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 …

[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 …

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 …

Neurodegenerative diseases: quantitative predictions of protein–RNA interactions

D Cirillo, F Agostini, P Klus, D Marchese, S Rodriguez… - Rna, 2013 - rnajournal.cshlp.org
Increasing evidence indicates that RNA plays an active role in a number of
neurodegenerative diseases. We recently introduced a theoretical framework, catRAPID, to …

RNA modulates aggregation of the recombinant mammalian prion protein by direct interaction

PS Kovachev, MPB Gomes, Y Cordeiro, NC Ferreira… - Scientific reports, 2019 - nature.com
Recent studies have proposed that nucleic acids act as potential cofactors for protein
aggregation and prionogenesis. By means of sedimentation, transmission electron …

Cerebral organoids as a new model for prion disease

BR Groveman, A Smith, K Williams, CL Haigh - PLoS Pathogens, 2021 - journals.plos.org
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 …

Stress and viral insults do not trigger E200K PrP conversion in human cerebral organoids

A Smith, BR Groveman, C Winkler, K Williams… - PloS one, 2022 - journals.plos.org
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 …

The N terminus of the prion protein mediates functional interactions with the neuronal cell adhesion molecule (NCAM) fibronectin domain

U Slapšak, G Salzano, L Amin, RNN Abskharon… - Journal of Biological …, 2016 - ASBMB
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 …

Structural determinants of the prion protein N-terminus and its adducts with copper ions

C Sánchez-López, G Rossetti, L Quintanar… - International journal of …, 2018 - mdpi.com
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 …

Modulation of p53 and prion protein aggregation by RNA

Y Cordeiro, T Vieira, PS Kovachev, S Sanyal… - Biochimica et Biophysica …, 2019 - Elsevier
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 …