https://ogma.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 The low affinity dopamine binding site on tyrosine hydroxylase: the role of the N-Terminus and in situ regulation of enzyme activity https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:8116 Sat 24 Mar 2018 08:40:01 AEDT ]]> Differential regulation of human tyrosine hydroxylase isoforms 1 and 2 in situ: isoform 2 is not phosphorylated at Ser35 https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:8022 Sat 24 Mar 2018 08:36:49 AEDT ]]> Expression of tyrosine hydroxylase increases the resistance of human neuroblastoma cells to oxidative insults https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:9573 Sat 24 Mar 2018 08:34:46 AEDT ]]> Differential regulation of the human tyrosine hydroxylase isoforms via hierarchical phosphorylation https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:1185 Sat 24 Mar 2018 08:28:29 AEDT ]]> Tyrosine hydroxylase activity is regulated by two distinct dopamine-binding sites https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:5208 Sat 24 Mar 2018 07:47:45 AEDT ]]> Mutational analysis of catecholamine binding in tyrosine hydroxylase https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:25252 Sat 24 Mar 2018 07:38:16 AEDT ]]>