The prion protein (PrP) has multiple stable isoforms. When PrP misfolds, it aggregates and causes neurological disease and death in mammals. The structure of the non-pathogenic isoform has been determined while the structures of the disease related isoforms are unknown. The nitration labeling patterns of three PrP isoforms with peroxynitrite and tetranitromethane, as detected by mass spectrometry, are reported. Two conserved tyrosine residues (tyrosines 149 and 150) are not labeled by either reagent in the normal cellular form of the prion protein but these residues become reactive after the protein has been converted to one of two aggregated isoforms. Another difference observed is that two other conserved tyrosine residues, 225 and 2...
Fatal neurodegenerative disorders termed transmissible spongiform encephalopathies (TSEs) are associ...
Prion diseases are fatal neurodegenerative disorders caused by an aberrant accumulation of the misfo...
Elucidation of the structure of PrP(Sc) continues to be one major challenge in prion research. The m...
The prion protein (PrP) has multiple stable isoforms. When PrP misfolds, it aggregates and causes n...
The prion protein (PrP) has multiple stable isoforms. When PrP misfolds, it aggregates and causes ne...
Conversion of prion protein (PrP) from its normal, cellular isoform, PrPC, to an infectious, misfold...
Conformational conversion of proteins in disease is likely to be accompanied by molecular surface ex...
The self-association of prion protein (PrP) is a critical step in the pathology of prion diseases. I...
The self-association of prion protein (PrP) is a critical step in the pathology of prion diseases. I...
The aggregation of the prion protein (PrP) plays a key role in the development of prion diseases. In...
Misofolding of mammalian prion proteins (PrP) is believed to be the cause of a group of rare and fat...
Prion diseases are a group of fatal and incurable neurodegenerative disorders of mammals. They uniqu...
The post-translational conversion of the ubiquitously expressed cellular form of the prion protein, ...
Prions cause neurodegenerative diseases for which no cure exists. Despite decades of research activi...
Background: Prion diseases are fatal neurodegenerative disorders that can arise sporadically, be gen...
Fatal neurodegenerative disorders termed transmissible spongiform encephalopathies (TSEs) are associ...
Prion diseases are fatal neurodegenerative disorders caused by an aberrant accumulation of the misfo...
Elucidation of the structure of PrP(Sc) continues to be one major challenge in prion research. The m...
The prion protein (PrP) has multiple stable isoforms. When PrP misfolds, it aggregates and causes n...
The prion protein (PrP) has multiple stable isoforms. When PrP misfolds, it aggregates and causes ne...
Conversion of prion protein (PrP) from its normal, cellular isoform, PrPC, to an infectious, misfold...
Conformational conversion of proteins in disease is likely to be accompanied by molecular surface ex...
The self-association of prion protein (PrP) is a critical step in the pathology of prion diseases. I...
The self-association of prion protein (PrP) is a critical step in the pathology of prion diseases. I...
The aggregation of the prion protein (PrP) plays a key role in the development of prion diseases. In...
Misofolding of mammalian prion proteins (PrP) is believed to be the cause of a group of rare and fat...
Prion diseases are a group of fatal and incurable neurodegenerative disorders of mammals. They uniqu...
The post-translational conversion of the ubiquitously expressed cellular form of the prion protein, ...
Prions cause neurodegenerative diseases for which no cure exists. Despite decades of research activi...
Background: Prion diseases are fatal neurodegenerative disorders that can arise sporadically, be gen...
Fatal neurodegenerative disorders termed transmissible spongiform encephalopathies (TSEs) are associ...
Prion diseases are fatal neurodegenerative disorders caused by an aberrant accumulation of the misfo...
Elucidation of the structure of PrP(Sc) continues to be one major challenge in prion research. The m...