5-Aminothiazoles Reveal a New Ligand-Binding Site on Prolyl Oligopeptidase Which is Important for Modulation of Its Protein–Protein Interaction-Derived Functions-Reference-Cited by-同舟云学术

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

Published:2024-03-28 Issue:7 Volume:67 Page:5421-5436
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Pätsi Henri T.¹^ORCID,Kilpeläinen Tommi P.²^ORCID,Jumppanen Mikael¹^ORCID,Uhari-Väänänen Johanna²^ORCID,Wielendaele Pieter Van³^ORCID,De Lorenzo Francesca²^ORCID,Cui Hengjing⁴^ORCID,Auno Samuli²^ORCID,Saharinen Janne¹,Seppälä Erin⁵^ORCID,Sipari Nina⁶^ORCID,Savinainen Juha⁵^ORCID,De Meester Ingrid³^ORCID,Lambeir Anne-Marie³^ORCID,Lahtela-Kakkonen Maija⁴^ORCID,Myöhänen Timo T.²⁴⁷^ORCID,Wallén Erik A. A.¹^ORCID

Affiliation:

1. Drug Research Program, Division of Pharmaceutical Chemistry and Technology, Faculty of Pharmacy, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland

2. Drug Research Program, Division of Pharmacology and Pharmacotherapy, Faculty of Pharmacy, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland

3. Laboratory of Medical Biochemistry, Department of Pharmaceutical Sciences, Faculty of Pharmaceutical, Biomedical and Veterinary Sciences, University of Antwerp, 2610 Wilrijk, Belgium

4. School of Pharmacy, Faculty of Health Sciences, University of Eastern Finland, Yliopistonranta 1C, 70211 Kuopio, Finland

5. School of Medicine/Biomedicine, Faculty of Health Sciences, University of Eastern Finland, Yliopistonranta 8, Kuopio 70211, Finland

6. Viikki Metabolomics Unit, Faculty of Biological and Environmental Sciences, University of Helsinki, Viikinkaari 5 E, 00014 Helsinki, Finland

7. Division of Pharmacology, Faculty of Medicine, University of Helsinki, P.O.Box 63, 00014 Helsinki, Finland

Funder

Sigrid Jus?liuksen S??ti?

Helsinki Institute of Life Science, Helsingin Yliopisto

Research Council of Finland

Business Finland

P?ivikki ja Sakari Sohlbergin S??ti?

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.3c01993

Reference34 articles.

1. 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

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

3. Prolyl oligopeptidase inhibition activates autophagy via protein phosphatase 2A

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

5. Prolyl oligopeptidase inhibition reduces oxidative stress via reducing NADPH oxidase activity by activating protein phosphatase 2A

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