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Structural basis of the metal specificity for nickel regulatory protein NikRRelationship between Ni(II) and Zn(II) Coordination and Nucleotide Binding by the Helicobacter pylori [NiFe]-Hydrogenase and Urease Maturation Factor HypBMetal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPasesProtease digestion analysis of Escherichia coli NikR: evidence for conformational stabilization with Ni(II).NikR-operator complex structure and the mechanism of repressor activation by metal ions.HMG-domain proteins specifically inhibit the repair of the major DNA adduct of the anticancer drug cisplatin by human excision nucleaseYeiR: a metal-binding GTPase from Escherichia coli involved in metal homeostasisMicrobial nickel proteins.The McbB component of microcin B17 synthetase is a zinc metalloprotein.Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins.[NiFe]-Hydrogenase Maturation.High-affinity metal binding by the Escherichia coli [NiFe]-hydrogenase accessory protein HypB is selectively modulated by SlyD.Microbial nickel: cellular uptake and delivery to enzyme centers.Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase.Ordered binding of retinoic acid and retinoid-X receptors to asymmetric response elements involves determinants adjacent to the DNA-binding domain.Nickel-responsive regulation of two novel Helicobacter pylori NikR-targeted genes.Escherichia coli HypA is a zinc metalloprotein with a weak affinity for nickel.A high-performance liquid chromatography method for determining transition metal content in proteins.Interactions of the Escherichia coli hydrogenase biosynthetic proteins: HybG complex formation.Fluorescence analysis of sulfonamide binding to carbonic anhydrase.The peptidyl-prolyl isomerase activity of SlyD is not required for maturation of Escherichia coli hydrogenase.Potassium is critical for the Ni(II)-responsive DNA-binding activity of Escherichia coli NikR.The Ni(II)-binding properties of the metallochaperone SlyD.Nonspecific interactions between Escherichia coli NikR and DNA are critical for nickel-activated DNA binding.The antibiotic microcin B17 is a DNA gyrase poison: characterisation of the mode of inhibition.Selectivity of metal binding and metal-induced stability of Escherichia coli NikR.pH-responsive DNA-binding activity of Helicobacter pylori NikR.A high-affinity metal-binding peptide from Escherichia coli HypB.Correction to Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-AssociatedCOG0523 Family of GTPases.Metal binding activity of the Escherichia coli hydrogenase maturation factor HypB.Human testis-determining factor SRY binds to the major DNA adduct of cisplatin and a putative target sequence with comparable affinities.The "metallo-specific" response of proteins: a perspective based on the Escherichia coli transcriptional regulator NikR.The role of complex formation between the Escherichia coli hydrogenase accessory factors HypB and SlyD.Relationship between the GTPase, metal-binding, and dimerization activities of E. coli HypB.Nickel in biology.The metal selectivity of a short peptide maquette imitating the high-affinity metal-binding site of E. coli HypB.The Escherichia coli metal-binding chaperone SlyD interacts with the large subunit of [NiFe]-hydrogenase 3.The response of Escherichia coli NikR to nickel: a second nickel-binding site.Metal-selective DNA-binding response of Escherichia coli NikR.Structural and Biological Analysis of the Metal Sites ofEscherichia coliHydrogenase Accessory Protein HypB†
P50
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P50
description
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հետազոտող
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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Deborah B. Zamble
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P106
P1153
6602972251
P21
P31
P496
0000-0002-8976-3375