Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
about
The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium.Protein design: toward functional metalloenzymesCrystal structure of the bacterial cell division regulator MinDConformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocationStructure of a nucleotide-bound Clp1-Pcf11 polyadenylation factorIdentifying important structural characteristics of arsenic resistance proteins by using designed three-stranded coiled coilsModel for eukaryotic tail-anchored protein binding based on the structure of Get3Structural insights into tail-anchored protein binding and membrane insertion by Get3The Crystal Structures of Yeast Get3 Suggest a Mechanism for Tail-Anchored Protein Membrane InsertionThe yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol.The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions.Probing the ATP-binding site of P1 ParA: partition and repression have different requirements for ATP binding and hydrolysis.Antimonite regulation of the ATPase activity of ArsA, the catalytic subunit of the arsenical pumpArsenic binding to proteinsIn search of tail-anchored protein machinery in plants: reevaluating the role of arsenite transporters.A kinetic model for the action of a resistance efflux pump.Characterization of the catalytic cycle of ATP hydrolysis by human P-glycoprotein. The two ATP hydrolysis events in a single catalytic cycle are kinetically similar but affect different functional outcomes.Evolution of bacterial protein-tyrosine kinases and their relaxed specificity toward substratesGene essentiality, conservation index and co-evolution of genes in cyanobacteriaBiochemical characterization of a novel ArsA ATPase complex from Alkaliphilus metalliredigens QYMFThe 1.4 A crystal structure of the ArsD arsenic metallochaperone provides insights into its interaction with the ArsA ATPaseEscherichia coli soft metal ion-translocating ATPases.Arsenic binding and transfer by the ArsD As(III) metallochaperonePathways of arsenic uptake and efflux.Accurate simulation and detection of coevolution signals in multiple sequence alignments.Mutations in the ArsA ATPase that restore interaction with the ArsD metallochaperone.Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transportersGenetic mapping of the interface between the ArsD metallochaperone and the ArsA ATPaseInvolvement of the azorhizobial chromosome partition gene (parA) in the onset of bacteroid differentiation during Sesbania rostrata stem nodule development.Multidimensional mutual information methods for the analysis of covariation in multiple sequence alignments.Structure and function of efflux pumps that confer resistance to drugsThe product of tadZ, a new member of the parA/minD superfamily, localizes to a pole in Aggregatibacter actinomycetemcomitansThe complex process of GETting tail-anchored membrane proteins to the ER.As(III) S-adenosylmethionine methyltransferases and other arsenic binding proteinsRole of conserved aspartates in the ArsA ATPaseTowards understanding the molecular basis of bacterial DNA segregation.Role of signature lysines in the deviant walker a motifs of the ArsA ATPase.The ArsD As(III) metallochaperonePreliminary X-ray crystallographic studies of yeast Get3.Synthesis and structure-activity correlation studies of metal complexes of alpha-N-heterocyclic carboxaldehyde thiosemicarbazones in Shewanella oneidensis.
P2860
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P2860
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
description
2000 nî lūn-bûn
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2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
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2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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name
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
@ast
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
@en
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
@nl
type
label
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
@ast
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
@en
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
@nl
prefLabel
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
@ast
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
@en
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
@nl
P2093
P2860
P356
P1433
P1476
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/19.17.4838
P407
P577
2000-09-01T00:00:00Z