ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12.
about
Structure, function, and evolution of bacterial ATP-binding cassette systemsStructural and functional analysis of the finished genome of the recently isolated toxic Anabaena sp. WA102.FutA2 is a ferric binding protein from Synechocystis PCC 6803Discovery and characterization of a unique mycobacterial heme acquisition systemTwo Distinct Ferritin-like Molecules in Pseudomonas aeruginosa : The Product of the bfrA Gene Is a Bacterial Ferritin (FtnA) and Not a Bacterioferritin (Bfr)Induction of the ferritin gene (ftnA) of Escherichia coli by Fe(2+)-Fur is mediated by reversal of H-NS silencing and is RyhB independentThe ferrichrome uptake pathway in Pseudomonas aeruginosa involves an iron release mechanism with acylation of the siderophore and recycling of the modified desferrichromeThe Complete Genome Sequence of the Emerging Pathogen Mycobacterium haemophilum Explains Its Unique Culture RequirementsIron homeostasis in the Rhodobacter genusIdentification of the periplasmic cobalamin-binding protein BtuF of Escherichia coli.Characterization of heme uptake cluster genes in the fish pathogen Vibrio anguillarum.ATP-binding cassette systems in Burkholderia pseudomallei and Burkholderia mallei.Purification, crystallization and data collection of Pectobacterium chrysanthemi AcsD, a type A siderophore synthetaseComparative genomic analyses of nickel, cobalt and vitamin B12 utilizationIdentification of rhtX and fptX, novel genes encoding proteins that show homology and function in the utilization of the siderophores rhizobactin 1021 by Sinorhizobium meliloti and pyochelin by Pseudomonas aeruginosa, respectivelyIsolation and characterization of FecA- and FeoB-mediated iron acquisition systems of the spirochete Leptospira biflexa by random insertional mutagenesis.Inactivation of the Ecs ABC transporter of Staphylococcus aureus attenuates virulence by altering composition and function of bacterial wallThe iron-regulated iupABC operon is required for saprophytic growth of the intracellular pathogen Rhodococcus equi at low iron concentrations.Regulation of petrobactin and bacillibactin biosynthesis in Bacillus anthracis under iron and oxygen variationRegulation of the expression of the Vibrio parahaemolyticus peuA gene encoding an alternative ferric enterobactin receptorProteobactin and a yersiniabactin-related siderophore mediate iron acquisition in Proteus mirabilis.Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes.Structural basis for iron binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens.FhuD1, a ferric hydroxamate-binding lipoprotein in Staphylococcus aureus: a case of gene duplication and lateral transfer.A widely distributed bacterial pathway for siderophore biosynthesis independent of nonribosomal peptide synthetases.Genome-wide Analysis of Mycoplasma hominis for the Identification of Putative Therapeutic Targets.Identification and characterization of a Streptococcus pyogenes operon involved in binding of hemoproteins and acquisition of iron.Enhancement of in vitro growth of pathogenic bacteria by norepinephrine: importance of inoculum density and role of transferrinCoordination chemistry of bacterial metal transport and sensing.Acquisition of siderophores in gram-negative bacteria.Lifestyle evolution in cyanobacterial symbionts of sponges.Iron transport systems in Neisseria meningitidisMultiple ABC transporters are involved in the acquisition of petrobactin in Bacillus anthracis.Mycobacteria, metals, and the macrophageATP-binding cassette transporters are targets for the development of antibacterial vaccines and therapies.Phylogenetic and Functional Substrate Specificity for Endolithic Microbial Communities in Hyper-Arid Environments.Ferric Uptake Regulator Fur Control of Putative Iron Acquisition Systems in Clostridium difficileAnalysis of a ferric uptake regulator (Fur) mutant of Desulfovibrio vulgaris HildenboroughIn silico identification of essential proteins in Corynebacterium pseudotuberculosis based on protein-protein interaction networksThe hydroxamate siderophore rhequichelin is required for virulence of the pathogenic actinomycete Rhodococcus equi.
P2860
Q24643436-59F06CBD-95F1-4C58-9929-9AFAFF503FB6Q27316494-0BAECCC0-73AE-414F-B22C-A3A06C82F273Q27649789-A4A8340B-C635-4957-9AAF-FEBE45A924D7Q27667213-0CD5DF8A-3637-42C1-ABD8-874CA76363FEQ27667858-8DADDF92-84A5-4AE2-8AF0-4356B199AB05Q28267896-03AD8BE4-B35F-4FA1-A36E-35FF00D84FE5Q28493210-79345CBD-4AFE-4BD1-BF0C-BACAB6074F80Q28607074-CA01AD79-1B61-416B-9874-E1DE39E4D9CBQ28660942-30E4CBFD-F3EC-45C2-A3F8-F4B26D9685E8Q30308529-E9A7B51D-87D9-441F-8461-01B8CE5FAAE6Q31108743-03DBF807-D319-4465-B6A7-D580DA015A18Q33280317-D12D1633-B0C8-435A-8E18-2991A3C7C936Q33383437-03AE1481-8E4E-4427-8DF6-0A1FA6F92DF4Q33408048-78DA9233-EB47-4F8D-8AE7-2724774DD146Q33551442-2038F748-EAD6-4573-9F36-909DD73F4302Q33755272-E4119CFB-E520-494E-A83F-71F51AA990D6Q33769673-CA52EB6F-36E9-4F36-9E11-F3F6AAF4EF77Q33788460-7A48F48E-A4EF-4996-83C8-DBEA8E9E02A5Q33932861-CA58E80D-2326-4683-93D3-9B179231B0AAQ34078721-DF868D51-DC4D-4585-A35E-E6200CC1538DQ34183602-6BBCA00B-9917-41B3-8A5F-08846C6E5538Q34215167-EE1D96D7-790C-4B0A-AE6D-30FD8A3AE039Q34349646-35C9A0D8-08A8-4D42-A71D-BB0317ECF007Q34357691-9DAC665E-19AA-4744-847B-FCB5B510CC60Q34395738-68433D8D-6AA8-4A6F-B8C9-305ECF26D42EQ34680309-FCC0B0D2-E8F7-44D9-A0B2-6ADE14B45B7AQ34713958-E36C3C05-E798-46D9-AEC5-15DFA99B263FQ34718907-63D091B7-7F56-49FE-A741-857DAB6317C3Q35005569-4F81A29A-0312-4B16-9175-24133C6D3AECQ35058516-326C0D41-4427-48D8-A0EE-4F2BBBECD543Q35676300-BE838597-2D2E-4F78-95CF-97D482E36F84Q35684980-C37B3904-23DF-4BB0-9C3B-8EDF940D43B7Q35881671-A5F30738-D310-40A4-9C93-8C91A9CF9D7BQ35907046-009EB3E7-3C54-472A-BA40-1158FF9BF312Q35959243-7A8666A5-A43E-4105-890C-498919F160F5Q35970077-4E80734A-A2B2-4DCC-90C8-1055117BE255Q35972984-F7E3B83A-4AB2-4B55-9120-6B47354CF962Q36092391-78BC6C2F-FAC2-4BE6-8E7D-A466AF21E956Q36183157-1A0C7E0F-F1AD-462A-98B4-EF18D2179C04Q36396908-6CB5CB74-0253-408B-A02A-06E870846E31
P2860
ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12.
description
2001 nî lūn-bûn
@nan
2001 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12.
@ast
ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12.
@en
ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12.
@nl
type
label
ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12.
@ast
ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12.
@en
ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12.
@nl
prefLabel
ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12.
@ast
ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12.
@en
ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12.
@nl
P921
P1476
ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12.
@en
P2093
P304
P356
10.1016/S0923-2508(01)01200-1
P577
2001-04-01T00:00:00Z