ArticleThe Journal of biological chemistry2009
Conformational properties of beta-PrP.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 37 citations in OpenAlex.
- The G127V variant of the prion protein interferes with dimer formation in vitro but not in cellulo.Scientific reports · 2021Article
- The First Report of the Prion Protein Gene (Genes · 2021Article
- Structural features distinguishing infectious ex vivo mammalian prions from non-infectious fibrillar assemblies generated in vitro.Scientific reports · 2019Article
- Role of the Disulfide Bond in Prion Protein Amyloid Formation: A Thermodynamic and Kinetic Analysis.Biophysical journal · 2018Article
- Prion protein dynamics before aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain.Scientific reports · 2016Article
- Ex vivo mammalian prions are formed of paired double helical prion protein fibrils.Open biology · 2016Article
- Article
- N-terminal domain of prion protein directs its oligomeric association.The Journal of biological chemistry · 2014Article
- Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition.Biochemistry · 2013Article
- Energy landscape of the prion protein helix 1 probed by metadynamics and NMR.Biophysical journal · 2012Article
- Structural analysis of prion proteins by means of drift cell and traveling wave ion mobility mass spectrometry.Journal of the American Society for Mass Spectrometry · 2010Article
- Prion protein self-peptides modulate prion interactions and conversion.BMC biochemistry · 2009Article
- Article
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Authors and funding
9 authors at 5 institutions in 1 country.
Funding
Abstract
Prion propagation involves a conformational transition of the cellular form of prion protein (PrPC) to a disease-specific isomer (PrPSc), shifting from a predominantly alpha-helical conformation to one dominated by beta-sheet structure. This conformational transition is of critical importance in understanding the molecular basis for prion disease. Here, we elucidate the conformational properties of a disulfide-reduced fragment of human PrP spanning residues 91-231 under acidic conditions, using a combination of heteronuclear NMR, analytical ultracentrifugation, and circular dichroism. We find that this form of the protein, which similarly to PrPSc, is a potent inhibitor of the 26 S proteasome, assembles into soluble oligomers that have significant beta-sheet content. The monomeric precursor to these oligomers exhibits many of the characteristics of a molten globule intermediate with some helical character in regions that form helices I and III in the PrPC conformation, whereas helix II exhibits little evidence for adopting a helical conformation, suggesting that this region is a likely source of interaction within the initial phases of the transformation to a beta-rich conformation. This precursor state is almost as compact as the folded PrPC structure and, as it assembles, only residues 126-227 are immobilized within the oligomeric structure, leaving the remainder in a mobile, random-coil state.
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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.