Structural rearrangements at physiological pH: nuclear magnetic resonance insights from the V210I human prion protein mutant
A major focus in prion structural biology studies is unraveling the molecular mechanism
leading to the structural conversion of PrPC to its pathological form, PrPSc. In our recent …
leading to the structural conversion of PrPC to its pathological form, PrPSc. In our recent …
Toward the molecular basis of inherited prion diseases: NMR structure of the human prion protein with V210I mutation
The development of transmissible spongiform encephalopathies (TSEs) is associated with
the conversion of the cellular prion protein (PrPC) into a misfolded, pathogenic isoform …
the conversion of the cellular prion protein (PrPC) into a misfolded, pathogenic isoform …
NMR structural studies of human cellular prion proteins
Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal
neurodegenerative disorders associated with the conformational conversion of the cellular …
neurodegenerative disorders associated with the conformational conversion of the cellular …
Probing early misfolding events in prion protein mutants by NMR spectroscopy
The post-translational conversion of the ubiquitously expressed cellular form of the prion
protein, PrPC, into its misfolded and pathogenic isoform, known as prion or PrPSc, plays a …
protein, PrPC, into its misfolded and pathogenic isoform, known as prion or PrPSc, plays a …
The H187R Mutation of the Human Prion Protein Induces Conversion of Recombinant Prion Protein to the PrPSc-like Form
LLP Hosszu, MH Tattum, S Jones, CR Trevitt… - Biochemistry, 2010 - ACS Publications
Prion diseases are associated with a conformational switch in the prion protein (PrP) from its
normal cellular form (denoted PrPC) to a disease-associated “scrapie” form (PrPSc). A …
normal cellular form (denoted PrPC) to a disease-associated “scrapie” form (PrPSc). A …
NMR characterization of the pH 4 β-intermediate of the prion protein: the N-terminal half of the protein remains unstructured and retains a high degree of flexibility
DBD O'Sullivan, CE Jones, SR Abdelraheim… - Biochemical …, 2007 - portlandpress.com
Prion diseases are associated with the misfolding of the PrP (prion protein) from a largely α-
helical isoform to a β-sheet-rich oligomer. CD has shown that lowering the pH to 4 under …
helical isoform to a β-sheet-rich oligomer. CD has shown that lowering the pH to 4 under …
Disulfide-crosslink scanning reveals prion–induced conformational changes and prion strain–specific structures of the pathological prion protein PrPSc
Y Taguchi, L Lu, C Marrero-Winkens, H Otaki… - Journal of Biological …, 2018 - ASBMB
Prions are composed solely of the pathological isoform (PrP Sc) of the normal cellular prion
protein (PrP C). Identification of different PrP Sc structures is crucially important for …
protein (PrP C). Identification of different PrP Sc structures is crucially important for …
CD and NMR studies of prion protein (PrP) helix 1: novel implications for its role in the PrPC→ PrPSc conversion process
The conversion of prion helix 1 from an α-helical into an extended conformation is generally
assumed to be an essential step in the conversion of the cellular isoform PrP C of the prion …
assumed to be an essential step in the conversion of the cellular isoform PrP C of the prion …
Influence of pH on NMR structure and stability of the human prion protein globular domain
L Calzolai, R Zahn - Journal of Biological Chemistry, 2003 - ASBMB
The NMR structure of the globular domain of the human prion protein (hPrP) with residues
121–230 at pH 7.0 shows the same global fold as the previously published structure …
121–230 at pH 7.0 shows the same global fold as the previously published structure …
Locally Disordered Conformer of the Hamster Prion Protein: A Crucial Intermediate to PrPSc?
K Kuwata, H Li, H Yamada, G Legname… - Biochemistry, 2002 - ACS Publications
A crucial step for transformation of the normal cellular isoform of the prion protein (PrPC) to
the infectious prion protein (PrPSc) is thought to entail a previously uncharacterized …
the infectious prion protein (PrPSc) is thought to entail a previously uncharacterized …