X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines
about
Binding of copper(I) by the Wilson disease protein and its copper chaperoneBiochemical basis of regulation of human copper-transporting ATPasesCellular multitasking: the dual role of human Cu-ATPases in cofactor delivery and intracellular copper balanceUnusual Cu(I)/Ag(I) coordination ofEscherichia coliCusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopyA structural-dynamical characterization of human Cox17Crystal Structures of Cisplatin Bound to a Human Copper ChaperoneStructural biology of copper traffickingYeast cox17 solution structure and Copper(I) bindingAnatomy of a red copper center: spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-to-Ala variants.Unification of the copper(I) binding affinities of the metallo-chaperones Atx1, Atox1, and related proteins: detection probes and affinity standards.The essential role of the Cu(II) state of Sco in the maturation of the Cu(A) center of cytochrome oxidase: evidence from H135Met and H135SeM variants of the Bacillus subtilis ScoPosttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.The lumenal loop Met672-Pro707 of copper-transporting ATPase ATP7A binds metals and facilitates copper release from the intramembrane sitesStabilization of Cu(I) for binding and calorimetric measurements in aqueous solution.A place for thioether chemistry in cellular copper ion recognition and trafficking.Multiple metal binding domains enhance the Zn(II) selectivity of the divalent metal ion transporter AztAOpportunities in multidimensional trace metal imaging: taking copper-associated disease research to the next levelLumenal loop M672-P707 of the Menkes protein (ATP7A) transfers copper to peptidylglycine monooxygenase.Stable Cu(II) and Cu(I) mononuclear intermediates in the assembly of the CuA center of Thermus thermophilus cytochrome oxidase.Conserved residues modulate copper release in human copper chaperone Atox1.A systems approach implicates nuclear receptor targeting in the Atp7b(-/-) mouse model of Wilson's disease.Selenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase.Three-dimensional structure of the human copper transporter hCTR1.An expanding range of functions for the copper chaperone/antioxidant protein Atox1.Copper transport in mammalian cells: special care for a metal with special needs.Cellular distribution of copper to superoxide dismutase involves scaffolding by membranes.Interaction of classical platinum agents with the monomeric and dimeric Atox1 proteins: a molecular dynamics simulation study.Copper chaperones. The concept of conformational control in the metabolism of copper.Metal-Organic and Organic TADF-Materials: Status, Challenges and Characterization.Dynamics of the metal binding domains and regulation of the human copper transporters ATP7B and ATP7A.Thiol-based copper handling by the copper chaperone Atox1.The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1.Insights into Cu(I) exchange in HAH1 using quantum mechanical and molecular simulations.Redox sulfur chemistry of the copper chaperone Atox1 is regulated by the enzyme glutaredoxin 1, the reduction potential of the glutathione couple GSSG/2GSH and the availability of Cu(I).Solution structures of a cyanobacterial metallochaperone: insight into an atypical copper-binding motif.The six metal binding domains in human copper transporter, ATP7B: molecular biophysics and disease-causing mutations.Interaction of cisplatin and analogue Pt(en)Cl2 with the copper metallo-chaperone Atox1.Molecular dynamics study of the metallochaperone Hah1 in its apo and Cu(I)-loaded states: role of the conserved residue M10.Substrate-linked conformational change in the periplasmic component of a Cu(I)/Ag(I) efflux system.
P2860
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P2860
X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines
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
X-ray absorption spectroscopy ...... xogenous thiols and phosphines
@ast
X-ray absorption spectroscopy ...... xogenous thiols and phosphines
@en
X-ray absorption spectroscopy ...... xogenous thiols and phosphines
@nl
type
label
X-ray absorption spectroscopy ...... xogenous thiols and phosphines
@ast
X-ray absorption spectroscopy ...... xogenous thiols and phosphines
@en
X-ray absorption spectroscopy ...... xogenous thiols and phosphines
@nl
prefLabel
X-ray absorption spectroscopy ...... xogenous thiols and phosphines
@ast
X-ray absorption spectroscopy ...... xogenous thiols and phosphines
@en
X-ray absorption spectroscopy ...... xogenous thiols and phosphines
@nl
P2093
P2860
P356
P1476
X-ray absorption spectroscopy ...... xogenous thiols and phosphines
@en
P2093
Martina Ralle
Ninian J Blackburn
Svetlana Lutsenko
P2860
P304
P356
10.1074/JBC.M303474200
P407
P577
2003-06-20T00:00:00Z