NikR-operator complex structure and the mechanism of repressor activation by metal ions.
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Evolution of Macromolecular Docking Techniques: The Case Study of Nickel and Iron Metabolism in Pathogenic BacteriaTranscription factor-based biosensors enlightened by the analyteStructural basis of the metal specificity for nickel regulatory protein NikRStructural Basis of the Transcriptional Regulation of the Proline Utilization Regulon by Multifunctional PutAStructural basis for the specialization of Nur, a nickel-specific Fur homolog, in metal sensing and DNA recognitionStructure, Function, and Targets of the Transcriptional Regulator SvtR from the Hyperthermophilic Archaeal Virus SIRV1Structural and mechanistic insights into Helicobacter pylori NikR activationStructural Basis of Low-Affinity Nickel Binding to the Nickel-Responsive Transcription Factor NikR from Escherichia coliHolo-Ni(II) Hp NikR Is an Asymmetric Tetramer Containing Two Different Nickel-Binding SitesCrystal structure and centromere binding of the plasmid segregation protein ParB from pCXC100Holo-Ni2+ Helicobacter pylori NikR contains four square-planar nickel-binding sites at physiological pHStructure and Function of AvtR, a Novel Transcriptional Regulator from a Hyperthermophilic Archaeal LipothrixvirusStructural Studies of E73 from a Hyperthermophilic Archaeal Virus Identify the “RH3” Domain, an Elaborated Ribbon–Helix–Helix Motif Involved in DNA RecognitionNi(II) coordination to mixed sites modulates DNA binding of HpNikR via a long-range effect.The Transcription Factor AmrZ Utilizes Multiple DNA Binding Modes to Recognize Activator and Repressor Sequences of Pseudomonas aeruginosa Virulence GenesDissecting the role of DNA sequence in Helicobacter pylori NikR/DNA recognition.The N-terminal arm of the Helicobacter pylori Ni2+-dependent transcription factor NikR is required for specific DNA binding.Integrative computational protocol for the discovery of inhibitors of the Helicobacter pylori nickel response regulator (NikR).Orientation and stereodynamic paths of planar monodentate ligands in square planar nickel N2S complexes.Imidazole-containing (N3S)-Ni(II) complexes relating to nickel containing biomolecules.Geobacter uraniireducens NikR displays a DNA binding mode distinct from other members of the NikR family.Helicobacter pylori NikR protein exhibits distinct conformations when bound to different promoters.Metalloregulatory proteins: metal selectivity and allosteric switching.Coordination chemistry of bacterial metal transport and sensing.Metal site occupancy and allosteric switching in bacterial metal sensor proteins.Role of the N-terminus in determining metal-specific responses in the E. coli Ni- and Co-responsive metalloregulator, RcnR.Apo and nickel-bound forms of the Pyrococcus horikoshii species of the metalloregulatory protein: NikR characterized by molecular dynamics simulations.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.Specific metal recognition in nickel trafficking.The hierarchic network of metal-response transcription factors in Escherichia coli.Functional annotation of a novel toxin-antitoxin system Xn-RelT of Xenorhabdus nematophila; a combined in silico and in vitro approach.Nickel-responsive transcriptional regulators.Metallochaperones and metalloregulation in bacteria.Mycobacterium tuberculosis NmtR harbors a nickel sensing site with parallels to Escherichia coli RcnR.Surface plasmon resonance and isothermal titration calorimetry to monitor the Ni(II)-dependent binding of Helicobacter pylori NikR to DNA.Nickel Sequestration by the Host-Defense Protein Human Calprotectin.Molecular dynamics simulation of the Escherichia coli NikR protein: equilibrium conformational fluctuations reveal interdomain allosteric communication pathways.On the interaction of Helicobacter pylori NikR, a Ni(II)-responsive transcription factor, with the urease operator: in solution and in silico studies.Recruitment of the ParG segregation protein to different affinity DNA sites
P2860
Q26801203-85693B2B-0E2E-4135-8226-4477D7864C3EQ26802012-E7B7DF58-8307-40D8-B0DC-33857E14B088Q27649535-654A0D0E-D590-46EB-AE70-7E7506369FC3Q27650991-66B9122E-E268-431F-BFD1-981928E24AC5Q27654530-37F90B59-28FB-4FBB-8F4D-74ECAD92A5C4Q27656008-534267C8-3EC4-4447-8B02-EEB78EAB24BFQ27659056-C554F44D-A6B6-496A-A021-F6DD9AD79569Q27664043-72A5E895-95F3-485A-89C1-FCD6A5668AD0Q27664650-93AA0D97-0AC0-4FBE-9052-A2C0095F4FF5Q27666129-D63D7D13-D354-41C0-B894-798049844B42Q27670660-F39C769D-8966-4F02-8385-8E0855BE9FBBQ27674412-0700B116-6EEC-4F1E-9CD1-C6704FAA4B0BQ27678006-1B1DD1B4-B358-4F57-B693-8E3C319533F3Q27678228-CF5A19FB-7B2D-4853-B322-DCE4494E9864Q27678592-2E92EDE6-C0AD-49AA-988B-1B654E07B8FCQ29346545-51260F73-63C9-410D-8732-3BCE9A46F6E6Q29346547-A83718E4-F681-4423-88FC-685252AA457EQ33832481-3F5845A3-79BA-4ABD-A3C4-0FC1FE27F945Q33985282-FA1DA843-8CDE-4BE5-809B-DA4E93F00CEFQ34015243-93009CF2-42C1-4B00-890D-FC0936EAB9CFQ34119172-CB405E2E-7C70-401E-AA89-60782ED604A6Q34963006-1EE6149B-6772-411B-BF09-35B8149B9352Q34990148-D2BBDDFE-EA94-43A0-BC6E-61C2775EA81AQ35005569-388A0C43-06E7-4E90-BAB8-C21C7919C63BQ35851912-EA999CD5-34D8-4952-A935-0C59E1C75196Q36032583-6A107B1E-4196-4D46-A3ED-12A89E2A7910Q37480906-6157E3A3-D830-412C-A0EA-E709C9F4AFF2Q37743209-7B92EFC0-24CC-4D3E-93A8-18FD97B187D9Q37767748-AF1A38B4-B127-4C19-B2E2-375E03C92702Q38042673-F7C98F10-8263-4FDF-BBFD-FFBD4309472CQ38230887-85934FF0-4EBD-466C-92D8-E56A1DBDD0E3Q38433531-864B6813-20DB-4B77-A215-7284FB7EDC93Q38534594-EF25A9EC-7456-4BD6-A0AF-088EF219C3D8Q39294308-BEAB07AC-1B46-45D0-9B46-6308FB2E759AQ39407946-85C57C7B-DEC9-47E4-8A52-BCA538FFE1B3Q39435560-A9FED85D-229F-4B4C-9C64-7675F546E981Q40188001-EAB9F2EA-173F-440A-8DD1-D8EA7B3EBEF8Q40737258-7F7434B5-ED25-47A8-9E06-ED8570A5CCBEQ41092715-D92A36DB-0768-49F8-B311-7B1D9037ECECQ41368080-EEDCA5C1-B02D-471D-B824-38AF73D8570D
P2860
NikR-operator complex structure and the mechanism of repressor activation by metal ions.
description
2006 nî lūn-bûn
@nan
2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
NikR-operator complex structure and the mechanism of repressor activation by metal ions.
@ast
NikR-operator complex structure and the mechanism of repressor activation by metal ions.
@en
type
label
NikR-operator complex structure and the mechanism of repressor activation by metal ions.
@ast
NikR-operator complex structure and the mechanism of repressor activation by metal ions.
@en
prefLabel
NikR-operator complex structure and the mechanism of repressor activation by metal ions.
@ast
NikR-operator complex structure and the mechanism of repressor activation by metal ions.
@en
P2860
P50
P356
P1476
NikR-operator complex structure and the mechanism of repressor activation by metal ions.
@en
P2093
Catherine L Drennan
P2860
P304
13676-13681
P356
10.1073/PNAS.0606247103
P407
P577
2006-08-31T00:00:00Z