The 14-3-3 protein affects the conformation of the regulatory domain of human tyrosine hydroxylase
about
Tyrosine hydroxylase and regulation of dopamine synthesisThe N-Terminal Sequence of Tyrosine Hydroxylase Is a Conformationally Versatile Motif That Binds 14-3-3 Proteins and MembranesThe 14-3-3 protein Bmh1 functions in the spindle position checkpoint by breaking Bfa1 asymmetry at yeast centrosomesThree-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranesRole of individual phosphorylation sites for the 14-3-3-protein-dependent activation of yeast neutral trehalase Nth1.14-3-3 protein masks the DNA binding interface of forkhead transcription factor FOXO4.Endogenous 3,4-dihydroxyphenylalanine and dopaquinone modifications on protein tyrosine: links to mitochondrially derived oxidative stress via hydroxyl radicalPhosphorylation dependence and stoichiometry of the complex formed by tyrosine hydroxylase and 14-3-3γ.Molecular mechanism of 14-3-3 protein-mediated inhibition of plant nitrate reductaseProtein-protein interactions as drug targets.The 31-kDa antigen of Angiostrongylus cantonensis comprises distinct antigenic glycoproteinsStructural modulation of phosducin by phosphorylation and 14-3-3 protein binding.Expression of recombinant antigenic proteins from Angiostrongylus cantonensis: a brief reportComplexity of dopamine metabolism.14-3-3zeta contributes to tyrosine hydroxylase activity in MN9D cells: localization of dopamine regulatory proteins to mitochondria.Complex molecular regulation of tyrosine hydroxylase.A new role for α-synuclein in Parkinson's disease: Alteration of ER-mitochondrial communication.Bioinformatic and experimental survey of 14-3-3-binding sites.A novel Pyrin-Associated Autoinflammation with Neutrophilic Dermatosis mutation further defines 14-3-3 binding of pyrin and distinction to Familial Mediterranean Fever.Structural Characterization of Phosducin and Its Complex with the 14-3-3 Protein.Fluorescence spectroscopy as a probe of the effect of phosphorylation at serine 40 of tyrosine hydroxylase on the conformation of its regulatory domain.Dissection of binding between a phosphorylated tyrosine hydroxylase peptide and 14-3-3zeta: A complex story elucidated by NMR.Identification by hydrogen/deuterium exchange of structural changes in tyrosine hydroxylase associated with regulation.Modulation of PC12 cell viability by forskolin-induced cyclic AMP levels through ERK and JNK pathways: an implication for L-DOPA-induced cytotoxicity in nigrostriatal dopamine neurons.Crystal structures of a yeast 14-3-3 protein from Lachancea thermotolerans in the unliganded form and bound to a human lipid kinase PI4KB-derived peptide reveal high evolutionary conservation.
P2860
Q21710723-DAE16F1F-22A9-40D2-A0AB-C11A0C1C6F23Q27680008-8370FBA6-F2BE-4A0A-9221-8C890FA13C62Q27931517-105B8751-E385-48C2-A87A-87B027B02446Q28260366-8F34A531-1259-48AD-9816-E3185EC42A8EQ31048647-B2504C30-0778-4B86-B692-D39BA7421668Q33439373-FC82E7E5-13A0-4322-8333-365D90158719Q33883022-BA6C1640-7CE5-4E74-AC9E-A4EF0F0C75EBQ34018057-DF72DE85-335E-4B63-B152-3E5347599381Q35762982-78B6E7EB-CE1A-49B3-A9D4-81F2A8F92C5CQ35824701-C132D615-0EA3-4DCC-A781-916F8C178135Q36378907-ABF46B1D-577E-4DF1-B266-99B74E9580EEQ36379125-3FA3327C-7C39-40B2-BFF4-98787B3F3312Q36946599-DEC2A853-29D1-4332-9BC0-77D96D999412Q36958208-311F21B3-A224-4265-BD64-D9ABC285E163Q37194162-DA3D651F-619E-46F1-AFAA-254D59D5568CQ38215359-3F6C803C-D10B-4EAF-ADDB-188EEB650938Q38465664-24AA26B6-D3AF-484C-A647-40E4D16A8E14Q39918674-C31612AA-38C8-4AF1-B95A-14E1E10871CDQ40042168-8449A766-B4B4-4E18-8211-3F40571C5D0BQ40942320-0F7F0085-EF10-44CC-AF81-096D67D1092BQ41775031-1DA24672-6AEB-495B-88E9-6B6CE11D4064Q42091637-522FF391-044C-4752-9B8E-06A0B9340806Q43066150-5DEBB48C-4A56-4B24-81E3-490216146C7DQ48545452-25856865-007E-49BB-B3F7-81F3466A5B0EQ51336908-7A52F85C-669C-4A28-AEC3-61A4C3442A99
P2860
The 14-3-3 protein affects the conformation of the regulatory domain of human tyrosine hydroxylase
description
2008 nî lūn-bûn
@nan
2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
name
The 14-3-3 protein affects the ...... of human tyrosine hydroxylase
@ast
The 14-3-3 protein affects the ...... of human tyrosine hydroxylase
@en
The 14-3-3 protein affects the ...... of human tyrosine hydroxylase
@nl
type
label
The 14-3-3 protein affects the ...... of human tyrosine hydroxylase
@ast
The 14-3-3 protein affects the ...... of human tyrosine hydroxylase
@en
The 14-3-3 protein affects the ...... of human tyrosine hydroxylase
@nl
prefLabel
The 14-3-3 protein affects the ...... of human tyrosine hydroxylase
@ast
The 14-3-3 protein affects the ...... of human tyrosine hydroxylase
@en
The 14-3-3 protein affects the ...... of human tyrosine hydroxylase
@nl
P2093
P50
P356
P1433
P1476
The 14-3-3 protein affects the ...... of human tyrosine hydroxylase
@en
P2093
Eliska Nedbalkova
Evzen Boura
Jan Silhan
Jan Teisinger
Jaroslav Vecer
P304
P356
10.1021/BI7019468
P407
P577
2008-01-09T00:00:00Z