Physiology of the prion protein
Prion diseases are transmissible spongiform encephalopathies (TSEs), attributed to
conformational conversion of the cellular prion protein (PrPC) into an abnormal conformer …
conformational conversion of the cellular prion protein (PrPC) into an abnormal conformer …
The two faces of protein misfolding: gain‐and loss‐of‐function in neurodegenerative diseases
KF Winklhofer, J Tatzelt, C Haass - The EMBO journal, 2008 - embopress.org
The etiologies of neurodegenerative diseases may be diverse; however, a common
pathological denominator is the formation of aberrant protein conformers and the occurrence …
pathological denominator is the formation of aberrant protein conformers and the occurrence …
[HTML][HTML] Pathogenic alpha-synuclein aggregates preferentially bind to mitochondria and affect cellular respiration
X Wang, K Becker, N Levine, M Zhang… - Acta neuropathologica …, 2019 - Springer
Misfolded alpha-synuclein (αSyn) is a major constituent of Lewy bodies and Lewy neurites,
which are pathological hallmarks of Parkinson's disease (PD). The contribution of αSyn to …
which are pathological hallmarks of Parkinson's disease (PD). The contribution of αSyn to …
Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions
B Caughey, GS Baron, B Chesebro… - Annual review of …, 2009 - annualreviews.org
The prion (infectious protein) concept has evolved with the discovery of new self-
propagating protein states in organisms as diverse as mammals and fungi. The infectious …
propagating protein states in organisms as diverse as mammals and fungi. The infectious …
Optimizing cathode materials for intermediate-temperature solid oxide fuel cells (SOFCs): Oxygen reduction on nanostructured lanthanum nickelate oxides
JSA Carneiro, RA Brocca, MLRS Lucena… - Applied Catalysis B …, 2017 - Elsevier
Kinetics of high temperature oxygen reduction reaction (ORR) on La 2 NiO 4+ δ (LNO)
nanostructures are investigated by means of electrochemical impedance spectroscopy, with …
nanostructures are investigated by means of electrochemical impedance spectroscopy, with …
N-terminal peptides from unprocessed prion proteins enter cells by macropinocytosis
M Magzoub, S Sandgren, P Lundberg… - Biochemical and …, 2006 - Elsevier
A peptide derived from the N-terminus of the unprocessed bovine prion protein (bPrPp),
incorporating the hydrophobic signal sequence (residues 1–24) and a basic domain …
incorporating the hydrophobic signal sequence (residues 1–24) and a basic domain …
Lipid Interaction Converts Prion Protein to a PrPSc-like Proteinase K-Resistant Conformation under Physiological Conditions
The conversion of prion protein (PrP) to the pathogenic PrPSc conformation is central to
prion disease. Previous studies revealed that PrP interacts with lipids and the interaction …
prion disease. Previous studies revealed that PrP interacts with lipids and the interaction …
Prion protein biosynthesis and its emerging role in neurodegeneration
O Chakrabarti, A Ashok, RS Hegde - Trends in biochemical sciences, 2009 - cell.com
Various fatal neurodegenerative disorders are caused by altered metabolism of the prion
protein (PrP). These diseases are typically transmissible by an unusual 'protein …
protein (PrP). These diseases are typically transmissible by an unusual 'protein …
[HTML][HTML] Mechanism of aggregation and membrane interactions of mammalian prion protein
The cellular prion protein (PrP C), which is present ubiquitously in all mammalian neurons,
is normally found to be linked to the cell membrane through a glycosylphosphatidylinositol …
is normally found to be linked to the cell membrane through a glycosylphosphatidylinositol …
Role of the highly conserved middle region of prion protein (PrP) in PrP− lipid interaction
F Wang, S Yin, X Wang, L Zha, MS Sy, J Ma - Biochemistry, 2010 - ACS Publications
Converting normal prion protein (PrPC) to the pathogenic PrPSc isoform is central to prion
disease. We previously showed that, in the presence of lipids, recombinant mouse PrP …
disease. We previously showed that, in the presence of lipids, recombinant mouse PrP …