@inbook{2845407a425243a192e7c363e07495af,
title = "Intracellular stability of tyrosine hydroxylase. Phosphorylation and proteasomal digestion of the enzyme.",
abstract = "Tyrosine hydroxylase (TH), the rate-limiting enzyme in the biosynthesis of catecholamines, is a key protein involved in the pathogenesis of neurodegenerative diseases such as Parkinson's disease. Elucidation of the mechanisms regulating the synthesis, degradation, and activity of TH should be a first target in order to understand the role of this enzyme in pathogenesis. Recently, several reports suggest that the ubiquitin-proteasome pathway is a prerequisite for the degradation of TH and that the N-terminal part of TH plays a critical role in the degradation. In this report, we propose the mechanism by which the N-terminal part of TH regulates the degradation of this enzyme. Moreover, we integrate our findings with recent progress in other areas of TH regulation.",
author = "Akira Nakashima and Kaneko, {Yoko S.} and Yu Kodani and Keiji Mori and Hiroshi Nagasaki and Toshiharu Nagatsu and Akira Ota",
note = "Funding Information: This work was supported by JSPS KAKENHI Grant Number 20180276 and also by a grant from Fujita Health University.",
year = "2013",
doi = "10.1016/B978-0-12-411512-5.00001-4",
language = "English",
series = "Advances in Pharmacology",
publisher = "Academic Press Inc.",
pages = "3--11",
booktitle = "Advances in Pharmacology",
address = "United States",
}