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Prions, prionoids and protein misfolding disorders

Nature reviews. Genetics, 2018-07, Vol.19 (7), p.405-418

2018

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Sustained translational repression by eIF2α-P mediates prion neurodegeneration

Nature (London), 2012-05, Vol.485 (7399), p.507-511

2012

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General Model of Prion Strains and Their Pathogenicity

Science (American Association for the Advancement of Science), 2007-11, Vol.318 (5852), p.930-936

2007

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Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies

Experimental & molecular medicine, 2015-03, Vol.47 (3), p.e147-e147

2015

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Liquid–liquid phase separation of full-length prion protein initiates conformational conversion in vitro

The Journal of biological chemistry, 2021-01, Vol.296, p.100367, Article 100367

2021

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Prion propagation and toxicity in vivo occur in two distinct mechanistic phases

Nature (London), 2011-02, Vol.470 (7335), p.540-542

2011

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Prion neuropathology follows the accumulation of alternate prion protein isoforms after infective titre has peaked

Nature communications, 2014-07, Vol.5 (1), p.4347, Article 4347

2014

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Role of sialylation of N-linked glycans in prion pathogenesis

Cell and tissue research, 2023-04, Vol.392 (1), p.201-214

2023

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A naturally occurring variant of the human prion protein completely prevents prion disease

Nature (London), 2015-06, Vol.522 (7557), p.478-481

2015

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Defining sporadic Creutzfeldt-Jakob disease strains and their transmission properties

Proceedings of the National Academy of Sciences - PNAS, 2010-06, Vol.107 (26), p.12005-12010

2010

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Asymptomatic deer excrete infectious prions in faeces

Nature, 2009-09, Vol.461 (7263), p.529-532

2009

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Formation of native prions from minimal components in vitro

Proceedings of the National Academy of Sciences - PNAS, 2007-06, Vol.104 (23), p.9741-9746

2007

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Proteinase K and the structure of PrPSc: The good, the bad and the ugly

Virus research, 2015-09, Vol.207, p.120-126

2015

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Insights into prion strains and neurotoxicity

Nature reviews. Molecular cell biology, 2007-07, Vol.8 (7), p.552-561

2007

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Full restoration of specific infectivity and strain properties from pure mammalian prion protein

PLoS pathogens, 2019-03, Vol.15 (3), p.e1007662

2019

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Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy

Nature communications, 2017-09, Vol.8 (1), p.753-10, Article 753

2017

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Mammalian Prions Generated from Bacterially Expressed Prion Protein in the Absence of Any Mammalian Cofactors

The Journal of biological chemistry, 2010-05, Vol.285 (19), p.14083-14087

2010

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Loss of small GTPase Rab7 activation in prion infection negatively affects a feedback loop regulating neuronal cholesterol metabolism

The Journal of biological chemistry, 2023-02, Vol.299 (2), p.102883-102883, Article 102883

2023

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Adaptation of the protein misfolding cyclic amplification (PMCA) technique for the screening of anti‐prion compounds

The FASEB journal, 2024-07, Vol.38 (14), p.e23843-n/a

2024

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From Kuru to Alzheimer: A personal outlook

Protein science, 2021-09, Vol.30 (9), p.1776-1792

Brunori, Maurizio

2021

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Transition of the prion protein from a structured cellular form (PrPC) to the infectious scrapie agent (PrPSc)

Protein science, 2019-12, Vol.28 (12), p.2055-2063

2019

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Microglia in prion diseases

The Journal of clinical investigation, 2017-09, Vol.127 (9), p.3230-3239

2017

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Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity

PLoS pathogens, 2014-09, Vol.10 (9), p.e1004366-e1004366

2014

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Full-length prion protein incorporated into prion aggregates is a marker for prion strain-specific destabilization of aggregate structure following cellular uptake

Journal of biochemistry (Tokyo), 2023-07, Vol.174 (2), p.165-181

2023

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The multivesicular body is the major internal site of prion conversion

Journal of cell science, 2015-04, Vol.128 (7), p.1434-1443

2015

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Prions, prionoids and protein misfolding disorders

Sustained translational repression by eIF2α-P mediates prion neurodegeneration

General Model of Prion Strains and Their Pathogenicity

Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies

Liquid–liquid phase separation of full-length prion protein initiates conformational conversion in vitro

Prion propagation and toxicity in vivo occur in two distinct mechanistic phases

Prion neuropathology follows the accumulation of alternate prion protein isoforms after infective titre has peaked

Role of sialylation of N-linked glycans in prion pathogenesis

A naturally occurring variant of the human prion protein completely prevents prion disease

Defining sporadic Creutzfeldt-Jakob disease strains and their transmission properties

Asymptomatic deer excrete infectious prions in faeces

Formation of native prions from minimal components in vitro

Proteinase K and the structure of PrPSc: The good, the bad and the ugly

Insights into prion strains and neurotoxicity

Full restoration of specific infectivity and strain properties from pure mammalian prion protein

Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy

Mammalian Prions Generated from Bacterially Expressed Prion Protein in the Absence of Any Mammalian Cofactors

Loss of small GTPase Rab7 activation in prion infection negatively affects a feedback loop regulating neuronal cholesterol metabolism

Adaptation of the protein misfolding cyclic amplification (PMCA) technique for the screening of anti‐prion compounds

From Kuru to Alzheimer: A personal outlook

Transition of the prion protein from a structured cellular form (PrPC) to the infectious scrapie agent (PrPSc)

Microglia in prion diseases

Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity

Full-length prion protein incorporated into prion aggregates is a marker for prion strain-specific destabilization of aggregate structure following cellular uptake

The multivesicular body is the major internal site of prion conversion

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