Related references
Note: Only part of the references are listed.In vitro and in vivo neurotoxicity of prion protein oligomers
Steve Simoneau et al.
PLOS PATHOGENS (2007)
Converting the prion protein: What makes the protein infectious
Ilia V. Baskakov et al.
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE (2007)
Protein particulates: Another generic form of protein aggregation?
Mark R. H. Krebs et al.
BIOPHYSICAL JOURNAL (2007)
The reconstitution of mammalian prion infectivity de novo
Ilia V. Baskakov
FEBS JOURNAL (2007)
Sequence and structural determinants of amyloid fibril formation
Francesco Bemporad et al.
ACCOUNTS OF CHEMICAL RESEARCH (2006)
Structural instability of the prion protein upon M205S/R mutations revealed by molecular dynamics simulations
Thomas Hirschberger et al.
BIOPHYSICAL JOURNAL (2006)
Modulation of prion protein structure by pressure and temperature
J Torrent et al.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS (2006)
Protein folding and aggregation: Two sides of the same coin in the condensation of proteins revealed by pressure studies
JL Silva et al.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS (2006)
Tuning amyloidogenic conformations through cosolvents and hydrostatic pressure: When the soft matter becomes even softer
W Dzwolak
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS (2006)
Protein aggregation and amyloidosis: confusion of the kinds?
F Rousseau et al.
CURRENT OPINION IN STRUCTURAL BIOLOGY (2006)
Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions
Filip Meersman et al.
CHEMICAL SOCIETY REVIEWS (2006)
High pressure modulates amyloid formation
J Torrent et al.
PROTEIN AND PEPTIDE LETTERS (2006)
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation
Y Cordeiro et al.
BIOPHYSICAL JOURNAL (2005)
Assembly of natural and recombinant prion protein into fibrils
KW Leffers et al.
BIOLOGICAL CHEMISTRY (2005)
The role of the 132-160 region in prion protein conformational transitions
J Torrent et al.
PROTEIN SCIENCE (2005)
An unusual soluble β-turn-rich conformation of prion is involved in fibril formation and toxic to neuronal cells
J Kazlauskaite et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2005)
In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrPSc
OV Bocharova et al.
JOURNAL OF MOLECULAR BIOLOGY (2005)
Misfolding pathways of the prion protein probed by molecular dynamics Simulations
A Barducci et al.
BIOPHYSICAL JOURNAL (2005)
Comparative computational analysis of prion proteins reveals two fragments with unusual structural properties and a pattern of increase in hydrophobicity associated with disease-promoting mutations
IB Kuznetsov et al.
PROTEIN SCIENCE (2004)
Hydration and packing effects on prion folding and β-sheet conversion -: High pressure spectroscopy and pressure perturbation calorimetry studies
Y Cordeiro et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
The structural transition of the prion protein into its pathogenic conformation is induced by unmasking hydrophobic sites
KW Leffers et al.
JOURNAL OF MOLECULAR BIOLOGY (2004)
High pressure induces scrapie-like prion protein misfolding and amyloid fibril formation
J Torrent et al.
BIOCHEMISTRY (2004)
Alternative prion structural changes revealed by high pressure
J Torrent et al.
BIOCHEMISTRY (2003)
Amyloidogenic unfolding intermediates differentiate sheep prion protein variants
H Rezaei et al.
JOURNAL OF MOLECULAR BIOLOGY (2002)
Pathway complexity of prion protein assembly into amyloid
IV Baskakov et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Revisiting volume changes in pressure-induced protein unfolding
CA Royer
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY (2002)
Pressure provides new insights into protein folding, dynamics and structure
JL Silva et al.
TRENDS IN BIOCHEMICAL SCIENCES (2001)
Prion diseases: What is the neurotoxic molecule?
R Chiesa et al.
NEUROBIOLOGY OF DISEASE (2001)
Folding of prion protein to its native α-helical conformation is under kinetic control
IV Baskakov et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility
H Rezaei et al.
EUROPEAN JOURNAL OF BIOCHEMISTRY (2000)
Aggregation and fibrillization of the recombinant human prion protein huPrP90-231
W Swietnicki et al.
BIOCHEMISTRY (2000)