about
Structure of a unique twofold symmetric haem-binding siteRole of the ferric uptake regulator of Pseudomonas aeruginosa in the regulation of siderophores and exotoxin A expression: purification and activity on iron-regulated promotersThe enhancement of plant growth by free-living bacteriaEvidence of Fe3+ interaction with the plug domain of the outer membrane transferrin receptor protein of Neisseria gonorrhoeae: implications for Fe transportGrowth of Pseudomonas mendocina on Fe(III) (hydr)oxides.Genomic analysis and temperature-dependent transcriptome profiles of the rhizosphere originating strain Pseudomonas aeruginosa M18.Antigenic and sequence diversity in gonococcal transferrin-binding protein A.Identification of regulatory elements that control expression of the tbpBA operon in Neisseria gonorrhoeae.Specific ligand binding attributable to individual epitopes of gonococcal transferrin binding protein A.Binding and accumulation of hemin in Porphyromonas gingivalis are induced by hemin.Cloning, sequencing, and characterization of the gene encoding FrpB, a major iron-regulated, outer membrane protein of Neisseria gonorrhoeaeThe iron-repressed, AraC-like regulator MpeR activates expression of fetA in Neisseria gonorrhoeaeBinding and surface exposure characteristics of the gonococcal transferrin receptor are dependent on both transferrin-binding proteins.Isolation and analysis of a fur mutant of Neisseria gonorrhoeae.Identification of transferrin-binding domains in TbpB expressed by Neisseria gonorrhoeae.The physiological role of ferritin-like compounds in bacteria.Beyond the Crystal Structure: Insight into the Function and Vaccine Potential of TbpA Expressed by Neisseria gonorrhoeae.Identification of TbpA residues required for transferrin-iron utilization by Neisseria gonorrhoeae.Augmenting Sulfur Metabolism and Herbivore Defense in Arabidopsis by Bacterial Volatile SignalingAnalysis of yggX and gshA mutants provides insights into the labile iron pool in Salmonella enterica.Characterization of a novel Neisseria meningitidis Fur and iron-regulated operon required for protection from oxidative stress: utility of DNA microarray in the assignment of the biological role of hypothetical genes.The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni.The search for antimicrobial agents effective against bacteria resistant to multiple antibiotics.Staphylococcal iron requirements, siderophore production, and iron-regulated protein expression.Identification and characterization of a novel ferric reductase from the hyperthermophilic Archaeon Archaeoglobus fulgidus.Advantage provided by iron for Escherichia coli growth and cultivability in drinking water.Construction of a ferritin-deficient mutant of Campylobacter jejuni: contribution of ferritin to iron storage and protection against oxidative stress.Cloning, sequencing and expression of the transferrin-binding protein 1 gene from Actinobacillus pleuropneumoniae.Opposing selective forces for expression of the gonococcal lactoferrin receptor.Identification and cloning of a fur homologue from Neisseria meningitidis.Characterization of two genes encoding ferritin-like protein in Actinobacillus actinomycetemcomitans.Overproduction of Campylobacter ferritin in Escherichia coli and induction of paracrystalline inclusion by ferrous compound.Electrospray ionization mass spectrometry analysis of the apo- and metal-substituted forms of the Fur protein
P2860
Q27729865-923CFC89-4F34-45AC-9625-5DEBEC6B74D9Q28492710-F0B8906A-4E6E-4856-A122-1176FB7197EDQ29398343-F9151CDB-8B91-45C5-975E-CE09E5AB3D85Q30155359-99B6CC52-7225-4A1A-A1EB-27FEF1F17966Q33990395-1EDDBFFD-5565-4ADE-B6F0-46399D61CCBFQ34007844-E4F78F7F-44E6-4C83-B33A-498B304E399EQ34007901-D891DB7A-0383-4D8F-8935-B2C26DC895A0Q34056830-BB68D351-D52D-4ED8-85C0-910DCEADFBF1Q34117720-321C350E-FEF7-4809-8AC8-8780B73EB458Q34530053-ECEB5ED8-C29F-4D54-9C07-54BAABDEB8BFQ35582900-FC9D2571-0A11-4863-8472-9772DF1EEC05Q35598127-8717B227-A0E1-4867-8494-D5883BB04364Q35603469-B608E2B6-FB4C-4760-B91C-12E7276FA6F6Q35609778-4B680F61-3EC7-4CFC-A9B9-3051CA8B0A90Q35913549-C95A1556-38EA-40D1-A9E4-E8778BE7772BQ35921314-01387871-8351-46BB-A423-783A669550F9Q36137942-62876454-CC6A-409C-96E9-78780054547CQ36593986-EF6BE26F-A672-44CD-B9C0-BFD72F7F6734Q36777986-93780982-D780-4B07-B859-639F85FC0594Q36974582-8794E61D-AEBF-4A7C-8687-84DDE331D83CQ38334755-D2B52CC5-BF0D-4A69-A42E-2573AF34D3ACQ39705906-A7962873-A26E-437B-9163-44F6CD4B4368Q39783740-36F3864F-E286-4223-B8AA-82ED8B902892Q39860497-34D25A37-F225-480A-9DF1-C682E22557C4Q41706855-6F78EE11-1C4A-47AA-B3DD-DFEE229A0EF6Q41777392-C2314F0A-25C2-407F-B397-DB1D3C11B3BBQ42638501-EF4BFB76-94D7-4463-BD61-A8551B12B1B0Q42981655-BFF134D9-EC61-49B2-B5EC-33690757C16BQ44622327-23FF25C9-B7BA-449F-A2AC-C84C9CB8B6C2Q48085197-7388C44B-953C-4913-B6F3-6A5904E80C4AQ48326243-461FEB87-115C-4EAE-BCBE-EFA4C9CE91C3Q54573320-A0F65420-C8D5-4243-B0FE-73422F8B76C6Q58110884-67A39A66-A78E-4011-9792-6577F5EC1D3C
P2860
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Iron assimilation and storage in prokaryotes.
@ast
Iron assimilation and storage in prokaryotes.
@en
type
label
Iron assimilation and storage in prokaryotes.
@ast
Iron assimilation and storage in prokaryotes.
@en
prefLabel
Iron assimilation and storage in prokaryotes.
@ast
Iron assimilation and storage in prokaryotes.
@en
P1476
Iron assimilation and storage in prokaryotes.
@en
P2093
P304
P356
10.1099/00221287-138-12-2475
P577
1992-12-01T00:00:00Z