Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake.
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Biochemical basis of regulation of human copper-transporting ATPasesCellular multitasking: the dual role of human Cu-ATPases in cofactor delivery and intracellular copper balanceSingle-molecule dynamics and mechanisms of metalloregulators and metallochaperonesCharacterization and Structure of a Zn2+ and [2Fe-2S]-containing Copper Chaperone from Archaeoglobus fulgidusUnusual Cu(I)/Ag(I) coordination ofEscherichia coliCusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopyStructure of a Copper Pump Suggests a Regulatory Role for Its Metal-Binding DomainMetal 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 DockingStructural biology of copper traffickingElucidation of the ATP7B N-domain Mg2+-ATP coordination site and its allosteric regulationIn silico investigation of the ATP7B gene: insights from functional prediction of non-synonymous substitution to protein structure.Nanobodies as Probes for Protein Dynamics in Vitro and in Cells.The role of metal binding and phosphorylation domains in the regulation of cisplatin-induced trafficking of ATP7B.Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B.Role of glutaredoxin1 and glutathione in regulating the activity of the copper-transporting P-type ATPases, ATP7A and ATP7B.In vitro thermodynamic dissection of human copper transfer from chaperone to target protein.Tackling metal regulation and transport at the single-molecule level.Interactions between metal-binding domains modulate intracellular targeting of Cu(I)-ATPase ATP7B, as revealed by nanobody binding.Relating dynamic protein interactions of metallochaperones with metal transfer at the single-molecule levelUnification of the copper(I) binding affinities of the metallo-chaperones Atx1, Atox1, and related proteins: detection probes and affinity standards.Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites.Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.Coordination chemistry of bacterial metal transport and sensing.Identification of New Potential Interaction Partners for Human Cytoplasmic Copper Chaperone Atox1: Roles in Gene Regulation?Evolution of copper transporting ATPases in eukaryotic organisms.A new metal binding domain involved in cadmium, cobalt and zinc transportHuman superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)Toward a molecular understanding of metal transport by P(1B)-type ATPases.Multiple metal binding domains enhance the Zn(II) selectivity of the divalent metal ion transporter AztAThe CXXC motifs in the metal binding domains are required for ATP7B to mediate resistance to cisplatin.Conserved residues modulate copper release in human copper chaperone Atox1.Expressional control of a cadmium-transporting P1B-type ATPase by a metal sensing degradation signal.Apical targeting and Golgi retention signals reside within a 9-amino acid sequence in the copper-ATPase, ATP7B.The use of blue native PAGE in the evaluation of membrane protein aggregation states for crystallization.Role of the P-Type ATPases, ATP7A and ATP7B in brain copper homeostasis.Disease-causing point-mutations in metal-binding domains of Wilson disease protein decrease stability and increase structural dynamics.Distinct phenotype of a Wilson disease mutation reveals a novel trafficking determinant in the copper transporter ATP7B.Human copper transporters: mechanism, role in human diseases and therapeutic potential.Mechanism of tumor resistance to cisplatin mediated by the copper transporter ATP7B.Copper chaperones. The concept of conformational control in the metabolism of copper.
P2860
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P2860
Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake.
description
2006 nî lūn-bûn
@nan
2006 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մարտին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Structure of human Wilson prot ...... aperone HAH1 in copper uptake.
@ast
Structure of human Wilson prot ...... aperone HAH1 in copper uptake.
@en
Structure of human Wilson prot ...... aperone HAH1 in copper uptake.
@nl
type
label
Structure of human Wilson prot ...... aperone HAH1 in copper uptake.
@ast
Structure of human Wilson prot ...... aperone HAH1 in copper uptake.
@en
Structure of human Wilson prot ...... aperone HAH1 in copper uptake.
@nl
prefLabel
Structure of human Wilson prot ...... aperone HAH1 in copper uptake.
@ast
Structure of human Wilson prot ...... aperone HAH1 in copper uptake.
@en
Structure of human Wilson prot ...... aperone HAH1 in copper uptake.
@nl
P2093
P2860
P50
P356
P1476
Structure of human Wilson prot ...... aperone HAH1 in copper uptake.
@en
P2093
David Achila
David L Huffman
Jennifer Bunce
P2860
P304
P356
10.1073/PNAS.0504472103
P407
P577
2006-03-29T00:00:00Z