Physiology of the prion protein

R Linden, VR Martins, MAM Prado… - Physiological …, 2008 - journals.physiology.org
Prion diseases are transmissible spongiform encephalopathies (TSEs), attributed to
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 …

[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 …

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 …

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 …

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 …

Lipid Interaction Converts Prion Protein to a PrPSc-like Proteinase K-Resistant Conformation under Physiological Conditions

F Wang, F Yang, Y Hu, X Wang, X Wang, C Jin… - Biochemistry, 2007 - ACS Publications
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 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 …

[HTML][HTML] Mechanism of aggregation and membrane interactions of mammalian prion protein

SA Thody, MK Mathew, JB Udgaonkar - Biochimica et Biophysica Acta …, 2018 - Elsevier
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 …

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 …