[HTML][HTML] The biological function of the prion protein: a cell surface scaffold of signaling modules
R Linden - Frontiers in molecular neuroscience, 2017 - frontiersin.org
The prion glycoprotein (PrPC) is mostly located at the cell surface, tethered to the plasma
membrane through a glycosyl-phosphatydil inositol (GPI) anchor. Misfolding of PrPC is …
membrane through a glycosyl-phosphatydil inositol (GPI) anchor. Misfolding of PrPC is …
[HTML][HTML] The prion protein and its ligands: Insights into structure-function relationships
The prion protein is a multifunctional protein that exists in at least two different folding states.
It is subject to diverse proteolytic processing steps that lead to prion protein fragments some …
It is subject to diverse proteolytic processing steps that lead to prion protein fragments some …
The prion protein ligand, stress-inducible phosphoprotein 1, regulates amyloid-β oligomer toxicity
VG Ostapchenko, FH Beraldo… - Journal of …, 2013 - Soc Neuroscience
In Alzheimer's disease (AD), soluble amyloid-β oligomers (AβOs) trigger neurotoxic
signaling, at least partially, via the cellular prion protein (PrPC). However, it is unknown …
signaling, at least partially, via the cellular prion protein (PrPC). However, it is unknown …
The prion protein unstructured N‐terminal region is a broad‐spectrum molecular sensor with diverse and contrasting potential functions
M Béland, X Roucou - Journal of neurochemistry, 2012 - Wiley Online Library
J. Neurochem.(2012) 120, 853–868. Abstract The physiological function of the prion protein
(PrPC) and its conversion into its infectious form (PrPSc) are central issues to understanding …
(PrPC) and its conversion into its infectious form (PrPSc) are central issues to understanding …
Allosteric function and dysfunction of the prion protein
Transmissible spongiform encephalopathies (TSEs) are neurodegenerative diseases
associated with progressive oligo-and multimerization of the prion protein (PrP C), its …
associated with progressive oligo-and multimerization of the prion protein (PrP C), its …
Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities
NSM Silva, DE Bertolino-Reis, PR Dores-Silva… - … et Biophysica Acta (BBA …, 2020 - Elsevier
HOP is a cochaperone belonging to the foldosome, a system formed by the cytoplasmic
Hsp70 and Hsp90 chaperones. HOP acts as an adapter protein capable of transferring client …
Hsp70 and Hsp90 chaperones. HOP acts as an adapter protein capable of transferring client …
Domains of STIP1 responsible for regulating PrPC-dependent amyloid-β oligomer toxicity
A Maciejewski, VG Ostapchenko, FH Beraldo… - Biochemical …, 2016 - portlandpress.com
Soluble oligomers of amyloid-beta peptide (AβO) transmit neurotoxic signals through the
cellular prion protein (PrPC) in Alzheimer's disease (AD). Secreted stress-inducible …
cellular prion protein (PrPC) in Alzheimer's disease (AD). Secreted stress-inducible …
Phase separation and disorder-to-order transition of human brain expressed X-linked 3 (hBEX3) in the presence of small fragments of tRNA
MJ do Amaral, TS Araujo, NC Díaz, F Accornero… - Journal of molecular …, 2020 - Elsevier
Abstract Brain Expressed X-linked (BEX) protein family consists of five members in humans
and is highly expressed during neuronal development. They are known to participate in cell …
and is highly expressed during neuronal development. They are known to participate in cell …
Evidence for Hsp90 co-chaperones in regulating Hsp90 function and promoting client protein folding
MB Cox, JL Johnson - Chaperones: Methods and Protocols, 2018 - Springer
Molecular chaperones are a diverse group of highly conserved proteins that transiently
interact with partially folded polypeptide chains during normal cellular processes such as …
interact with partially folded polypeptide chains during normal cellular processes such as …
PrPC signalling in neurons: from basics to clinical challenges
TZ Hirsch, J Hernandez-Rapp, S Martin-Lannerée… - Biochimie, 2014 - Elsevier
The cellular prion protein PrP C was identified over twenty-five years ago as the normal
counterpart of the scrapie prion protein PrP Sc, itself the main if not the sole component of …
counterpart of the scrapie prion protein PrP Sc, itself the main if not the sole component of …