Limited proteolysis of tyrosine rydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding

Ruth I. McCulloch; Paul F. Fitzpatrick

doi:10.1006/abbi.1999.1259

Limited proteolysis of tyrosine rydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding

Ruth I. McCulloch, Paul F. Fitzpatrick

Department of Biochemistry & Structural Biology

Research output: Contribution to journal › Article › peer-review

28 Scopus citations

Original language	English (US)
Pages (from-to)	143-145
Number of pages	3
Journal	Archives of Biochemistry and Biophysics
Volume	367
Issue number	1
DOIs	https://doi.org/10.1006/abbi.1999.1259
State	Published - Jul 1 1999

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1006/abbi.1999.1259

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title = "Limited proteolysis of tyrosine rydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding",

author = "McCulloch, {Ruth I.} and Fitzpatrick, {Paul F.}",

note = "Funding Information: 1This research was supported in part by NIH Grant GM 47291 and Robert A. Welch Foundation Grant A-1245. 2To whom correspondence should be addressed. Fax: (409) 845-9274. E-mail: fitzpat@tamu.edu.",

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T1 - Limited proteolysis of tyrosine rydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding

AU - McCulloch, Ruth I.

AU - Fitzpatrick, Paul F.

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AN - SCOPUS:0033167087

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Limited proteolysis of tyrosine rydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding

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