Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1
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The Role of Copper Chaperone Atox1 in Coupling Redox Homeostasis to Intracellular Copper DistributionMetal Binding Domains 3 and 4 of the Wilson Disease Protein: Solution Structure and Interaction with the Copper(I) Chaperone HAH1 † ‡Copper(I)-mediated protein-protein interactions result from suboptimal interaction surfacesStructural biology of copper traffickingDeterminants for simultaneous binding of copper and platinum to human chaperone Atox1: hitchhiking not hijackingPhysicochemical code for quinary protein interactions in Escherichia coli.The structure and function of frataxin.Copper binding to the Alzheimer's disease amyloid precursor proteinTackling metal regulation and transport at the single-molecule level.Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake.Mechanisms for copper acquisition, distribution and regulation.Cisplatin binds human copper chaperone Atox1 and promotes unfolding in vitroFunctional partnership of the copper export machinery and glutathione balance in human cells.Triplin, a small molecule, reveals copper ion transport in ethylene signaling from ATX1 to RAN1.Inhibition of human copper trafficking by a small molecule significantly attenuates cancer cell proliferationStructural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadA.Conserved residues modulate copper release in human copper chaperone Atox1.An expanding range of functions for the copper chaperone/antioxidant protein Atox1.Probing the coordination environment of the human copper chaperone HAH1: characterization of Hg(II)-bridged homodimeric species in solution.Atox1 contains positive residues that mediate membrane association and aid subsequent copper loadingInteraction of classical platinum agents with the monomeric and dimeric Atox1 proteins: a molecular dynamics simulation study.The MXCXXC class of metallochaperone proteins: model studies.Copper chaperones. The concept of conformational control in the metabolism of copper.The structural flexibility of the human copper chaperone Atox1: Insights from combined pulsed EPR studies and computations.The C-Terminus of Human Copper Importer Ctr1 Acts as a Binding Site and Transfers Copper to Atox1.The different intermolecular interactions of the soluble copper-binding domains of the menkes protein, ATP7A.An NMR study of the interaction of the N-terminal cytoplasmic tail of the Wilson disease protein with copper(I)-HAH1.Insights into Cu(I) exchange in HAH1 using quantum mechanical and molecular simulations.Dynamic multibody protein interactions suggest versatile pathways for copper trafficking.Copper binding modulates the platination of human copper chaperone Atox1 by antitumor trans-platinum complexes.Conserved residue modulates copper-binding properties through structural dynamics in human copper chaperone Atox1.The structural plasticity of the human copper chaperone for SOD1: insights from combined size-exclusion chromatographic and solution X-ray scattering studies.In silico modeling of the Menkes copper-translocating P-type ATPase 3rd metal binding domain predicts that phosphorylation regulates copper-binding.Probing transient copper chaperone-Wilson disease protein interactions at the single-molecule level with nanovesicle trapping.Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants.Structural biology of cisplatin complexes with cellular targets: the adduct with human copper chaperone atox1 in aqueous solution.Interaction of cisplatin and analogue Pt(en)Cl2 with the copper metallo-chaperone Atox1.A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.Molecular dynamics study of the metallochaperone Hah1 in its apo and Cu(I)-loaded states: role of the conserved residue M10.Computational modelling of the redistribution of copper isotopes by proteins in the liver.
P2860
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P2860
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1
description
2004 nî lūn-bûn
@nan
2004 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1
@ast
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1
@en
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1
@nl
type
label
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1
@ast
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1
@en
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1
@nl
prefLabel
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1
@ast
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1
@en
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1
@nl
P2093
P50
P3181
P356
P1433
P1476
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1
@en
P2093
Antonio Rosato
Efthalia Katsari
Ioanna Anastassopoulou
P304
P3181
P356
10.1021/BI0487591
P407
P577
2004-10-19T00:00:00Z