High-affinity Ni2+ binding selectively promotes binding of Helicobacter pylori NikR to its target urease promoter.
about
Interplay of metal ions and ureaseEvolution of Macromolecular Docking Techniques: The Case Study of Nickel and Iron Metabolism in Pathogenic BacteriaStructural and mechanistic insights into Helicobacter pylori NikR activationNi(II) coordination to mixed sites modulates DNA binding of HpNikR via a long-range effect.Structural basis of an engineered dual-specific antibody: conformational diversity leads to a hypervariable loop metal-binding siteDissecting the role of DNA sequence in Helicobacter pylori NikR/DNA recognition.Built shallow to maintain homeostasis and persistent infection: insight into the transcriptional regulatory network of the gastric human pathogen Helicobacter pylori.Mua (HP0868) is a nickel-binding protein that modulates urease activity in Helicobacter pylori.Helicobacter pylori NikR protein exhibits distinct conformations when bound to different promoters.Combination of isothermal titration calorimetry and time-resolved luminescence for high affinity antibody-ligand interaction thermodynamics and kineticsIdentification of the human zinc transcriptional regulatory element (ZTRE): a palindromic protein-binding DNA sequence responsible for zinc-induced transcriptional repression.Comprehensive mapping of the Helicobacter pylori NikR regulon provides new insights in bacterial nickel responsesRegulatory circuits in Helicobacter pylori : network motifs and regulators involved in metal-dependent responses.New roles for bacterial siderophores in metal transport and tolerance.Nickel-responsive transcriptional regulators.Metallochaperones and metalloregulation in bacteria.Surface plasmon resonance and isothermal titration calorimetry to monitor the Ni(II)-dependent binding of Helicobacter pylori NikR to DNA.Crosstalk between the HpArsRS two-component system and HpNikR is necessary for maximal activation of urease transcription.Metal-responsive promoter DNA compaction by the ferric uptake regulator.On the interaction of Helicobacter pylori NikR, a Ni(II)-responsive transcription factor, with the urease operator: in solution and in silico studies.AnhE, a metallochaperone involved in the maturation of a cobalt-dependent nitrile hydratase.An ABC transporter and a TonB ortholog contribute to Helicobacter mustelae nickel and cobalt acquisition.In vivo recognition of the fecA3 target promoter by Helicobacter pylori NikR.Hot biological catalysis: isothermal titration calorimetry to characterize enzymatic reactions.Growth phase and metal-dependent transcriptional regulation of the fecA genes in Helicobacter pylori.A novel nickel responsive MerR-like regulator, NimR, from Haemophilus influenzae
P2860
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P2860
High-affinity Ni2+ binding selectively promotes binding of Helicobacter pylori NikR to its target urease promoter.
description
2008 nî lūn-bûn
@nan
2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
High-affinity Ni2+ binding sel ...... to its target urease promoter.
@ast
High-affinity Ni2+ binding sel ...... to its target urease promoter.
@en
type
label
High-affinity Ni2+ binding sel ...... to its target urease promoter.
@ast
High-affinity Ni2+ binding sel ...... to its target urease promoter.
@en
prefLabel
High-affinity Ni2+ binding sel ...... to its target urease promoter.
@ast
High-affinity Ni2+ binding sel ...... to its target urease promoter.
@en
P50
P3181
P1476
High-affinity Ni2+ binding sel ...... to its target urease promoter.
@en
P2093
Barbara Zambelli
Simona Romagnoli
P304
P3181
P356
10.1016/J.JMB.2008.08.066
P407
P577
2008-09-04T00:00:00Z