Prion protein at the crossroads of physiology and disease
E Biasini, JA Turnbaugh, U Unterberger… - Trends in neurosciences, 2012 - cell.com
The presence of the cellular prion protein (PrP C) on the cell surface is critical for the
neurotoxicity of prions. Although several biological activities have been attributed to PrP C, a …
neurotoxicity of prions. Although several biological activities have been attributed to PrP C, a …
Prion propagation, toxicity and degradation
A Aguzzi, J Falsig - Nature neuroscience, 2012 - nature.com
Prion science has been on a rollercoaster for two decades. In the mid 1990s, the specter of
mad cow disease (bovine spongiform encephalopathy, BSE) provoked an unprecedented …
mad cow disease (bovine spongiform encephalopathy, BSE) provoked an unprecedented …
The N-terminus of the prion protein is a toxic effector regulated by the C-terminus
B Wu, AJ McDonald, K Markham, CB Rich, KP McHugh… - Elife, 2017 - elifesciences.org
PrPC, the cellular isoform of the prion protein, serves to transduce the neurotoxic effects of
PrPSc, the infectious isoform, but how this occurs is mysterious. Here, using a combination …
PrPSc, the infectious isoform, but how this occurs is mysterious. Here, using a combination …
A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation
L Westergard, JA Turnbaugh, DA Harris - Journal of Biological Chemistry, 2011 - ASBMB
The cellular prion protein (PrP C) undergoes constitutive proteolytic cleavage between
residues 111/112 to yield a soluble N-terminal fragment (N1) and a membrane-anchored C …
residues 111/112 to yield a soluble N-terminal fragment (N1) and a membrane-anchored C …
Mechanisms of prion-induced toxicity
RCC Mercer, DA Harris - Cell and Tissue Research, 2023 - Springer
Prion diseases are devastating neurodegenerative diseases caused by the structural
conversion of the normally benign prion protein (PrPC) to an infectious, disease-associated …
conversion of the normally benign prion protein (PrPC) to an infectious, disease-associated …
Evidence for preexisting prion substrain diversity in a biologically cloned prion strain
T Gunnels, RA Shikiya, TC York, AJ Block… - PLoS …, 2023 - journals.plos.org
Prion diseases are a group of inevitably fatal neurodegenerative disorders affecting
numerous mammalian species, including Sapiens. Prions are composed of PrPSc, the …
numerous mammalian species, including Sapiens. Prions are composed of PrPSc, the …
A neuronal culture system to detect prion synaptotoxicity
Synaptic pathology is an early feature of prion as well as other neurodegenerative diseases.
Although the self-templating process by which prions propagate is well established, the …
Although the self-templating process by which prions propagate is well established, the …
The N-terminal, polybasic region of PrPC dictates the efficiency of prion propagation by binding to PrPSc
JA Turnbaugh, U Unterberger, P Saá… - Journal of …, 2012 - Soc Neuroscience
Prion propagation involves a templating reaction in which the infectious form of the prion
protein (PrP Sc) binds to the cellular form (PrP C), generating additional molecules of PrP …
protein (PrP Sc) binds to the cellular form (PrP C), generating additional molecules of PrP …
Multifaceted role of sialylation in prion diseases
IV Baskakov, E Katorcha - Frontiers in Neuroscience, 2016 - frontiersin.org
Mammalian prion or PrPSc is a proteinaceous infectious agent that consists of a misfolded,
self-replicating state of a sialoglycoprotein called the prion protein, or PrPC. Sialylation of …
self-replicating state of a sialoglycoprotein called the prion protein, or PrPC. Sialylation of …
Mutant PrP suppresses glutamatergic neurotransmission in cerebellar granule neurons by impairing membrane delivery of VGCC α2δ-1 subunit
A Senatore, S Colleoni, C Verderio, E Restelli, R Morini… - Neuron, 2012 - cell.com
How mutant prion protein (PrP) leads to neurological dysfunction in genetic prion diseases
is unknown. Tg (PG14) mice synthesize a misfolded mutant PrP which is partially retained in …
is unknown. Tg (PG14) mice synthesize a misfolded mutant PrP which is partially retained in …