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Proteasomal degradation of tyrosine hydroxylase and neurodegeneration.
Nakashima A. Nakashima A. J Neurochem. 2012 Jan;120(2):199-201. doi: 10.1111/j.1471-4159.2011.07562.x. J Neurochem. 2012. PMID: 22035286 No abstract available.
Intracellular stability of tyrosine hydroxylase: phosphorylation and proteasomal digestion of the enzyme.
Nakashima A, Kaneko YS, Kodani Y, Mori K, Nagasaki H, Nagatsu T, Ota A. Nakashima A, et al. Adv Pharmacol. 2013;68:3-11. doi: 10.1016/B978-0-12-411512-5.00001-4. Adv Pharmacol. 2013. PMID: 24054137 Review.
Elucidation of the mechanisms regulating the synthesis, degradation, and activity of TH should be a first target in order to understand the role of this enzyme in pathogenesis. Recently, several reports suggest that the ubiquitin-proteasome pathway is a prerequisite …
Elucidation of the mechanisms regulating the synthesis, degradation, and activity of TH should be a first target in order to understa …
Phosphorylation of the N-terminal portion of tyrosine hydroxylase triggers proteasomal digestion of the enzyme.
Nakashima A, Mori K, Kaneko YS, Hayashi N, Nagatsu T, Ota A. Nakashima A, et al. Biochem Biophys Res Commun. 2011 Apr 8;407(2):343-7. doi: 10.1016/j.bbrc.2011.03.020. Epub 2011 Mar 8. Biochem Biophys Res Commun. 2011. PMID: 21392500
Tyrosine hydroxylase (TH) is the rate-limiting enzyme in catecholamine biosynthesis, and its N-terminus plays a critical role in the intracellular stability of the enzyme. ...
Tyrosine hydroxylase (TH) is the rate-limiting enzyme in catecholamine biosynthesis, and its N-terminus plays a critical role in the …
The mutation of two amino acid residues in the N-terminus of tyrosine hydroxylase (TH) dramatically enhances the catalytic activity in neuroendocrine AtT-20 cells.
Nakashima A, Kaneko YS, Mori K, Fujiwara K, Tsugu T, Suzuki T, Nagatsu T, Ota A. Nakashima A, et al. J Neurochem. 2002 Jul;82(1):202-6. doi: 10.1046/j.1471-4159.2002.00921.x. J Neurochem. 2002. PMID: 12091481
The sequence Arg37-Arg38 of tyrosine hydroxylase (TH) is known to play a significant role in the feedback inhibition by the end product DA. ...In a cell-free system, the level of the DA inhibition of the RR-EE mutant enzyme was to the same or smaller degree than tha …
The sequence Arg37-Arg38 of tyrosine hydroxylase (TH) is known to play a significant role in the feedback inhibition by the end produ …
Dopamine inhibition of human tyrosine hydroxylase type 1 is controlled by the specific portion in the N-terminus of the enzyme.
Nakashima A, Mori K, Suzuki T, Kurita H, Otani M, Nagatsu T, Ota A. Nakashima A, et al. J Neurochem. 1999 May;72(5):2145-53. doi: 10.1046/j.1471-4159.1999.0722145.x. J Neurochem. 1999. PMID: 10217296
Tyrosine hydroxylase (TH), which converts L-tyrosine to L-DOPA, is a rate-limiting enzyme in the biosynthesis of catecholamines; its activity is regulated by feedback inhibition by catecholamine products including dopamine. To investigate the specific portion of the N-term …
Tyrosine hydroxylase (TH), which converts L-tyrosine to L-DOPA, is a rate-limiting enzyme in the biosynthesis of catecholamines; its …
Regulation of oxidative stress in long-lived lipopolysaccharide-activated microglia.
Kaneko YS, Ota A, Nakashima A, Mori K, Nagatsu I, Nagatsu T. Kaneko YS, et al. Clin Exp Pharmacol Physiol. 2012 Jul;39(7):599-607. doi: 10.1111/j.1440-1681.2012.05716.x. Clin Exp Pharmacol Physiol. 2012. PMID: 22519637
The study was conducted in microglia obtained from murine neonate brain, which are destined to die within a few days under ordinary culture conditions. 3. ...Because long-lived microglia may play a critical role in the exacerbation of neurodegeneration, bringing act …
The study was conducted in microglia obtained from murine neonate brain, which are destined to die within a few days under ordinary c …
Tetrahydrobiopterin biosynthesis in white and brown adipose tissues is enhanced following intraperitoneal administration of bacterial lipopolysaccharide.
Fujiwara K, Mori K, Kaneko YS, Nakashima A, Nagasaka A, Itoh M, Ota A. Fujiwara K, et al. Biochim Biophys Acta. 2004 Feb 24;1670(3):181-98. doi: 10.1016/j.bbagen.2003.12.004. Biochim Biophys Acta. 2004. PMID: 14980445
Collectively, our results showed that tetrahydrobiopterin biosynthesis can be augmented by increased GCH activity caused by a synergistic effect of lipopolysaccharide and cytokines in white and brown adipose tissues. These observations support the view that tetrahydrobiopt …
Collectively, our results showed that tetrahydrobiopterin biosynthesis can be augmented by increased GCH activity caused by a synergi …
RNAi of 14-3-3eta protein increases intracellular stability of tyrosine hydroxylase.
Nakashima A, Hayashi N, Kaneko YS, Mori K, Sabban EL, Nagatsu T, Ota A. Nakashima A, et al. Biochem Biophys Res Commun. 2007 Nov 23;363(3):817-21. doi: 10.1016/j.bbrc.2007.09.042. Epub 2007 Sep 21. Biochem Biophys Res Commun. 2007. PMID: 17900529
Tyrosine hydroxylase is the rate-limiting enzyme in catecholamine biosynthesis, and its N-terminus plays a critical role in the intracellular stability of the enzyme. ...
Tyrosine hydroxylase is the rate-limiting enzyme in catecholamine biosynthesis, and its N-terminus plays a critical role in the intra …
Peripheral injection of lipopolysaccharide enhances expression of inflammatory cytokines in murine locus coeruleus: possible role of increased norepinephrine turnover.
Kaneko YS, Mori K, Nakashima A, Sawada M, Nagatsu I, Ota A. Kaneko YS, et al. J Neurochem. 2005 Jul;94(2):393-404. doi: 10.1111/j.1471-4159.2005.03209.x. J Neurochem. 2005. PMID: 15998290
Cytokines and catecholamines are known to constitute a significant portion of the regulatory neuroimmune networks involved in maintaining homeostasis in the central nervous system (CNS). ...This report, based on the results of both in vivo and in vitro experiments, is the …
Cytokines and catecholamines are known to constitute a significant portion of the regulatory neuroimmune networks involved in maintai …
Deletion of N-terminus of human tyrosine hydroxylase type 1 enhances stability of the enzyme in AtT-20 cells.
Nakashima A, Hayashi N, Kaneko YS, Mori K, Egusa H, Nagatsu T, Ota A. Nakashima A, et al. J Neurosci Res. 2005 Jul 1;81(1):110-20. doi: 10.1002/jnr.20540. J Neurosci Res. 2005. PMID: 15898085
Wildtype human tyrosine hydroxylase (TH) type 1 and 4 mutants (del-52, a form with the first 52 amino acid residues deleted; del-157, one with the first 157 amino acid residues deleted; RR-EE, one in which Arg37-Arg38 was replaced by Glu37-Glu38; and S40D, one in which Ser …
Wildtype human tyrosine hydroxylase (TH) type 1 and 4 mutants (del-52, a form with the first 52 amino acid residues deleted; del-157, …
772 results
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