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 …
The protease-sensitive N-terminal polybasic region of prion protein modulates its conversion to the pathogenic prion conformer
X Zhang, YH Pan, Y Chen, C Pan, J Ma, C Yuan… - Journal of Biological …, 2021 - ASBMB
Conversion of normal prion protein (PrP C) to the pathogenic PrP Sc conformer is central to
prion diseases such as Creutzfeldt–Jakob disease and scrapie; however, the detailed …
prion diseases such as Creutzfeldt–Jakob disease and scrapie; however, the detailed …
Toward molecular dissection of PrPC-PrPSc interactions
L Solforosi, A Bellon, M Schaller, JT Cruite… - Journal of Biological …, 2007 - ASBMB
Direct interaction between endogenous cellular prion protein (PrP C) and misfolded,
disease-associated (PrP Sc) conformers is a key event in prion propagation, which precedes …
disease-associated (PrP Sc) conformers is a key event in prion propagation, which precedes …
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 …
The Octarepeat Region of the Prion Protein Is Conformationally Altered in PrPSc
AY Yam, CM Gao, X Wang, P Wu, D Peretz - PloS one, 2010 - journals.plos.org
Background Prion diseases are fatal neurodegenerative disorders characterized by
misfolding and aggregation of the normal prion protein PrPC. Little is known about the …
misfolding and aggregation of the normal prion protein PrPC. Little is known about the …
Identifying key components of the PrPC-PrPSc replicative interface
GC Abalos, JT Cruite, A Bellon, S Hemmers… - Journal of Biological …, 2008 - ASBMB
In prion disease, direct interaction between the cellular prion protein (PrP C) and its
misfolded disease-associated conformer PrP Sc is a crucial, although poorly understood …
misfolded disease-associated conformer PrP Sc is a crucial, although poorly understood …
The polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP
VG Ostapchenko, N Makarava, R Savtchenko… - Journal of molecular …, 2008 - Elsevier
Individual variations in structure and morphology of amyloid fibrils produced from a single
polypeptide are likely to underlie the molecular origin of prion strains and control the …
polypeptide are likely to underlie the molecular origin of prion strains and control the …
PrPSc-Specific Antibody Reveals C-Terminal Conformational Differences between Prion Strains
E Saijo, AG Hughson, GJ Raymond, A Suzuki… - Journal of …, 2016 - Am Soc Microbiol
Understanding the structure of PrPSc and its strain variation has been one of the major
challenges in prion disease biology. To study the strain-dependent conformations of PrPSc …
challenges in prion disease biology. To study the strain-dependent conformations of PrPSc …
Understanding prion structure and conversion
G Spagnolli, JR Requena, E Biasini - Progress in Molecular Biology and …, 2020 - Elsevier
Since their original identification, prions have represented enigmatic agents that defy the
classical concept of genetic inheritance. For almost four decades, the high-resolution …
classical concept of genetic inheritance. For almost four decades, the high-resolution …
[HTML][HTML] The deletion of amino acids 114–121 in the TM1 domain of mouse prion protein stabilizes its conformation but does not affect the overall structure
B Thaa, R Zahn, U Matthey, PMH Kroneck… - … et Biophysica Acta (BBA …, 2008 - Elsevier
A mutant of mouse prion protein (PrPC) carrying a deletion of residues 114–121 (PrPΔ114–
121) has previously been described to lack convertibility into the scrapie-associated isoform …
121) has previously been described to lack convertibility into the scrapie-associated isoform …