Inhibition-mediated changes in prolyl oligopeptidase dynamics possibly related to α-synuclein aggregation
Author:
Affiliation:
1. Faculty of Physics, Astronomy and Informatics, Nicolaus Copernicus University in Toruń, 87-100 Toruń, Poland
2. Faculty of Mathematics, Physics and Informatics, Gdansk University, Wita Stwosza 57, 80-952 Gdańsk, Poland
Abstract
Funder
Uniwersytet Mikolaja Kopernika w Toruniu
Fundacja na rzecz Nauki Polskiej
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2022/CP/D1CP05238A
Reference51 articles.
1. Leucylglycinamide Released from Oxytocin by Human Uterine Enzyme
2. Structure, Function and Biological Relevance of Prolyl Oligopeptidase
3. On the role of prolyl oligopeptidase in health and disease
4. Suggested functions for prolyl oligopeptidase: A puzzling paradox
5. New tricks of prolyl oligopeptidase inhibitors – A common drug therapy for several neurodegenerative diseases
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