ArticlePloS one2012
Structural organization of mammalian prions as probed by limited proteolysis.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- Spontaneous generation of diverse recombinant prion strains: sulfated glycan cofactors facilitate strain emergence but do not determine specific strain properties.Acta neuropathologica communications · 2025Article
- The pre-induction temperature affects recombinant HuGM-CSF aggregation in thermoinducible Escherichia coli.Applied microbiology and biotechnology · 2022Article
- Combination of structure-based virtual screening, molecular docking and molecular dynamics approaches for the discovery of anti-prion fibril flavonoids.Frontiers in molecular biosciences · 2022Article
- Structure of prion β-oligomers as determined by short-distance crosslinking constraint-guided discrete molecular dynamics simulations.Proteomics · 2021Article
- Quantifying the Role of Lysine in Prion Replication by Nano-LC Mass Spectrometry and Bioassay.Frontiers in bioengineering and biotechnology · 2020Article
- Development of a new largely scalable in vitro prion propagation method for the production of infectious recombinant prions for high resolution structural studies.PLoS pathogens · 2019Article
- Full atomistic model of prion structure and conversion.PLoS pathogens · 2019Article
- Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants.International journal of molecular sciences · 2019Article
- Article
- Comparing the Folds of Prions and Other Pathogenic Amyloids.Pathogens (Basel, Switzerland) · 2018Review
- The Structure of PrPPathogens (Basel, Switzerland) · 2018Review
- Recombinant PrPSc shares structural features with brain-derived PrPSc: Insights from limited proteolysis.PLoS pathogens · 2018Article
- Generation of a new infectious recombinant prion: a model to understand Gerstmann-Sträussler-Scheinker syndrome.Scientific reports · 2017Article
- Structural Biology of PrP Prions.Cold Spring Harbor perspectives in medicine · 2017Review
- The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy.PLoS pathogens · 2016Article
- N(ε)-Carboxymethyl Modification of Lysine Residues in Pathogenic Prion Isoforms.Molecular neurobiology · 2016Article
- Article
- The diversity and relationship of prion protein self-replicating states.Virus research · 2015Review
- Techniques to elucidate the conformation of prions.World journal of biological chemistry · 2015Review
- The structure of human prions: from biology to structural models-considerations and pitfalls.Viruses · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Elucidation of the structure of PrP(Sc) continues to be one major challenge in prion research. The mechanism of propagation of these infectious agents will not be understood until their structure is solved. Given that high resolution techniques such as NMR or X-ray crystallography cannot be used, a number of lower resolution analytical approaches have been attempted. Thus, limited proteolysis has been successfully used to pinpoint flexible regions within prion multimers (PrP(Sc)). However, the presence of covalently attached sugar antennae and glycosylphosphatidylinositol (GPI) moieties makes mass spectrometry-based analysis impractical. In order to surmount these difficulties we analyzed PrP(Sc) from transgenic mice expressing prion protein (PrP) lacking the GPI membrane anchor. Such animals produce prions that are devoid of the GPI anchor and sugar antennae, and, thereby, permit the detection and location of flexible, proteinase K (PK) susceptible regions by Western blot and mass spectrometry-based analysis. GPI-less PrP(Sc) samples were digested with PK. PK-resistant peptides were identified, and found to correspond to molecules cleaved at positions 81, 85, 89, 116, 118, 133, 134, 141, 152, 153, 162, 169 and 179. The first 10 peptides (to position 153), match very well with PK cleavage sites we previously identified in wild type PrP(Sc). These results reinforce the hypothesis that the structure of PrP(Sc) consists of a series of highly PK-resistant β-sheet strands connected by short flexible PK-sensitive loops and turns. A sizeable C-terminal stretch of PrP(Sc) is highly resistant to PK and therefore perhaps also contains β-sheet secondary structure.
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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.