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Article

RNAi of 14-3-3eta protein increases intracellular stability of tyrosine hydroxylase.

Biochemical and biophysical research communications - 23 Nov 2007

Nakashima Akira, Hayashi Nobuhiro, Kaneko Yoko S, Mori Keiji, Sabban Esther L, Nagatsu Toshiharu, Ota Akira

Abstract excerpt

Tyrosine hydroxylase is the rate-limiting enzyme in catecholamine biosynthesis, and its N-terminus plays a critical role in the intracellular stability of the enzyme. In the present study, we investigated the mechanism by which the N-terminus of human tyrosine hydroxylase type 1 (hTH1) affects the stability. The results obtained by using N-terminus-deleted hTH1 mutants identified the sequence up to Ala(23) as...

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Identifiers

PMID: 17900529
DOI: 10.1016/j.bbrc.2007.09.042

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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