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Your search keyword '"Judith Mihály"' showing total 4 results
Start Over Author "Judith Mihály" Journal neurobiology of disease
4 results on '"Judith Mihály"'

1. Corrigendum to 'DJ-1 can form β-sheet structured aggregates that co-localize with pathological amyloid deposits'. Neurobiology of Disease 134 (2020) 104629

Author

Katalin Solti, Wei-Li Kuan, Balázs Fórizs, Gergely Kustos, Judith Mihály, Zoltán Varga, Balázs Herberth, Éva Moravcsik, Róbert Kiss, Manuela Kárpáti, Anna Mikes, Yanyan Zhao, Tímea Imre, Jean-Christophe Rochet, Franklin Aigbirhio, Caroline H. Williams-Gray, Roger A. Barker, and Gergely Tóth

Subjects
Neurosciences. Biological psychiatry. Neuropsychiatry, RC321-571
Published
2020
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2. DJ-1 can form β-sheet structured aggregates that co-localize with pathological amyloid deposits

Author

Katalin Solti, Wei-Li Kuan, Balázs Fórizs, Gergely Kustos, Judith Mihály, Zoltán Varga, Balázs Herberth, Éva Moravcsik, Róbert Kiss, Manuela Kárpáti, Anna Mikes, Yanyan Zhao, Tímea Imre, Jean-Christophe Rochet, Franklin Aigbirhio, Caroline H. Williams-Gray, Roger A. Barker, and Gergely Tóth

Subjects
DJ-1, Parkinson's, Alzheimer's, Aggregation, Amyloid, Neurosciences. Biological psychiatry. Neuropsychiatry, RC321-571
Abstract

The loss of native function of the DJ-1 protein has been linked to the development of Parkinson's (PD) and other neurodegenerative diseases. Here we show that DJ-1 aggregates into β-sheet structured soluble and fibrillar aggregates in vitro under physiological conditions and that this process is promoted by the oxidation of its catalytic Cys106 residue. This aggregation resulted in the loss of its native biochemical glyoxalase function and in addition oxidized DJ-1 aggregates were observed to localize within Lewy bodies, neurofibrillary tangles and amyloid plaques in human PD and Alzheimer's (AD) patients' post-mortem brain tissue. These findings suggest that the aggregation of DJ-1 may be a critical player in the development of the pathology of PD and AD and demonstrate that loss of DJ-1 function can happen through DJ-1 aggregation. This could then contribute to AD and PD disease onset and progression.

Published
2020
Full Text
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3. DJ-1 can form β-sheet structured aggregates that co-localize with pathological amyloid deposits

Author

Manuéla Kárpáti, Gergely Tóth, Franklin I. Aigbirhio, Judith Mihály, Yanyan Zhao, Balázs Fórizs, Tímea Imre, Balázs Herberth, Jean-Christophe Rochet, Katalin Solti, Roger A. Barker, Anna Mikes, Róbert Gábor Kiss, Caroline H. Williams-Gray, Éva Moravcsik, Gergely Kustos, Wei-Li Kuan, Zoltán Varga, Kuan, William [0000-0002-0273-1320], Zhao, Yanyan [0000-0003-3827-3349], Aigbirhio, Franklin [0000-0001-9453-5257], Williams-Gray, Caroline [0000-0002-2648-9743], Barker, Roger [0000-0001-8843-7730], and Apollo - University of Cambridge Repository

Subjects
0301 basic medicine, DJ-1, Amyloid, Disease onset, Parkinson's, Protein Deglycase DJ-1, Beta sheet, Plaque, Amyloid, Brain tissue, Protein Aggregation, Pathological, lcsh:RC321-571, Protein Aggregates, 03 medical and health sciences, Aggregation, 0302 clinical medicine, Alzheimer Disease, Humans, Pathological, lcsh:Neurosciences. Biological psychiatry. Neuropsychiatry, Chemistry, Brain, Neurofibrillary Tangles, Parkinson Disease, Alzheimer's, In vitro, Cell biology, 030104 developmental biology, Neurology, Lewy Bodies, Protein Conformation, beta-Strand, 030217 neurology & neurosurgery, Function (biology)
Abstract

The loss of native function of the DJ-1 protein has been linked to the development of Parkinson's (PD) and other neurodegenerative diseases. Here we show that DJ-1 aggregates into β-sheet structured soluble and fibrillar aggregates in vitro under physiological conditions and that this process is promoted by the oxidation of its catalytic Cys106 residue. This aggregation resulted in the loss of its native biochemical glyoxalase function and in addition oxidized DJ-1 aggregates were observed to localize within Lewy bodies, neurofibrillary tangles and amyloid plaques in human PD and Alzheimer's (AD) patients' post-mortem brain tissue. These findings suggest that the aggregation of DJ-1 may be a critical player in the development of the pathology of PD and AD and demonstrate that loss of DJ-1 function can happen through DJ-1 aggregation. This could then contribute to AD and PD disease onset and progression.

Published
2020

4. Corrigendum to 'DJ-1 can form β-sheet structured aggregates that co-localize with pathological amyloid deposits'. Neurobiology of Disease 134 (2020) 104629

Author

Yanyan Zhao, Caroline H. Williams-Gray, Balázs Fórizs, Gergely Kustos, Anna Mikes, Gergely Toth, Éva Moravcsik, Wei-Li Kuan, Katalin Solti, Judith Mihály, Róbert Gábor Kiss, Manuéla Kárpáti, Zoltán Varga, Roger A. Barker, Franklin I. Aigbirhio, Tímea Imre, Balázs Herberth, and Jean-Christophe Rochet

Subjects
Pathology, medicine.medical_specialty, Neurology, Amyloid, Chemistry, Beta sheet, medicine, Disease, lcsh:Neurosciences. Biological psychiatry. Neuropsychiatry, Pathological, lcsh:RC321-571
Published
2020
Full Text
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