Evidence for Cu(I)-thiolate ligation and prediction of a putative copper-binding site in the Escherichia coli NADH dehydrogenase-2.
about
The multiple antibiotic resistance regulator MarR is a copper sensor in Escherichia coliA fresh view of the cell biology of copper in enterobacteria.Prediction of the functional class of metal-binding proteins from sequence derived physicochemical properties by support vector machine approachLinear array of conserved sequence motifs to discriminate protein subfamilies: study on pyridine nucleotide-disulfide reductases.Comparative genomic analyses of copper transporters and cuproproteomes reveal evolutionary dynamics of copper utilization and its link to oxygen.Escherichia coli mechanisms of copper homeostasis in a changing environment.Semiquinone and cluster N6 signals in His-tagged proton-translocating NADH:ubiquinone oxidoreductase (complex I) from Escherichia coliMechanisms of copper homeostasis in bacteria.Type II NADH:quinone oxidoreductase family: phylogenetic distribution, structural diversity and evolutionary divergences.Apoptosis-like death, an extreme SOS response in Escherichia coliThe Tat Substrate CueO Is Transported in an Incomplete Folding StateLability and liability of endogenous copper pools.Survival of Escherichia coli cells on solid copper surfaces is increased by glutathione.Functional properties of the alternative NADH:ubiquinone oxidoreductase from E. coli through comparative 3-D modelling.Electron transfer ability from NADH to menaquinone and from NADPH to oxygen of type II NADH dehydrogenase of Corynebacterium glutamicum.Tellurite reduction by Escherichia coli NDH-II dehydrogenase results in superoxide production in membranes of toxicant-exposed cells.Modification of substrate specificity in single point mutants of Agrobacterium tumefaciens type II NADH dehydrogenase.The Escherichia coli copper-responsive copA promoter is activated by gold.Cupric Reductase Activity in Copper-Resistant Amycolatopsis tucumanensis
P2860
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P2860
Evidence for Cu(I)-thiolate ligation and prediction of a putative copper-binding site in the Escherichia coli NADH dehydrogenase-2.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Evidence for Cu
@nl
Evidence for Cu(I)-thiolate li ...... hia coli NADH dehydrogenase-2.
@en
type
label
Evidence for Cu
@nl
Evidence for Cu(I)-thiolate li ...... hia coli NADH dehydrogenase-2.
@en
prefLabel
Evidence for Cu
@nl
Evidence for Cu(I)-thiolate li ...... hia coli NADH dehydrogenase-2.
@en
P2093
P50
P1476
Evidence for Cu(I)-thiolate li ...... hia coli NADH dehydrogenase-2.
@en
P2093
Eddy M Massa
Luisa Rodríguez-Montelongo
Ricardo N Farías
P356
10.1016/S0003-9861(02)00277-1
P407
P577
2002-09-01T00:00:00Z