Fluorescence spectroscopy as a probe of the effect of phosphorylation at serine 40 of tyrosine hydroxylase on the conformation of its regulatory domain.

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Bibliographic Details
Title: Fluorescence spectroscopy as a probe of the effect of phosphorylation at serine 40 of tyrosine hydroxylase on the conformation of its regulatory domain.
Authors: Wang S; Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States., Lasagna M, Daubner SC, Reinhart GD, Fitzpatrick PF
Source: Biochemistry [Biochemistry] 2011 Mar 29; Vol. 50 (12), pp. 2364-70. Date of Electronic Publication: 2011 Feb 22.
Publication Type: Journal Article; Research Support, N.I.H., Extramural
Journal Info: Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370623 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-4995 (Electronic) Linking ISSN: 00062960 NLM ISO Abbreviation: Biochemistry Subsets: MEDLINE
Database: MEDLINE Ultimate
Description
ISSN:1520-4995
DOI:10.1021/bi101844p