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Expanding insights of mitochondrial dysfunction in Parkinson's disease

Nature reviews. Neuroscience, 2006-03, Vol.7 (3), p.207-219

2006

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Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1

Science (American Association for the Advancement of Science), 2004-05, Vol.304 (5674), p.1158-1160

2004

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Kinetin Riboside and Its ProTides Activate the Parkinson’s Disease Associated PTEN-Induced Putative Kinase 1 (PINK1) Independent of Mitochondrial Depolarization

Journal of medicinal chemistry, 2017-04, Vol.60 (8), p.3518-3524

2017

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PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65

Open biology, 2012-05, Vol.2 (5), p.120080

2012

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mito-QC illuminates mitophagy and mitochondrial architecture in vivo

The Journal of cell biology, 2016-08, Vol.214 (3), p.333-345

2016

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A heterozygous effect for PINK1 mutations in Parkinson's disease?

Annals of neurology, 2006-10, Vol.60 (4), p.414-419

2006

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Phosphorylation of Parkin at Serine65 is essential for activation: elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity

Open biology, 2014-03, Vol.4 (3), p.130213

2014

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TigarB causes mitochondrial dysfunction and neuronal loss in PINK1 deficiency

Annals of neurology, 2013-12, Vol.74 (6), p.837-847

2013

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Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog

Nature chemical biology, 2015-07, Vol.11 (7), p.496-503

2015

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The novel MAPT mutation K298E: mechanisms of mutant tau toxicity, brain pathology and tau expression in induced fibroblast-derived neurons

Acta neuropathologica, 2014-02, Vol.127 (2), p.283-295

2014

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Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress

Journal of neurochemistry, 2006-07, Vol.98 (1), p.156-169

2006

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The Anthelmintic Drug Niclosamide and Its Analogues Activate the Parkinson's Disease Associated Protein Kinase PINK1

Chembiochem : a European journal of chemical biology, 2018-03, Vol.19 (5), p.425-429

2018

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Probes of ubiquitin E3 ligases enable systematic dissection of parkin activation

Nature chemical biology, 2016-05, Vol.12 (5), p.324-331

2016

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Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation

EMBO reports, 2015-08, Vol.16 (8), p.939-954

2015

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PINK1-dependent phosphorylation of Serine111 within the SF3 motif of Rab GTPases impairs effector interactions and LRRK2-mediated phosphorylation at Threonine72

Biochemical journal, 2020-05, Vol.477 (9), p.1651-1668

2020

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Are PARKIN patients ideal candidates for dopaminergic cell replacement therapies?

The European journal of neuroscience, 2019-02, Vol.49 (4), p.453-462

2019

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Therapeutic approaches to enhance PINK1/Parkin mediated mitophagy for the treatment of Parkinson’s disease

Neuroscience letters, 2019-07, Vol.705, p.7-13

2019

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Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations

Open biology, 2011-11, Vol.1 (3), p.110012-110012

2011

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PTEN-induced kinase 1 (PINK1) and Parkin: Unlocking a mitochondrial quality control pathway linked to Parkinson's disease

Current opinion in neurobiology, 2022-02, Vol.72, p.111-119

2022

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Parkinson's: A Disease of Aberrant Vesicle Trafficking

Annual review of cell and developmental biology, 2020-10, Vol.36 (1), p.237-264

2020

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Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1

The EMBO journal, 2015-11, Vol.34 (22), p.2840-2861

2015

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UCHL-1 is not a Parkinson's disease susceptibility gene

Annals of neurology, 2006-04, Vol.59 (4), p.627-633

2006

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PINK1 and Parkin: emerging themes in mitochondrial homeostasis

Current opinion in cell biology, 2017-04, Vol.45, p.83-91

2017

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Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations

eLife, 2017-10, Vol.6

2017

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Expanding insights of mitochondrial dysfunction in Parkinson's disease

Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1

Kinetin Riboside and Its ProTides Activate the Parkinson’s Disease Associated PTEN-Induced Putative Kinase 1 (PINK1) Independent of Mitochondrial Depolarization

PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65

mito-QC illuminates mitophagy and mitochondrial architecture in vivo

A heterozygous effect for PINK1 mutations in Parkinson's disease?

Phosphorylation of Parkin at Serine65 is essential for activation: elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity

TigarB causes mitochondrial dysfunction and neuronal loss in PINK1 deficiency

Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog

The novel MAPT mutation K298E: mechanisms of mutant tau toxicity, brain pathology and tau expression in induced fibroblast-derived neurons

Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress

The Anthelmintic Drug Niclosamide and Its Analogues Activate the Parkinson's Disease Associated Protein Kinase PINK1

Probes of ubiquitin E3 ligases enable systematic dissection of parkin activation

Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation

PINK1-dependent phosphorylation of Serine111 within the SF3 motif of Rab GTPases impairs effector interactions and LRRK2-mediated phosphorylation at Threonine72

Are PARKIN patients ideal candidates for dopaminergic cell replacement therapies?

Therapeutic approaches to enhance PINK1/Parkin mediated mitophagy for the treatment of Parkinson’s disease

Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations

PTEN-induced kinase 1 (PINK1) and Parkin: Unlocking a mitochondrial quality control pathway linked to Parkinson's disease

Parkinson's: A Disease of Aberrant Vesicle Trafficking

Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1

Phosphorylation of Parkin at serine 65 is essential for its activation in vivo

UCHL-1 is not a Parkinson's disease susceptibility gene

PINK1 and Parkin: emerging themes in mitochondrial homeostasis

Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations

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