Kinetic analysis of the interaction of the copper chaperone Atox1 with the metal binding sites of the Menkes protein
about
Binding of copper(I) by the Wilson disease protein and its copper chaperoneCopper-dependent interaction of dynactin subunit p62 with the N terminus of ATP7B but not ATP7AA single PDZ domain protein interacts with the Menkes copper ATPase, ATP7A. A new protein implicated in copper homeostasisCharacterization of COMMD protein-protein interactions in NF-kappaB signallingMolecular pathogenesis of Wilson and Menkes disease: correlation of mutations with molecular defects and disease phenotypesSingle-molecule dynamics and mechanisms of metalloregulators and metallochaperonesHuman Sco1 functional studies and pathological implications of the P174L mutantMetal Binding Domains 3 and 4 of the Wilson Disease Protein: Solution Structure and Interaction with the Copper(I) Chaperone HAH1 † ‡The Architecture of CopA from Archeaoglobus fulgidus Studied by Cryo-Electron Microscopy and Computational DockingThe copper toxicosis gene product Murr1 directly interacts with the Wilson disease proteinStructural biology of copper traffickingThe interactome of the copper transporter ATP7A belongs to a network of neurodevelopmental and neurodegeneration factors.In vitro thermodynamic dissection of human copper transfer from chaperone to target protein.Tackling metal regulation and transport at the single-molecule level.Nanovesicle trapping for studying weak protein interactions by single-molecule FRETThe Methylococcus capsulatus (Bath) secreted protein, MopE*, binds both reduced and oxidized copperRelating dynamic protein interactions of metallochaperones with metal transfer at the single-molecule levelEvidence that translation reinitiation leads to a partially functional Menkes protein containing two copper-binding sites.The Menkes and Wilson disease genes counteract in copper toxicosis in Labrador retrievers: a new canine model for copper-metabolism disorders.Role of the P-Type ATPases, ATP7A and ATP7B in brain copper homeostasis.Plasmonics for the study of metal ion-protein interactions.An NMR study of the interaction of the N-terminal cytoplasmic tail of the Wilson disease protein with copper(I)-HAH1.Dynamic multibody protein interactions suggest versatile pathways for copper trafficking.In silico modeling of the Menkes copper-translocating P-type ATPase 3rd metal binding domain predicts that phosphorylation regulates copper-binding.Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease protein.
P2860
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P2860
Kinetic analysis of the interaction of the copper chaperone Atox1 with the metal binding sites of the Menkes protein
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Kinetic analysis of the intera ...... ng sites of the Menkes protein
@ast
Kinetic analysis of the intera ...... ng sites of the Menkes protein
@en
Kinetic analysis of the intera ...... ng sites of the Menkes protein
@nl
type
label
Kinetic analysis of the intera ...... ng sites of the Menkes protein
@ast
Kinetic analysis of the intera ...... ng sites of the Menkes protein
@en
Kinetic analysis of the intera ...... ng sites of the Menkes protein
@nl
prefLabel
Kinetic analysis of the intera ...... ng sites of the Menkes protein
@ast
Kinetic analysis of the intera ...... ng sites of the Menkes protein
@en
Kinetic analysis of the intera ...... ng sites of the Menkes protein
@nl
P2093
P2860
P356
P1476
Kinetic analysis of the intera ...... ng sites of the Menkes protein
@en
P2093
Andrea Schlicksupp
Daniel Strausak
Julian F B Mercer
Michelle K Howie
Rudiger Pipkorn
Stephen D Firth
P2860
P304
P356
10.1074/JBC.M212437200
P407
P577
2003-06-06T00:00:00Z