ReviewProtein engineering, design & selection : PEDS2009
The consequences of pathogenic mutations to the human prion protein.
Review in Protein engineering, design & selection : PEDS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
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.
Who cites it
28 citing papers in PubMed.
- Article
- Homodimeric complexes of the 90-231 human prion: a multilayered computational study based on FMO/GRID-DRY approach.Journal of molecular modeling · 2022Article
- Destabilization of polar interactions in the prion protein triggers misfolding and oligomerization.Protein science : a publication of the Protein Society · 2021Article
- Expression and Functional Study of Single Mutations of Carbonic Anhydrase 8 in Neuronal Cells.Cellular and molecular neurobiology · 2021Article
- Structural Determinants of the Prion Protein N-Terminus and Its Adducts with Copper Ions.International journal of molecular sciences · 2018Review
- Glycosylation Significantly Inhibits the Aggregation of Human Prion Protein and Decreases Its Cytotoxicity.Scientific reports · 2018Article
- Prion disease.Handbook of clinical neurology · 2018Review
- Simulations of membrane-bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding.Journal of neurochemistry · 2017Article
- Genetic prion disease: Experience of a rapidly progressive dementia center in the United States and a review of the literature.American journal of medical genetics. Part B, Neuropsychiatric genetics : the official publication of the International Society of Psychiatric Genetics · 2017Review
- Selective vulnerability to neurodegenerative disease: the curious case of Prion Protein.Disease models & mechanisms · 2014Review
- Introducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitro.PloS one · 2013Article
- Relationships between clinicopathological features and cerebrospinal fluid biomarkers in Japanese patients with genetic prion diseases.PloS one · 2013Article
- Biology and genetics of prions causing neurodegeneration.Annual review of genetics · 2013Review
- Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions.International journal of cell biology · 2013Review
- Disease-associated mutations in the prion protein impair laminin-induced process outgrowth and survival.The Journal of biological chemistry · 2012Article
- Probing the role of structural features of mouse PrP in yeast by expression as Sup35-PrP fusions.Prion · 2012Review
- Direct observation of multiple misfolding pathways in a single prion protein molecule.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The landscape of the prion protein's structural response to mutation revealed by principal component analysis of multiple NMR ensembles.PLoS computational biology · 2012Article
- Role of prion protein aggregation in neurotoxicity.International journal of molecular sciences · 2012Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Prion diseases, in which the conformational transition of the native prion protein (PrP) to a misfolded form causes aggregation and subsequent neurodegeneration, have fascinated the scientific community as this transmissible disease appears to be purely protein-based. Disease can arise due to genetic factors only. At least 30 single point mutations have been indicated to cause disease in humans. Somehow, these mutations must influence the stability, processing and/or cellular interactions of PrP, such that aggregation can occur and disease develops. In this review, the current evidence for such effects of single point mutations is discussed, indicating that PrP can be affected in many different ways, although questions remain about the mechanism by which mutations cause disease.
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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.