Three-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranes
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 MembranesSustained N-methyl-d-aspartate receptor hypofunction remodels the dopamine system and impairs phasic signaling.Tyrosine Hydroxylase Binding to Phospholipid Membranes Prompts Its Amyloid Aggregation and Compromises Bilayer Integrity.HAMLET interacts with lipid membranes and perturbs their structure and integrity.Locomotor hyperactivity in 14-3-3ζ KO mice is associated with dopamine transporter dysfunction.Identification of a novel lytic peptide for the treatment of solid tumours.Phosphorylation dependence and stoichiometry of the complex formed by tyrosine hydroxylase and 14-3-3γ.The peripheral binding of 14-3-3γ to membranes involves isoform-specific histidine residues.Implications for proteasome nuclear localization revealed by the structure of the nuclear proteasome tether protein Cut8.Dysregulated 14-3-3 Family in Peripheral Blood Leukocytes of Patients with Schizophrenia.Identification of chaperones in a MPP+-induced and ATRA/TPA-differentiated SH-SY5Y cell PD model.Complex molecular regulation of tyrosine hydroxylase.Divergence in enzyme regulation between Caenorhabditis elegans and human tyrosine hydroxylase, the key enzyme in the synthesis of dopamine.Regulation of tyrosine hydroxylase is preserved across different homo- and heterodimeric 14-3-3 proteins.Binding of phosphatidic acid to 14-3-3 proteins hampers their ability to activate the plant plasma membrane H+-ATPase.Phosphorylation at serine 31 targets tyrosine hydroxylase to vesicles for transport along microtubules.The binding of 14-3-3γ to membranes studied by intrinsic fluorescence spectroscopy.Nicotinic stimulation of catecholamine synthesis and tyrosine hydroxylase phosphorylation in cervine adrenal medullary chromaffin cells.
P2860
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P2860
Three-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranes
description
2009 nî lūn-bûn
@nan
2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Three-way interaction between ...... d negatively charged membranes
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Three-way interaction between ...... d negatively charged membranes
@en
Three-way interaction between ...... d negatively charged membranes
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type
label
Three-way interaction between ...... d negatively charged membranes
@ast
Three-way interaction between ...... d negatively charged membranes
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Three-way interaction between ...... d negatively charged membranes
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Three-way interaction between ...... d negatively charged membranes
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Three-way interaction between ...... d negatively charged membranes
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Three-way interaction between ...... d negatively charged membranes
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P2093
P2860
P50
P3181
P356
P1476
Three-way interaction between ...... d negatively charged membranes
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P2093
Anne Baumann
Bjørg Almås
Rune Kleppe
P2860
P304
P3181
P356
10.1074/JBC.M109.027706
P407
P577
2009-11-20T00:00:00Z