FIND

researchers

DISCOVER

relevant articles

PROMOTE

your research

REGISTER

now for free

RI McCulloch

Research Profile

Chemicals & Drugs

Concepts & Ideas

Kinetics

Living Beings

Rats

Physiology

Phenomena

Register to see full profile

Co-author Network

Co-Publications
Name
3
Paul Fitzpatrick
2
Susan Colette Daubner
1
Holly Ellis

Register to see all co-authors

Publications

TOP 3
RI McCulloch; Susan Colette Daubner; Paul F Fitzpatrick
Effects of substitution at serine 40 of tyrosine hydroxylase on catecholamine binding.
Holly R Ellis; Susan Colette Daubner; RI McCulloch; Paul F Fitzpatrick
Phenylalanine residues in the active site of tyrosine hydroxylase: mutagenesis of Phe300 and Phe309 to alanine and metal ion-catalyzed hydroxylation of Phe300.
RI McCulloch; Paul F Fitzpatrick
Limited proteolysis of tyrosine hydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding.

Register to see all publications

Register for free to view:

Visualized networks:

See your personal network in
sophisticated graphical views

GeoTargeted Searches:

Locate experts around the world
and connect with global collaborators

Research Profiles:

See the research activity
of experts around the globe

Register to see more

Geonetwork of RI McCulloch (preview)

Cities where this author has publications
Cities where co-authors of this author have publications

Flash Player Required

Register to see more

All Publications

2001: RI McCulloch; Susan Colette Daubner; Paul F Fitzpatrick
Effects of substitution at serine 40 of tyrosine hydroxylase on catecholamine binding.
Biochemistry 2001;40(24):7273-8.
1999: Holly R Ellis; Susan Colette Daubner; RI McCulloch; Paul F Fitzpatrick
Phenylalanine residues in the active site of tyrosine hydroxylase: mutagenesis of Phe300 and Phe309 to alanine and metal ion-catalyzed hydroxylation of Phe300.
Biochemistry 1999;38(34):10909-14.
1999: RI McCulloch; Paul F Fitzpatrick
Limited proteolysis of tyrosine hydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding.
Archives of biochemistry and biophysics 1999;367(1):143-5.

Register to see more

Copyright © 2011 Elsevier Inc. All rights reserved.