The biological function of the prion protein: a cell surface scaffold of signaling modules
R Linden - Frontiers in molecular neuroscience, 2017 - frontiersin.org
The prion glycoprotein (PrPC) is mostly located at the cell surface, tethered to the plasma
membrane through a glycosyl-phosphatydil inositol (GPI) anchor. Misfolding of PrPC is …
membrane through a glycosyl-phosphatydil inositol (GPI) anchor. Misfolding of PrPC is …
Molecular biology and pathology of prion strains in sporadic human prion diseases
P Gambetti, I Cali, S Notari, Q Kong, WQ Zou… - Acta …, 2011 - Springer
Prion diseases are believed to propagate by the mechanism involving self-perpetuating
conformational conversion of the normal form of the prion protein, PrP C, to the misfolded …
conformational conversion of the normal form of the prion protein, PrP C, to the misfolded …
Influence of disease-causing mutations on protein structural networks
VM Prabantu, N Naveenkumar… - Frontiers in Molecular …, 2021 - frontiersin.org
The interactions between residues in a protein tertiary structure can be studied effectively
using the approach of protein structure network (PSN). A PSN is a node-edge representation …
using the approach of protein structure network (PSN). A PSN is a node-edge representation …
Fatal familial insomnia and sporadic fatal insomnia
L Cracco, BS Appleby, P Gambetti - Handbook of clinical neurology, 2018 - Elsevier
Fatal familial insomnia (FFI) and sporadic fatal insomnia (sFI), or thalamic form of sporadic
Creutzfeldt–Jakob disease MM2 (sCJDMM2T), are prion diseases originally named and …
Creutzfeldt–Jakob disease MM2 (sCJDMM2T), are prion diseases originally named and …
Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding
MW van der Kamp, V Daggett - Journal of molecular biology, 2010 - Elsevier
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding
and aggregation of the prion protein PrP. These diseases can be hereditary in humans and …
and aggregation of the prion protein PrP. These diseases can be hereditary in humans and …
Zinc drives a tertiary fold in the prion protein with familial disease mutation sites at the interface
AR Spevacek, EGB Evans, JL Miller, HC Meyer… - Structure, 2013 - cell.com
The cellular prion protein PrP C consists of two domains—a flexible N-terminal domain,
which participates in copper and zinc regulation, and a largely helical C-terminal domain …
which participates in copper and zinc regulation, and a largely helical C-terminal domain …
Structures of pathological and functional amyloids and prions, a solid-state NMR perspective
Infectious proteins or prions are a remarkable class of pathogens, where pathogenicity and
infectious state correspond to conformational transition of a protein fold. The conformational …
infectious state correspond to conformational transition of a protein fold. The conformational …
MAPT mutations associated with familial tauopathies lead to formation of conformationally distinct oligomers that have cross‐seeding ability
The microtubule associated protein, tau, is implicated in a multitude of neurodegenerative
disorders that are collectively termed as tauopathies. These disorders are characterized by …
disorders that are collectively termed as tauopathies. These disorders are characterized by …
Mechanism of misfolding of the human prion protein revealed by a pathological mutation
M Sanz-Hernández, JD Barritt… - Proceedings of the …, 2021 - National Acad Sciences
The misfolding and aggregation of the human prion protein (PrP) is associated with
transmissible spongiform encephalopathies (TSEs). Intermediate conformations forming …
transmissible spongiform encephalopathies (TSEs). Intermediate conformations forming …
Transgenic fatal familial insomnia mice indicate prion infectivity-independent mechanisms of pathogenesis and phenotypic expression of disease
I Bouybayoune, S Mantovani, F Del Gallo… - PLoS …, 2015 - journals.plos.org
Fatal familial insomnia (FFI) and a genetic form of Creutzfeldt-Jakob disease (CJD178) are
clinically different prion disorders linked to the D178N prion protein (PrP) mutation. The …
clinically different prion disorders linked to the D178N prion protein (PrP) mutation. The …