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Pathological roles of α-synuclein in neurological disorders

Lancet neurology, 2011-11, Vol.10 (11), p.1015-1025

2011

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The Neurobiology of LRRK2 and its Role in the Pathogenesis of Parkinson’s Disease

Neurochemical research, 2014-03, Vol.39 (3), p.576-592

2014

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Kinase activity of mutant LRRK2 manifests differently in hetero-dimeric vs homo-dimeric complexes

Biochemical journal, 2019-02, Vol.476 (3), p.559-579

2019

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LRRK2 Parkinson disease mutations enhance its microtubule association

Human molecular genetics, 2012-02, Vol.21 (4), p.890-899

2012

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Activation of FADD-Dependent Neuronal Death Pathways as a Predictor of Pathogenicity for LRRK2 Mutations

PloS one, 2016-11, Vol.11 (11), p.e0166053-e0166053

2016

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The WD40 domain is required for LRRK2 neurotoxicity

PloS one, 2009-12, Vol.4 (12), p.e8463

2009

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Defining (and blocking) neuronal death in Parkinson’s disease: Does it matter what we call it?

Brain research, 2021-11, Vol.1771, p.147639-147639, Article 147639

2021

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Nurr1: RXRα heterodimer activation as monotherapy for Parkinson’s disease

Proceedings of the National Academy of Sciences - PNAS, 2017-04, Vol.114 (15), p.3999-4004

2017

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A motif within the armadillo repeat of Parkinson's-linked LRRK2 interacts with FADD to hijack the extrinsic death pathway

Scientific reports, 2018-02, Vol.8 (1), p.3455-17, Article 3455

2018

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Is spinal muscular atrophy a disease of the motor neurons only: pathogenesis and therapeutic implications?

Cellular and molecular life sciences : CMLS, 2016-03, Vol.73 (5), p.1003-1020

2016

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Why the Gut Microbiome Must Be Considered When Evaluating the Impact of Pesticides on Parkinson’s Disease Risk

Journal of Parkinson's disease, 2023-01, Vol.13 (7), p.1077-1078

2023

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P62/SQSTM1 is a novel leucine-rich repeat kinase 2 (LRRK2) substrate that enhances neuronal toxicity

Biochemical journal, 2018-04, Vol.475 (7), p.1271-1293

2018

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The Parkinson Disease Protein Leucine-Rich Repeat Kinase 2 Transduces Death Signals via Fas-Associated Protein with Death Domain and Caspase-8 in a Cellular Model of Neurodegeneration

The Journal of neuroscience, 2009-01, Vol.29 (4), p.1011-1016

2009

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The Future of Targeted Gene-Based Treatment Strategies and Biomarkers in Parkinson's Disease

Biomolecules (Basel, Switzerland), 2020-06, Vol.10 (6), p.912

2020

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Leucine-Rich Repeat Kinase 2 (LRRK2)

1, 2017

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Elevated In Vitro Kinase Activity in Peripheral Blood Mononuclear Cells of Leucine‐Rich Repeat Kinase 2 G2019S Carriers: A Novel Enzyme‐Linked Immunosorbent Assay–Based Method

Movement disorders, 2020-11, Vol.35 (11), p.2095-2100

2020

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Longitudinal transcriptomic analysis of mouse sciatic nerve reveals pathways associated with age‐related muscle pathology

Journal of cachexia, sarcopenia and muscle, 2023-06, Vol.14 (3), p.1322-1336

2023

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Perspective on the current state of the LRRK2 field

NPJ Parkinson's Disease, 2023-07, Vol.9 (1), p.104-104, Article 104

2023

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Involvement of macroautophagy in the dissolution of neuronal inclusions

The international journal of biochemistry & cell biology, 2004-12, Vol.36 (12), p.2551-2562

2004

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Expression of A53T Mutant But Not Wild-Type alpha -Synuclein in PC12 Cells Induces Alterations of the Ubiquitin-Dependent Degradation System, Loss of Dopamine Release, and Autophagic Cell Death

The Journal of neuroscience, 2001-12, Vol.21 (24), p.9549-9560

2001

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Distinct profiles of LRRK2 activation and Rab GTPase phosphorylation in clinical samples from different PD cohorts

NPJ Parkinson's Disease, 2022-06, Vol.8 (1), p.73-73, Article 73

2022

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Proteasomal inhibition leads to formation of ubiquitin/α‐synuclein‐immunoreactive inclusions in PC12 cells

Journal of neurochemistry, 2001-08, Vol.78 (4), p.899-908

2001

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LRRK2 and the “LRRKtosome” at the Crossroads of Programmed Cell Death: Clues from RIP Kinase Relatives

Leucine-Rich Repeat Kinase 2 (LRRK2), 2017-01, p.193-208

2017

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Disruption of the LRRK2‐FADD Interface Using Constrained Peptides

Peptide science (Hoboken, N.J.), 2024-07

2024

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Insights into the Influence of Specific Splicing Events on the Structural Organization of LRRK2

International journal of molecular sciences, 2018-09, Vol.19 (9), p.2784

2018

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Pathological roles of α-synuclein in neurological disorders

The Neurobiology of LRRK2 and its Role in the Pathogenesis of Parkinson’s Disease

Kinase activity of mutant LRRK2 manifests differently in hetero-dimeric vs homo-dimeric complexes

LRRK2 Parkinson disease mutations enhance its microtubule association

Activation of FADD-Dependent Neuronal Death Pathways as a Predictor of Pathogenicity for LRRK2 Mutations

The WD40 domain is required for LRRK2 neurotoxicity

Defining (and blocking) neuronal death in Parkinson’s disease: Does it matter what we call it?

Nurr1: RXRα heterodimer activation as monotherapy for Parkinson’s disease

A motif within the armadillo repeat of Parkinson's-linked LRRK2 interacts with FADD to hijack the extrinsic death pathway

Is spinal muscular atrophy a disease of the motor neurons only: pathogenesis and therapeutic implications?

Why the Gut Microbiome Must Be Considered When Evaluating the Impact of Pesticides on Parkinson’s Disease Risk

P62/SQSTM1 is a novel leucine-rich repeat kinase 2 (LRRK2) substrate that enhances neuronal toxicity

The Parkinson Disease Protein Leucine-Rich Repeat Kinase 2 Transduces Death Signals via Fas-Associated Protein with Death Domain and Caspase-8 in a Cellular Model of Neurodegeneration

The Future of Targeted Gene-Based Treatment Strategies and Biomarkers in Parkinson's Disease

Leucine-Rich Repeat Kinase 2 (LRRK2)

Elevated In Vitro Kinase Activity in Peripheral Blood Mononuclear Cells of Leucine‐Rich Repeat Kinase 2 G2019S Carriers: A Novel Enzyme‐Linked Immunosorbent Assay–Based Method

Longitudinal transcriptomic analysis of mouse sciatic nerve reveals pathways associated with age‐related muscle pathology

Perspective on the current state of the LRRK2 field

Involvement of macroautophagy in the dissolution of neuronal inclusions

Expression of A53T Mutant But Not Wild-Type alpha -Synuclein in PC12 Cells Induces Alterations of the Ubiquitin-Dependent Degradation System, Loss of Dopamine Release, and Autophagic Cell Death

Distinct profiles of LRRK2 activation and Rab GTPase phosphorylation in clinical samples from different PD cohorts

Proteasomal inhibition leads to formation of ubiquitin/α‐synuclein‐immunoreactive inclusions in PC12 cells

LRRK2 and the “LRRKtosome” at the Crossroads of Programmed Cell Death: Clues from RIP Kinase Relatives

Disruption of the LRRK2‐FADD Interface Using Constrained Peptides

Insights into the Influence of Specific Splicing Events on the Structural Organization of LRRK2

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