) increase the likelihood of misfolding and predispose to diseases is not yet known. Differences in the evidences provided by structural and metabolic studies of these mutants suggest that in vivo folding could be playing an essential role in their pathogenesis. To address this role, here we use the single or combined M206S and M213S artificial mutants causing labile folds and express them in cells. We find that these mutants are highly toxic, fold as transmembrane PrP, and lack the intramolecular disulfide bond. When the mutations are placed in a chain with impeded transmembrane PrP formation, toxicity is rescued. These results suggest that oxidative folding impairment, as on aging, can be fundamental for the genesis of intracellular neurotoxic intermediates key in prion neurodegenerations.
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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.