The regulation of catalytic activity of the menkes copper-translocating P-type ATPase. Role of high affinity copper-binding sites.
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Copper binding to the N-terminal metal-binding sites or the CPC motif is not essential for copper-induced trafficking of the human Wilson protein (ATP7B)A single PDZ domain protein interacts with the Menkes copper ATPase, ATP7A. A new protein implicated in copper homeostasisSolution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutationsArabidopsis HMA2, a divalent heavy metal-transporting P(IB)-type ATPase, is involved in cytoplasmic Zn2+ homeostasisBiochemical basis of regulation of human copper-transporting ATPasesMolecular pathogenesis of Wilson and Menkes disease: correlation of mutations with molecular defects and disease phenotypesBiochemical characterization of P-type copper ATPasesThe Binding Mode of ATP Revealed by the Solution Structure of the N-domain of Human ATP7ACod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis.A mutational study in the transmembrane domain of Ccc2p, the yeast Cu(I)-ATPase, shows different roles for each Cys-Pro-Cys cysteine.Biochemical and genetic analyses of yeast and human high affinity copper transporters suggest a conserved mechanism for copper uptakeIdentification of methionine-rich clusters that regulate copper-stimulated endocytosis of the human Ctr1 copper transporterEssential roles in development and pigmentation for the Drosophila copper transporter DmATP7.Diversity of the metal-transporting P1B-type ATPasesA conditional mutation affecting localization of the Menkes disease copper ATPase. Suppression by copper supplementation.A combined zinc/cadmium sensor and zinc/cadmium export regulator in a heavy metal pump.The T1048I mutation in ATP7A gene causes an unusual Menkes disease presentation.Structure, function, and regulation of renal organic anion transporters.The lumenal loop Met672-Pro707 of copper-transporting ATPase ATP7A binds metals and facilitates copper release from the intramembrane sitesCalcium and copper transport ATPases: analogies and diversities in transduction and signaling mechanisms.Biochemical characterization of AtHMA6/PAA1, a chloroplast envelope Cu(I)-ATPase.Functional and Biochemical Characterization of Cucumber Genes Encoding Two Copper ATPases CsHMA5.1 and CsHMA5.2.HMA6 and HMA8 are two chloroplast Cu+-ATPases with different enzymatic properties.Characterization of a cobalt-specific P(1B)-ATPaseToward a molecular understanding of metal transport by P(1B)-type ATPases.Role of the P-Type ATPases, ATP7A and ATP7B in brain copper homeostasis.Recent developments in plant zinc homeostasis and the path toward improved biofortification and phytoremediation programs.The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein.Comparative study of the active cadmium efflux systems operating at the plasma membrane and tonoplast of cucumber root cells.Mechanisms of charge transfer in human copper ATPases ATP7A and ATP7B.Identification of Two Conserved Residues Involved in Copper Release from Chloroplast PIB-1-ATPases.Functional properties of the copper-transporting ATPase ATP7B (the Wilson's disease protein) expressed in insect cells.Purification and membrane reconstitution of catalytically active Menkes copper-transporting P-type ATPase (MNK; ATP7A)An NMR study of the interaction of the N-terminal cytoplasmic tail of the Wilson disease protein with copper(I)-HAH1.A possible regulatory role for the metal-binding domain of CadA, the Listeria monocytogenes Cd2+-ATPase.Cd2+ and the N-terminal metal-binding domain protect the putative membranous CPC motif of the Cd2+-ATPase of Listeria monocytogenes.Characterization of ATP7A missense mutants suggests a correlation between intracellular trafficking and severity of Menkes diseaseMitochondrial Ferredoxin Determines Vulnerability of Cells to Copper Excess.In silico modeling of the Menkes copper-translocating P-type ATPase 3rd metal binding domain predicts that phosphorylation regulates copper-binding.Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain.
P2860
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P2860
The regulation of catalytic activity of the menkes copper-translocating P-type ATPase. Role of high affinity copper-binding sites.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
The regulation of catalytic ac ...... affinity copper-binding sites.
@en
The regulation of catalytic ac ...... affinity copper-binding sites.
@nl
type
label
The regulation of catalytic ac ...... affinity copper-binding sites.
@en
The regulation of catalytic ac ...... affinity copper-binding sites.
@nl
prefLabel
The regulation of catalytic ac ...... affinity copper-binding sites.
@en
The regulation of catalytic ac ...... affinity copper-binding sites.
@nl
P2093
P2860
P356
P1476
The regulation of catalytic ac ...... affinity copper-binding sites.
@en
P2093
Camakaris J
Strausak D
Voskoboinik I
P2860
P304
28620-28627
P356
10.1074/JBC.M103532200
P407
P577
2001-05-23T00:00:00Z