Tyrosine hydroxylase in rat brain dopaminergic nerve termina…
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- DOI 10.1016/s0021-9258(19)67644-1
- PMID https://pubmed.ncbi.nlm.nih.gov/1672315
- OpenAlex ID W2113083939
- Type Article
- Language EN
- Published 01 Mar 1991
- Volume 266 (9)
- Pages 5650–5657
- Source Journal of Biological Chemistry
- Publisher Elsevier BV
- FWCI 2.57
- Countries 1
- Institutions 3
- Added 24 Jun 2016
- Updated 16 Oct 2026
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Tyrosine hydroxylase in rat brain dopaminergic nerve terminals. Multiple-site phosphorylation in vivo and in synaptosomes.
Article 1991 EN Hybrid
Tyrosine hydroxylase, which catalyzes the initial step in catecholamine biosynthesis, is phosphorylated at serines 8, 19, 31, and 40 in intact pheochromocytoma (PC12) cells (Haycock, J.W. (1990) J. Biol. Chem. 265, 11682-11691). After 32Pi labeling of rat corpus striata in vivo or rat corpus striatal synaptosomes, 32P incorporation into tyrosine hydroxylase occurred predominantly at serines 19, 31…
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2 authors| # | Author | Institutions | ORCID |
|---|---|---|---|
| 1 | John W. Haycock | Louisiana State University (US) University Medical Center New … (US) +1 | |
| 2 | Dean A. Haycock | Louisiana State University (US) University Medical Center New … (US) +1 | — |
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