Selective vulnerability to neurodegenerative disease: the curious case of Prion Protein

WS Jackson - Disease models & mechanisms, 2014 - journals.biologists.com
The mechanisms underlying the selective targeting of specific brain regions by different
neurodegenerative diseases is one of the most intriguing mysteries in medicine. For …

Prions: beyond a single protein

AS Das, WQ Zou - Clinical microbiology reviews, 2016 - Am Soc Microbiol
Since the term protein was first coined in 1838 and protein was discovered to be the
essential component of fibrin and albumin, all cellular proteins were presumed to play …

Glycoform-selective prion formation in sporadic and familial forms of prion disease

X Xiao, J Yuan, S Haik, I Cali, Y Zhan, M Moudjou… - PLoS …, 2013 - journals.plos.org
The four glycoforms of the cellular prion protein (PrPC) variably glycosylated at the two N-
linked glycosylation sites are converted into their pathological forms (PrPSc) in most cases …

Role of sialylation of N-linked glycans in prion pathogenesis

N Makarava, IV Baskakov - Cell and tissue research, 2023 - Springer
Mammalian prion or PrPSc is a proteinaceous infectious agent that consists of a misfolded,
self-replicating state of the prion protein or PrPC. PrPC and PrPSc are posttranslationally …

Recombinant Human Prion Protein Inhibits Prion Propagation in vitro

J Yuan, YA Zhan, R Abskharon, X Xiao, MC Martinez… - Scientific reports, 2013 - nature.com
Prion diseases are associated with the conformational conversion of the cellular prion
protein (PrPC) into the pathological scrapie isoform (PrPSc) in the brain. Both the in vivo and …

Further characterization of glycoform-selective prions of variably protease-sensitive prionopathy

W Zhang, X Xiao, M Ding, J Yuan, A Foutz, M Moudjou… - Pathogens, 2021 - mdpi.com
Prion is an infectious protein (PrPSc) that is derived from a cellular glycoprotein (PrPC)
through a conformational transition and associated with a group of prion diseases in animals …

The pathogenic mutation T182A converts the prion protein into a molten globule-like conformation whose misfolding to oligomers but not to fibrils is drastically …

J Singh, JB Udgaonkar - Biochemistry, 2016 - ACS Publications
Delineation of the effects of pathogenic mutations linked with familial prion diseases on the
structure and misfolding of prion protein (PrP) will be useful in understanding the molecular …

In Vitro Seeding Activity of Glycoform-Deficient Prions from Variably Protease-Sensitive Prionopathy and Familial CJD Associated with PrPV180I Mutation

Z Wang, J Yuan, P Shen, R Abskharon, Y Lang… - Molecular …, 2019 - Springer
Both sporadic variably protease-sensitive prionopathy (VPSPr) and familial Creutzfeldt-
Jakob disease linked to the prion protein (PrP) V180I mutation (fCJD V180I) have been …

[HTML][HTML] Protease-sensitive prions with 144-bp insertion mutations

X Xiao, I Cali, Z Dong, G Puoti, J Yuan, L Qing… - Aging (Albany …, 2013 - ncbi.nlm.nih.gov
Insertion of 144-base pair (bp) containing six extra octapeptide repeats between residues 51
and 91 of prion protein (PrP) gene is associated with inherited prion diseases. Most cases …

Glycoform-selective prions in sporadic and genetic variably protease-sensitive prionopathies

Z Wang, J Yuan, T Gilliland, M Gerasimenko… - Prions and …, 2023 - Springer
Unlike other human prion diseases, including the most common Creutzfeldt–Jakob disease
(CJD), variably protease-sensitive prionopathy (VPSPr) is characterized by the deposition of …