Limelight on alpha-synuclein: pathological and mechanistic implications in neurodegeneration
P Wales, R Pinho, DF Lázaro… - Journal of Parkinson's …, 2013 - content.iospress.com
The pathogenesis of many neurodegenerative disorders arises in association with the
misfolding and accumulation of a wide variety of proteins. Much emphasis has been placed …
misfolding and accumulation of a wide variety of proteins. Much emphasis has been placed …
[HTML][HTML] Proteins behaving badly. Substoichiometric molecular control and amplification of the initiation and nature of amyloid fibril formation: lessons from and for …
DB Kell, E Pretorius - Progress in biophysics and molecular biology, 2017 - Elsevier
The chief and largely terminal element of normal blood clotting is considered to involve the
polymerisation of the mainly α-helical fibrinogen to fibrin, with a binding mechanism …
polymerisation of the mainly α-helical fibrinogen to fibrin, with a binding mechanism …
Prion protein misfolding, strains, and neurotoxicity: an update from studies on mammalian prions
I Poggiolini, D Saverioni… - International journal of cell …, 2013 - Wiley Online Library
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a
group of fatal neurodegenerative disorders affecting humans and other mammalian species …
group of fatal neurodegenerative disorders affecting humans and other mammalian species …
Neurodegenerative diseases: quantitative predictions of protein–RNA interactions
Increasing evidence indicates that RNA plays an active role in a number of
neurodegenerative diseases. We recently introduced a theoretical framework, catRAPID, to …
neurodegenerative diseases. We recently introduced a theoretical framework, catRAPID, to …
RNA modulates aggregation of the recombinant mammalian prion protein by direct interaction
Recent studies have proposed that nucleic acids act as potential cofactors for protein
aggregation and prionogenesis. By means of sedimentation, transmission electron …
aggregation and prionogenesis. By means of sedimentation, transmission electron …
Cerebral organoids as a new model for prion disease
The rapid development of induced pluripotent stem cell (iPSC) technology has considerably
expanded the range of human cell and tissue models available for investigators. IPSCs can …
expanded the range of human cell and tissue models available for investigators. IPSCs can …
Stress and viral insults do not trigger E200K PrP conversion in human cerebral organoids
Prion diseases are a group of rare, transmissible, and invariably fatal neurodegenerative
diseases that affect both humans and animals. The cause of these diseases is misfolding of …
diseases that affect both humans and animals. The cause of these diseases is misfolding of …
The N terminus of the prion protein mediates functional interactions with the neuronal cell adhesion molecule (NCAM) fibronectin domain
The cellular form of the prion protein (PrP C) is a highly conserved glycoprotein mostly
expressed in the central and peripheral nervous systems by different cell types in mammals …
expressed in the central and peripheral nervous systems by different cell types in mammals …
Structural determinants of the prion protein N-terminus and its adducts with copper ions
The N-terminus of the prion protein is a large intrinsically disordered region encompassing
approximately 125 amino acids. In this paper, we review its structural and functional …
approximately 125 amino acids. In this paper, we review its structural and functional …
Modulation of p53 and prion protein aggregation by RNA
Several RNA-binding proteins undergo reversible liquid-liquid phase transitions, which, in
pathological conditions, might evolve into transitions to solid-state phases, giving rise to …
pathological conditions, might evolve into transitions to solid-state phases, giving rise to …