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New tricks of prolyl oligopeptidase inhibitors – A common drug therapy for several neurodegenerative diseases

Biochemical pharmacology, 2019-03, Vol.161, p.113-120

2019

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Inhibition of Prolyl Oligopeptidase Restores Spontaneous Motor Behavior in the α-Synuclein Virus Vector-Based Parkinson's Disease Mouse Model by Decreasing α-Synuclein Oligomeric Species in Mouse Brain

The Journal of neuroscience, 2016-12, Vol.36 (49), p.12485-12497

2016

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Deletion or inhibition of prolyl oligopeptidase blocks lithium‐induced phosphorylation of GSK3b and Akt by activation of protein phosphatase 2A

Basic & clinical pharmacology & toxicology, 2021-10, Vol.129 (4), p.287-296

2021

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5‑Aminothiazoles Reveal a New Ligand-Binding Site on Prolyl Oligopeptidase Which is Important for Modulation of Its Protein–Protein Interaction-Derived Functions

Journal of medicinal chemistry, 2024-04, Vol.67 (7), p.5421-5436

2024

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Removal of prolyl oligopeptidase reduces alpha-synuclein toxicity in cells and in vivo

Scientific reports, 2018-01, Vol.8 (1), p.1552-18, Article 1552

2018

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The beneficial effect of a prolyl oligopeptidase inhibitor, KYP-2047, on alpha-synuclein clearance and autophagy in A30P transgenic mouse

Neurobiology of disease, 2014-08, Vol.68, p.1-15

2014

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Prolyl oligopeptidase inhibition reduces PolyQ aggregation and improves cell viability in cellular model of Huntington’s disease

Journal of cellular and molecular medicine, 2019-12, Vol.23 (12), p.8511-8515

2019

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Behavioural and dopaminergic changes in double mutated human A30PA53T alpha-synuclein transgenic mouse model of Parkinson´s disease

Scientific reports, 2019-11, Vol.9 (1), p.17382-13, Article 17382

2019

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Prolyl oligopeptidase inhibition activates autophagy via protein phosphatase 2A

Pharmacological research, 2020-01, Vol.151, p.104558, Article 104558

2020

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Nonpeptidic Oxazole-Based Prolyl Oligopeptidase Ligands with Disease-Modifying Effects on α‑Synuclein Mouse Models of Parkinson’s Disease

Journal of medicinal chemistry, 2023-06, Vol.66 (11), p.7475-7496

2023

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Prolyl Oligopeptidase Enhances α-Synuclein Dimerization via Direct Protein-Protein Interaction

The Journal of biological chemistry, 2015-02, Vol.290 (8), p.5117-5126

2015

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Nigral injection of a proteasomal inhibitor, lactacystin, induces widespread glial cell activation and shows various phenotypes of Parkinson’s disease in young and adult mouse

Experimental brain research, 2017-07, Vol.235 (7), p.2189-2202

2017

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Nigrostriatal 6-hydroxydopamine lesions increase alpha-synuclein levels and permeability in rat colon

Neurobiology of aging, 2023-09, Vol.129, p.62-71

2023

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The effect of prolyl oligopeptidase inhibitors on alpha-synuclein aggregation and autophagy cannot be predicted by their inhibitory efficacy

Biomedicine & pharmacotherapy, 2020-08, Vol.128, p.110253, Article 110253

2020

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Prolyl Oligopeptidase Regulates Dopamine Transporter Oligomerization and Phosphorylation in a PKC- and ERK-Independent Manner

International journal of molecular sciences, 2021-02, Vol.22 (4), p.1777

2021

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Prolyl oligopeptidase inhibition attenuates the toxicity of a proteasomal inhibitor, lactacystin, in the alpha-synuclein overexpressing cell culture

Neuroscience letters, 2017-01, Vol.636, p.83-89

2017

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Removal of proteinase K resistant αSyn species does not correlate with cell survival in a virus vector-based Parkinson's disease mouse model

Neuropharmacology, 2022-11, Vol.218, p.109213-109213, Article 109213

2022

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Prolyl oligopeptidase inhibition reduces alpha‐synuclein aggregation in a cellular model of multiple system atrophy

Journal of cellular and molecular medicine, 2021-10, Vol.25 (20), p.9634-9646

2021

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Inhibition of prolyl oligopeptidase increases the survival of alpha-synuclein overexpressing cells after rotenone exposure by reducing alpha-synuclein oligomers

Neuroscience letters, 2014-11, Vol.583, p.37-42

2014

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Distribution of catechol-O-methyltransferase (COMT) proteins and enzymatic activities in wild-type and soluble COMT deficient mice

Journal of neurochemistry, 2010-06, Vol.113 (6), p.1632-1643

2010

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A prolyl oligopeptidase inhibitor reduces tau pathology in cellular models and in mice with tauopathy

Science translational medicine, 2023-04, Vol.15 (691), p.eabq2915

2023

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2‑Imidazole as a Substitute for the Electrophilic Group Gives Highly Potent Prolyl Oligopeptidase Inhibitors

ACS medicinal chemistry letters, 2021-10, Vol.12 (10), p.1578-1584

2021

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Tetrazole as a Replacement of the Electrophilic Group in Characteristic Prolyl Oligopeptidase Inhibitors

ACS medicinal chemistry letters, 2019-12, Vol.10 (12), p.1635-1640

2019

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Issues About the Physiological Functions of Prolyl Oligopeptidase Based on Its Discordant Spatial Association With Substrates and Inconsistencies Among mRNA, Protein Levels, and Enzymatic Activity

The journal of histochemistry and cytochemistry, 2009-09, Vol.57 (9), p.831-848

2009

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Distribution of Prolyl Oligopeptidase in Human Peripheral Tissues and in Ovarian and Colorectal Tumors

The journal of histochemistry and cytochemistry, 2012-09, Vol.60 (9), p.706-715

2012

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New tricks of prolyl oligopeptidase inhibitors – A common drug therapy for several neurodegenerative diseases

Inhibition of Prolyl Oligopeptidase Restores Spontaneous Motor Behavior in the α-Synuclein Virus Vector-Based Parkinson's Disease Mouse Model by Decreasing α-Synuclein Oligomeric Species in Mouse Brain

Deletion or inhibition of prolyl oligopeptidase blocks lithium‐induced phosphorylation of GSK3b and Akt by activation of protein phosphatase 2A

5‑Aminothiazoles Reveal a New Ligand-Binding Site on Prolyl Oligopeptidase Which is Important for Modulation of Its Protein–Protein Interaction-Derived Functions

Removal of prolyl oligopeptidase reduces alpha-synuclein toxicity in cells and in vivo

The beneficial effect of a prolyl oligopeptidase inhibitor, KYP-2047, on alpha-synuclein clearance and autophagy in A30P transgenic mouse

Prolyl oligopeptidase inhibition reduces PolyQ aggregation and improves cell viability in cellular model of Huntington’s disease

Behavioural and dopaminergic changes in double mutated human A30PA53T alpha-synuclein transgenic mouse model of Parkinson´s disease

Prolyl oligopeptidase inhibition activates autophagy via protein phosphatase 2A

Nonpeptidic Oxazole-Based Prolyl Oligopeptidase Ligands with Disease-Modifying Effects on α‑Synuclein Mouse Models of Parkinson’s Disease

Prolyl Oligopeptidase Enhances α-Synuclein Dimerization via Direct Protein-Protein Interaction

Nigral injection of a proteasomal inhibitor, lactacystin, induces widespread glial cell activation and shows various phenotypes of Parkinson’s disease in young and adult mouse

Nigrostriatal 6-hydroxydopamine lesions increase alpha-synuclein levels and permeability in rat colon

The effect of prolyl oligopeptidase inhibitors on alpha-synuclein aggregation and autophagy cannot be predicted by their inhibitory efficacy

Prolyl Oligopeptidase Regulates Dopamine Transporter Oligomerization and Phosphorylation in a PKC- and ERK-Independent Manner

Prolyl oligopeptidase inhibition attenuates the toxicity of a proteasomal inhibitor, lactacystin, in the alpha-synuclein overexpressing cell culture

Removal of proteinase K resistant αSyn species does not correlate with cell survival in a virus vector-based Parkinson's disease mouse model

Prolyl oligopeptidase inhibition reduces alpha‐synuclein aggregation in a cellular model of multiple system atrophy

Inhibition of prolyl oligopeptidase increases the survival of alpha-synuclein overexpressing cells after rotenone exposure by reducing alpha-synuclein oligomers

Distribution of catechol-O-methyltransferase (COMT) proteins and enzymatic activities in wild-type and soluble COMT deficient mice

A prolyl oligopeptidase inhibitor reduces tau pathology in cellular models and in mice with tauopathy

2‑Imidazole as a Substitute for the Electrophilic Group Gives Highly Potent Prolyl Oligopeptidase Inhibitors

Tetrazole as a Replacement of the Electrophilic Group in Characteristic Prolyl Oligopeptidase Inhibitors

Issues About the Physiological Functions of Prolyl Oligopeptidase Based on Its Discordant Spatial Association With Substrates and Inconsistencies Among mRNA, Protein Levels, and Enzymatic Activity

Distribution of Prolyl Oligopeptidase in Human Peripheral Tissues and in Ovarian and Colorectal Tumors

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