(Q40721425)

English

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

scientific article published on July 2002

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scholarly article

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Europe PubMed Central

PubMed publication ID

23 September 2017

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 (English)

1 reference

Europe PubMed Central

PubMed publication ID

23 September 2017

Takahiro Suzuki

6

object named as

Takahiro Suzuki

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Europe PubMed Central

PubMed publication ID

23 September 2017

author name string

Akira Nakashima

1

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Europe PubMed Central

PubMed publication ID

23 September 2017

Yoko S Kaneko

2

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Europe PubMed Central

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23 September 2017

Keiji Mori

3

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Europe PubMed Central

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23 September 2017

Kentaro Fujiwara

4

1 reference

Europe PubMed Central

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23 September 2017

Toshimitsu Tsugu

5

1 reference

Europe PubMed Central

PubMed publication ID

23 September 2017

Toshiharu Nagatsu

7

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23 September 2017

Akira Ota

8

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Europe PubMed Central

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23 September 2017

language of work or name

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publication date

1 July 2002

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Europe PubMed Central

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23 September 2017

number of pages

5

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Journal of Neurochemistry

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23 September 2017

82

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23 September 2017

1

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23 September 2017

202-206

1 reference

Europe PubMed Central

PubMed publication ID

23 September 2017

Retroviral transfer of a human tyrosine hydroxylase cDNA in various cell lines: regulated release of dopamine in mouse anterior pituitary AtT-20 cells

1 reference

https://api.crossref.org/works/10.1046%2FJ.1471-4159.2002.00921.X

21 January 2018

In vivo release of dopa and dopamine from genetically engineered cells grafted to the denervated rat striatum

1 reference

https://api.crossref.org/works/10.1046%2FJ.1471-4159.2002.00921.X

21 January 2018

Structure and function of the aromatic amino acid hydroxylases.

1 reference

https://api.crossref.org/works/10.1046%2FJ.1471-4159.2002.00921.X

21 January 2018

Structural basis of autoregulation of phenylalanine hydroxylase

1 reference

https://api.crossref.org/works/10.1046%2FJ.1471-4159.2002.00921.X

21 January 2018

Effects of substitution at serine 40 of tyrosine hydroxylase on catecholamine binding

1 reference

https://api.crossref.org/works/10.1046%2FJ.1471-4159.2002.00921.X

21 January 2018

Dopamine inhibition of human tyrosine hydroxylase type 1 is controlled by the specific portion in the N-terminus of the enzyme.

1 reference

https://api.crossref.org/works/10.1046%2FJ.1471-4159.2002.00921.X

21 January 2018

Effects of dopamine on N-terminus-deleted human tyrosine hydroxylase type 1 expressed in Escherichia coli.

1 reference

https://api.crossref.org/works/10.1046%2FJ.1471-4159.2002.00921.X

21 January 2018

Triple transduction with adeno-associated virus vectors expressing tyrosine hydroxylase, aromatic-L-amino-acid decarboxylase, and GTP cyclohydrolase I for gene therapy of Parkinson's disease

1 reference

https://api.crossref.org/works/10.1046%2FJ.1471-4159.2002.00921.X

21 January 2018

Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2

1 reference

https://api.crossref.org/works/10.1046%2FJ.1471-4159.2002.00921.X

21 January 2018

Synthesis of L-3,4-dihydroxyphenylalanine by tyrosine hydroxylase cDNA-transfected C6 cells: application for intracerebral grafting

1 reference

https://api.crossref.org/works/10.1046%2FJ.1471-4159.2002.00921.X

21 January 2018

Grafting fibroblasts genetically modified to produce L-dopa in a rat model of Parkinson disease

1 reference

https://api.crossref.org/works/10.1046%2FJ.1471-4159.2002.00921.X

21 January 2018

Identifiers

10.1046/J.1471-4159.2002.00921.X

1 reference

Europe PubMed Central

PubMed publication ID

23 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

23 September 2017

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