Proteomics

Dataset Information

0

AN01_Rattus


ABSTRACT: Identification by nano-LC-MS/MS of NT5DC2 as a protein binding to tyrosine hydroxylase: Down-regulation of NT5DC2 by siRNA increases catecholamine synthesis in PC12D cells

ORGANISM(S): Rattus Norvegicus

SUBMITTER: Akira Nakashima 

PROVIDER: PXD014417 | JPOST Repository | Sat Jul 20 00:00:00 BST 2019

REPOSITORIES: jPOST

Dataset's files

Source:
Action DRS
20180314_10_anti_TH_1_60m5uL.raw Raw
20180314_13_anti_TH_2_60m5uL.raw Raw
20180314_16_anti_TH_3_60m5uL.raw Raw
20180314_21_anti_GAPDH_1_60m5uL.raw Raw
20180314_24_anti_GAPDH_2_60m5uL.raw Raw
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Publications

Identification by nano-LC-MS/MS of NT5DC2 as a protein binding to tyrosine hydroxylase: Down-regulation of NT5DC2 by siRNA increases catecholamine synthesis in PC12D cells.

Nakashima Akira A   Yamaguchi Hisateru H   Kodani Yu Y   Kaneko Yoko S YS   Kawata Miho M   Nagasaki Hiroshi H   Nagatsu Toshiharu T   Ota Akira A  

Biochemical and biophysical research communications 20190703 4


Tyrosine hydroxylase (TH), which catalyzes the conversion of l-tyrosine to l-DOPA, is the rate-limiting enzyme in the biosynthesis of catecholamines. It is well known that both α-synuclein and 14-3-3 protein family members bind to the TH molecule and regulate phosphorylation of its N-terminus by kinases to control the catalytic activity. In this present study we investigated whether other proteins aside from these 2 proteins might also bind to TH molecules. Nano-LC-MS/MS analysis revealed that 5  ...[more]

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