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Regulatory mechanisms of tau protein fibrillation under the conditions of liquid–liquid phase separation

Proceedings of the National Academy of Sciences - PNAS, 2020-12, Vol.117 (50), p.31882-31890

2020

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Liquid–liquid phase separation of tau protein: The crucial role of electrostatic interactions

The Journal of biological chemistry, 2019-07, Vol.294 (29), p.11054-11059

2019

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Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43

Nature communications, 2021-03, Vol.12 (1), p.1620-1620, Article 1620

2021

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Small molecules as potent biphasic modulators of protein liquid-liquid phase separation

Nature communications, 2020-11, Vol.11 (1), p.5574-15, Article 5574

2020

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Amyloid fibrils from the N-terminal prion protein fragment are infectious

Proceedings of the National Academy of Sciences - PNAS, 2016-11, Vol.113 (48), p.13851-13856

2016

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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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Tau liquid–liquid phase separation in neurodegenerative diseases

Trends in cell biology, 2022-07, Vol.32 (7), p.611-623

2022

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Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange

Nature structural & molecular biology, 2011-04, Vol.18 (4), p.504-506

2011

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Structural Studies of Amyloid Fibrils by Paramagnetic Solid-State Nuclear Magnetic Resonance Spectroscopy

Journal of the American Chemical Society, 2018-10, Vol.140 (41), p.13161-13166

2018

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Molecular architecture of human prion protein amyloid: A parallel, in-register β-structure

Proceedings of the National Academy of Sciences - PNAS, 2007-11, Vol.104 (48), p.18946-18951

2007

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Molecular Conformation and Dynamics of the Y145Stop Variant of Human Prion Protein in Amyloid Fibrils

Proceedings of the National Academy of Sciences - PNAS, 2008-04, Vol.105 (17), p.6284-6289

2008

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β-Sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange

Proceedings of the National Academy of Sciences - PNAS, 2007-01, Vol.104 (5), p.1510-1515

2007

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Structural determinants of phenotypic diversity and replication rate of human prions

PLoS pathogens, 2015-04, Vol.11 (4), p.e1004832-e1004832

2015

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Crystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer Formation

Journal of the American Chemical Society, 2013-07, Vol.135 (28), p.10202-10205

2013

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A Metastable Contact and Structural Disorder in the Estrogen Receptor Transactivation Domain

Structure (London), 2019-02, Vol.27 (2), p.229-240.e4

2019

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Protein-solvent interfaces in human Y145Stop prion protein amyloid fibrils probed by paramagnetic solid-state NMR spectroscopy

Journal of structural biology, 2019-04, Vol.206 (1), p.36-42

2019

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Liquid–Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation

Journal of molecular biology, 2020-03, Vol.432 (7), p.1910-1925

2020

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Self-propagating, protease-resistant, recombinant prion protein conformers with or without in vivo pathogenicity

PLoS pathogens, 2017-07, Vol.13 (7), p.e1006491-e1006491

2017

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Fibril Conformation as the Basis of Species- and Strain-Dependent Seeding Specificity of Mammalian Prion Amyloids

Cell, 2005-04, Vol.121 (1), p.63-72

2005

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Zinc promotes liquid–liquid phase separation of tau protein

The Journal of biological chemistry, 2020-05, Vol.295 (18), p.5850-5856

2020

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Soluble prion protein and its N-terminal fragment prevent impairment of synaptic plasticity by Aβ oligomers: Implications for novel therapeutic strategy in Alzheimer's disease

Neurobiology of disease, 2016-07, Vol.91, p.124-131

2016

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Conformational Stability of Mammalian Prion Protein Amyloid Fibrils Is Dictated by a Packing Polymorphism within the Core Region

The Journal of biological chemistry, 2014-01, Vol.289 (5), p.2643-2650

2014

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Antimicrobial activity of human prion protein is mediated by its N-terminal region

PloS one, 2009-10, Vol.4 (10), p.e7358-e7358

2009

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Small Protease Sensitive Oligomers of PrPSc in Distinct Human Prions Determine Conversion Rate of PrPC

PLoS pathogens, 2012-08, Vol.8 (8), p.e1002835

2012

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Regulatory mechanisms of tau protein fibrillation under the conditions of liquid–liquid phase separation

Liquid–liquid phase separation of tau protein: The crucial role of electrostatic interactions

Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43

Small molecules as potent biphasic modulators of protein liquid-liquid phase separation

Amyloid fibrils from the N-terminal prion protein fragment are infectious

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

Tau liquid–liquid phase separation in neurodegenerative diseases

Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange

Structural Studies of Amyloid Fibrils by Paramagnetic Solid-State Nuclear Magnetic Resonance Spectroscopy

Molecular architecture of human prion protein amyloid: A parallel, in-register β-structure

Molecular Conformation and Dynamics of the Y145Stop Variant of Human Prion Protein in Amyloid Fibrils

β-Sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange

Structural determinants of phenotypic diversity and replication rate of human prions

Crystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer Formation

A Metastable Contact and Structural Disorder in the Estrogen Receptor Transactivation Domain

Protein-solvent interfaces in human Y145Stop prion protein amyloid fibrils probed by paramagnetic solid-state NMR spectroscopy

Liquid–Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation

Self-propagating, protease-resistant, recombinant prion protein conformers with or without in vivo pathogenicity

Fibril Conformation as the Basis of Species- and Strain-Dependent Seeding Specificity of Mammalian Prion Amyloids

Zinc promotes liquid–liquid phase separation of tau protein

Soluble prion protein and its N-terminal fragment prevent impairment of synaptic plasticity by Aβ oligomers: Implications for novel therapeutic strategy in Alzheimer's disease

Conformational Stability of Mammalian Prion Protein Amyloid Fibrils Is Dictated by a Packing Polymorphism within the Core Region

Antimicrobial activity of human prion protein is mediated by its N-terminal region

Small Protease Sensitive Oligomers of PrPSc in Distinct Human Prions Determine Conversion Rate of PrPC

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