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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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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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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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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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Leucine-Rich Repeat Kinase 2 (LRRK2)

1, 2017

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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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Disruption of the LRRK2‐FADD Interface Using Constrained Peptides

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

2024

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Leucine rich repeat kinase 2 (LRRK2) peptide modulators: Recent advances and future directions

Peptide science (Hoboken, N.J.), 2022-01, Vol.114 (1), p.n/a

2022

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Models of LRRK2-Associated Parkinson’s Disease

Leucine-Rich Repeat Kinase 2 (LRRK2), 2017-01, p.163-191

2017

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Cyclin-Dependent Kinase Activity Is Required for Apoptotic Death But Not Inclusion Formation in Cortical Neurons after Proteasomal Inhibition

The Journal of neuroscience, 2003-02, Vol.23 (4), p.1237-1245

2003

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Mechanisms of Caspase-Independent Neuronal Death: Energy Depletion and Free Radical Generation

The Journal of neuroscience, 2003-12, Vol.23 (35), p.11015-11025

2003

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Understanding the GTPase Activity of LRRK2: Regulation, Function, and Neurotoxicity

Leucine-Rich Repeat Kinase 2 (LRRK2), 2017-01, p.71-88

2017

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Small-Molecule Inhibitors of LRRK2

Advances in neurobiology, 2017-01, Vol.14, p.241-264

2017

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alpha-synuclein is required for the fibrillar nature of ubiquitinated inclusions induced by proteasomal inhibition in primary neurons

The Journal of biological chemistry, 2004-11, Vol.279 (45), p.46915-46920

2004

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Cyclin-Dependent Kinases and P53 Pathways Are Activated Independently and Mediate Bax Activation in Neurons after DNA Damage

The Journal of neuroscience, 2001-07, Vol.21 (14), p.5017-5026

2001

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LRRK2 Phosphorylation

Advances in neurobiology, 2017-01, Vol.14, p.51-70

2017

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Regulation of LRRK2 by Phosphatases

Advances in neurobiology, 2017-01, Vol.14, p.145-160

2017

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Vitamin B 12 modulates Parkinson's disease LRRK2 kinase activity through allosteric regulation and confers neuroprotection

Cell research, 2019-04, Vol.29 (4), p.313

2019

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Allosteric Inhibition of Parkinson’s-Linked LRRK2 by Constrained Peptides

ACS chemical biology, 2021-11, Vol.16 (11), p.2326-2338

2021

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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)

2020

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Pathological roles of [alpha]-synuclein in neurological disorders

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

2011

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Pathological roles of α-synuclein in neurological disorders

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

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

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

Leucine-Rich Repeat Kinase 2 (LRRK2)

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

Disruption of the LRRK2‐FADD Interface Using Constrained Peptides

Leucine rich repeat kinase 2 (LRRK2) peptide modulators: Recent advances and future directions

Models of LRRK2-Associated Parkinson’s Disease

Cyclin-Dependent Kinase Activity Is Required for Apoptotic Death But Not Inclusion Formation in Cortical Neurons after Proteasomal Inhibition

Mechanisms of Caspase-Independent Neuronal Death: Energy Depletion and Free Radical Generation

Understanding the GTPase Activity of LRRK2: Regulation, Function, and Neurotoxicity

Small-Molecule Inhibitors of LRRK2

alpha-synuclein is required for the fibrillar nature of ubiquitinated inclusions induced by proteasomal inhibition in primary neurons

Cyclin-Dependent Kinases and P53 Pathways Are Activated Independently and Mediate Bax Activation in Neurons after DNA Damage

LRRK2 Phosphorylation

Regulation of LRRK2 by Phosphatases

Vitamin B 12 modulates Parkinson's disease LRRK2 kinase activity through allosteric regulation and confers neuroprotection

Allosteric Inhibition of Parkinson’s-Linked LRRK2 by Constrained Peptides

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

Pathological roles of [alpha]-synuclein in neurological disorders

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