ArticlePrion
Prion pathogenesis is independent of caspase-12.
Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 44 citations in OpenAlex.
- Therapeutic Assay with the Non-toxic C-Terminal Fragment of Tetanus Toxin (TTC) in Transgenic Murine Models of Prion Disease.Molecular neurobiology · 2021Article
- Prion-Associated Neurodegeneration Causes Both Endoplasmic Reticulum Stress and Proteasome Impairment in a Murine Model of Spontaneous Disease.International journal of molecular sciences · 2021Article
- What Is Our Current Understanding of PrPPathogens (Basel, Switzerland) · 2017Review
- The Endoplasmic Reticulum Chaperone GRP78/BiP Modulates Prion Propagation in vitro and in vivo.Scientific reports · 2017Article
- The Endoplasmic Reticulum Unfolded Protein Response in Neurodegenerative Disorders and Its Potential Therapeutic Significance.Frontiers in molecular neuroscience · 2017Review
- Unfolded Protein Response and Macroautophagy in Alzheimer's, Parkinson's and Prion Diseases.Molecules (Basel, Switzerland) · 2015Review
- The Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein.The Journal of biological chemistry · 2015Article
- Prion infections and anti-PrP antibodies trigger converging neurotoxic pathways.PLoS pathogens · 2015Article
- Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases.Nature reviews. Neuroscience · 2014Review
- Endoplasmic reticulum and the unfolded protein response: dynamics and metabolic integration.International review of cell and molecular biology · 2013Review
- Synaptic dysfunction in prion diseases: a trafficking problem?International journal of cell biology · 2013Review
- Article
- Abnormal calcium homeostasis and protein folding stress at the ER: A common factor in familial and infectious prion disorders.Communicative & integrative biology · 2011Article
- Article
- The intricate mechanisms of neurodegeneration in prion diseases.Trends in molecular medicine · 2011Review
- Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress.PloS one · 2010Article
- Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Progress in neurobiology · 2010Review
- Endoplasmic reticulum stress, inflammation, and perinatal brain damage.Pediatric research · 2009Review
- Cytoplasmic prion protein induces forebrain neurotoxicity.Biochimica et biophysica acta · 2009Article
- Heat shock factor 1 regulates lifespan as distinct from disease onset in prion disease.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 6 institutions in 2 countries.
Funding
Abstract
The pathogenic mechanism(s) underlying neurodegenerative diseases associated with protein misfolding is unclear. Several studies have implicated ER stress pathways in neurodegenerative conditions, including prion disease, amyotrophic lateral sclerosis, Alzheimer's disease and many others. The ER stress response and upregulation of ER stress-responsive chaperones is observed in the brains of patients affected with Creutzfeldt-Jacob disease and in mouse models of prion diseases. In particular, the processing of caspase-12, an ER-localized caspase, correlates with neuronal cell death in prion disease. However, the contribution of caspase-12 to neurodegeneration has not been directly addressed in vivo. We confirm that ER stress is induced and that caspase-12 is proteolytically processed in a murine model of infectious prion disease. To address the causality of caspase-12 in mediating infectious prion pathogenesis, we inoculated mice deficient in caspase-12 with prions. The survival, behavior, pathology and accumulation of proteinase K-resistant PrP are indistinguishable between caspase-12 knockout and control mice, suggesting that caspase-12 is not necessary for mediating the neurotoxic effects of prion protein misfolding.
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What OpenQuestion holds
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.