ArticlePrion
Reversible monomer-oligomer transition in human prion protein.
Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Experimental NOE, Chemical Shift, and Proline Isomerization Data Provide Detailed Insights into Amelotin Oligomerization.Journal of the American Chemical Society · 2023Article
- Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain.Scientific reports · 2016Article
- Unique Properties of the Rabbit Prion Protein Oligomer.PloS one · 2016Article
- N-terminal domain of prion protein directs its oligomeric association.The Journal of biological chemistry · 2014Article
- Article
- Direct evidence of generation and accumulation of β-sheet-rich prion protein in scrapie-infected neuroblastoma cells with human IgG1 antibody specific for β-form prion protein.The Journal of biological chemistry · 2012Article
- Energy landscape of the prion protein helix 1 probed by metadynamics and NMR.Biophysical journal · 2012Article
- Conformational properties of beta-PrP.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
8 authors.
Funding
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Abstract
The structure and the dissociation reaction of oligomers Pr(Poligo) from reduced human prion huPrP(C)(23-231) have been studied by (1)H-NMR and tryptophan fluorescence spectroscopy at varying pressure, along with circular dichroism and atomic force microscopy. The 1H-NMR and fluorescence spectral feature of the oligomer is consistent with the notion that the N-terminal residues including all seven Trp residues, are free and mobile, while residues 105 approximately 210, comprising the AGAAAAGA motif and S1-Loop-HelixA-Loop-S2-Loop-HelixC, are engaged in intra- and/ or inter-molecular interactions. By increasing pressure to 200 MPa, the oligomers tend to dissociate into monomers which may be identified with PrP(C*), a rare metastable form of PrP(C) stabilized at high pressure (Kachel et al., BMC Struct Biol 6:16). The results strongly suggest that the oligomeric form PrP(oligo) is in dynamic equilibrium with the monomeric forms via PrP(C*), namely huPrP(C)[left arrow over right arrow]huPrP(C*)[left arrow over right arrow]huPrP(oligo).
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Registered trials
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