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Characterization and Structure of a Zn2+ and [2Fe-2S]-containing Copper Chaperone from Archaeoglobus fulgidusMechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: the interaction of Escherichia coli CopA and CusFEvolution and diversity of periplasmic proteins involved in copper homeostasis in gamma proteobacteria.Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites.A novel zinc binding system, ZevAB, is critical for survival of nontypeable Haemophilus influenzae in a murine lung infection model.A novel antimycobacterial compound acts as an intracellular iron chelator.Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.Metal transport across biomembranes: emerging models for a distinct chemistry.Role in metal homeostasis of CtpD, a Co²⁺ transporting P(1B4)-ATPase of Mycobacterium smegmatis.The role of Na,K-ATPase alpha subunit serine 775 and glutamate 779 in determining the extracellular K+ and membrane potential-dependent properties of the Na,K-pumpThe mechanism of Cu+ transport ATPases: interaction with CU+ chaperones and the role of transient metal-binding sites.The structure and function of heavy metal transport P1B-ATPases.A novel P(1B)-type Mn2+-transporting ATPase is required for secreted protein metallation in mycobacteria.Fine-tuning of Substrate Affinity Leads to Alternative Roles of Mycobacterium tuberculosis Fe2+-ATPases.Mechanisms of copper homeostasis in bacteria.Sinorhizobium meliloti Nia is a P(1B-5)-ATPase expressed in the nodule during plant symbiosis and is involved in Ni and Fe transport.Differential roles for the Co(2+) /Ni(2+) transporting ATPases, CtpD and CtpJ, in Mycobacterium tuberculosis virulence.Bacterial Cu(+)-ATPases: models for molecular structure-function studies.The Listeria monocytogenes Fur-regulated virulence protein FrvA is an Fe(II) efflux P1B4 -type ATPase.Cation and cardiac glycoside binding sites of the Na,K-ATPase.N-acetylimidazole inactivates renal Na,K-ATPase by disrupting ATP binding to the catalytic site.PfeT, a P1B4 -type ATPase, effluxes ferrous iron and protects Bacillus subtilis against iron intoxicationCopper homeostasis networks in the bacterium Pseudomonas aeruginosa.Activation of Archaeoglobus fulgidus Cu(+)-ATPase CopA by cysteine.Thermal stability of CopA, a polytopic membrane protein from the hyperthermophile Archaeoglobus fulgidus.Reversible unfolding of a thermophilic membrane protein in phospholipid/detergent mixed micelles.Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus fulgidus.Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain.Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu(+)-ATPase CopA.Identification of ion-selectivity determinants in heavy-metal transport P1B-type ATPases.Biochemical identification of transmembrane segments of the Ca(2+)-ATPase of sarcoplasmic reticulum.Nucleic acid content and residue determination in tissues of chicks born from 2,4-dichlorophenoxyacetic butyl ester treated eggs.Periplasmic response upon disruption of transmembrane Cu transport in Pseudomonas aeruginosa.Ligand binding sites of Na,K-ATPase.Distinct functional roles of homologous Cu+ efflux ATPases in Pseudomonas aeruginosa.An important role for periplasmic storage in Pseudomonas aeruginosa copper homeostasis revealed by a combined experimental and computational modeling studyConformational alterations resulting from mutations in cytoplasmic domains of the alpha subunit of the Na,K-ATPaseBiochemical alterations in skeletal muscle induced by 2,4-dichlorophenoxyacetic butyl ester during chick embryonic developmentOuabain interactions with the H5-H6 hairpin of the Na,K-ATPase reveal a possible inhibition mechanism via the cation binding domainReactivity of cysteines in the transmembrane region of the Na, K-ATPase alpha subunit probed with Hg(2+)
P50
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P50
description
Forscher
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chercheur
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J M Argüello
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J M Argüello
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J M Argüello
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J M Argüello
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J M Argüello
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J M Argüello
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J M Argüello
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J M Argüello
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J M Argüello
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J M Argüello
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J M Argüello
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P31
P496
0000-0003-3940-6297