Siderophores: structure and function of microbial iron transport compounds.
about
The Aspergillus fumigatus siderophore biosynthetic gene sidA, encoding L-ornithine N5-oxygenase, is required for virulenceCommon themes in microbial pathogenicity revisitedComparative and functional genomic analyses of iron transport and regulation in Leptospira sppEnterobactin: an archetype for microbial iron transportBacterial response to siderophore and quorum-sensing chemical signals in the seawater microbial communityCharacterization of the iron-regulated desA promoter of Streptomyces pilosus as a system for controlled gene expression in actinomycetesMonoclonal antibodies against the iron regulated outer membrane Proteins of Acinetobacter baumannii are bactericidalThe outer membrane protein Omp35 affects the reduction of Fe(III), nitrate, and fumarate by Shewanella oneidensis MR-1Potential Biotechnological Strategies for the Cleanup of Heavy Metals and MetalloidsROSET Model of TonB Action in Gram-Negative Bacterial Iron AcquisitionPhytochelators Intended for Clinical Use in Iron Overload, Other Diseases of Iron Imbalance and Free Radical PathologyEngineering rhizobial bioinoculants: a strategy to improve iron nutritionMechanisms of mammalian iron homeostasisA putative P-type ATPase required for virulence and resistance to haem toxicity in Listeria monocytogenesCrystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuAHigh resolution structure of an alternate form of the ferric ion binding protein from Haemophilus influenzaeArchitecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulatorCrystal Structure and Biochemical Features of EfeB/YcdB from Escherichia coli O157Structures of Streptococcus pneumoniae PiaA and Its Complex with Ferrichrome Reveal Insights into the Substrate Binding and Release of High Affinity Iron TransportersStructural insight into the ISC domain of VibB from Vibrio cholerae at atomic resolution: a snapshot just before the enzymatic reactionGGA2- and ubiquitin-dependent trafficking of Arn1, the ferrichrome transporter of Saccharomyces cerevisiaeA receptor domain controls the intracellular sorting of the ferrichrome transporter, ARN1.The role of the FRE family of plasma membrane reductases in the uptake of siderophore-iron in Saccharomyces cerevisiae.Siderophore-iron uptake in saccharomyces cerevisiae. Identification of ferrichrome and fusarinine transporters.Genes Involved in the Biosynthesis and Transport of Acinetobactin in Acinetobacter baumanniiHistoplasma requires SID1, a member of an iron-regulated siderophore gene cluster, for host colonizationThe Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophagesBacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressorsIdentification of new, conserved, non-ribosomal peptide synthetases from fluorescent pseudomonads involved in the biosynthesis of the siderophore pyoverdineLipoprotein FtsB in Streptococcus pyogenes binds ferrichrome in two steps with residues Tyr137 and Trp204 as critical ligandsN-octanoyl dopamine inhibits the expression of a subset of κB regulated genes: potential role of p65 Ser276 phosphorylationProduction of the catechol type siderophore bacillibactin by the honey bee pathogen Paenibacillus larvaeDisruption of Transporters Affiliated with Enantio-Pyochelin Biosynthesis Gene Cluster of Pseudomonas protegens Pf-5 Has Pleiotropic EffectsA first analysis of metallome biosignatures of hyperthermophilic ArchaeaGlobal analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon.Interaction of Bacillus subtilis Fur (ferric uptake repressor) with the dhb operator in vitro and in vivo.Structure-function relationships in the bifunctional ferrisiderophore FpvA receptor from Pseudomonas aeruginosa.Exchangeability of N termini in the ligand-gated porins of Escherichia coli.Energy-dependent motion of TonB in the Gram-negative bacterial inner membraneIron-binding compounds from Agrobacterium spp.: biological control strain Agrobacterium rhizogenes K84 produces a hydroxamate siderophore
P2860
Q24534744-3334C637-8D9C-435F-B478-B1305A1FB2A4Q24643808-3D852DE6-C8A1-45BF-BFEC-1EF33D4D13AFQ24673088-A33ED2BA-4D5F-46C9-9B84-119B20B645F2Q24683689-CB4285E1-2CDE-48F2-B740-83DE3670FE5FQ24794926-EF1400B3-2EA7-4B81-8F3E-2D6FDFF1AB46Q24801939-AE50EB73-A449-4E12-8E88-8B44D55E172AQ24803309-1062ABE4-B5F4-4926-98B1-58F21B4FB374Q24804045-A7F22A42-8C61-4CCD-AF8C-7C4C9DEEBE07Q26750969-30C45551-D274-4C7A-8406-5DB2B03086E0Q26770858-9411811E-7FAB-48A3-9E1F-9C6B7A6D5623Q26863390-9BA507BD-612E-4ED1-A672-B8E36B597081Q26998396-9827B37B-687B-4818-B210-BEBD8BD2B5DFQ27010510-8D54F5EB-A1F5-4664-82D3-5B84982EA3AFQ27309201-7FA26441-C8E1-4800-B2EA-FB37D230AC7CQ27624891-73E8A6FB-277C-4107-A32E-3474DA7ECDF6Q27640323-41C4D6FA-F999-4F2E-8936-DB2E6F64DE62Q27640480-8974D207-E06A-4441-9820-216CDC96312DQ27666975-0BE39B86-005C-4276-B4A5-5851F6EF0734Q27679699-A51C7434-19F0-4AD2-80D5-024B34FB8B0CQ27682324-CAB2DBC4-56CC-49CE-90B1-581759B34D88Q27932123-E6EC90C1-A544-436B-8E32-0887E72945CBQ27936416-A6660917-FE73-437C-BE7C-956CC0C47735Q27936996-B545E79A-E8BF-4425-933D-211D61311EB6Q27938421-9F12730D-0CE4-4C8F-BA7C-52F241D11F6CQ28084863-1FD5DFB4-0954-46D2-888B-0CA826674F5AQ28472490-BD433A9E-C99C-4562-BA60-8D3111057EBDQ28487578-3BFD6046-C643-4830-AA61-CCE2DF22C1B2Q28488940-23CF166C-F15B-4EFD-912F-BD1F166E3134Q28493064-8862E491-E7B5-4217-90FF-694B24654779Q28534055-E4D9725A-171C-4DB7-A417-7B874646E0D7Q28536426-D8ADE804-0474-4F11-A431-BBE9FD3DDC1FQ28543101-682FE12A-F2B6-401A-B069-F4A941C9DBABQ28552805-28991061-C114-46D9-8FB2-C5B241A614FEQ28710370-3566701A-976A-4026-A37C-47C18BAC9932Q29346686-E09F865E-1802-4C1E-910A-A28FB9AFF381Q29346693-C3975D42-A06E-494E-A19D-BE1D5750E502Q30157396-4B9926E3-36DA-439E-A1CC-4EB110E87677Q30168335-6A94C800-B5D1-4875-A5BB-9D3DE115CC99Q30541432-50E30D0D-FFC4-49E4-B628-D6B9D3D75FD7Q30649455-AC57BD21-9D14-4AEA-8F9F-2026EC0C70B2
P2860
Siderophores: structure and function of microbial iron transport compounds.
description
1995 nî lūn-bûn
@nan
1995 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Siderophores: structure and function of microbial iron transport compounds.
@ast
Siderophores: structure and function of microbial iron transport compounds.
@en
Siderophores: structure and function of microbial iron transport compounds.
@nl
type
label
Siderophores: structure and function of microbial iron transport compounds.
@ast
Siderophores: structure and function of microbial iron transport compounds.
@en
Siderophores: structure and function of microbial iron transport compounds.
@nl
prefLabel
Siderophores: structure and function of microbial iron transport compounds.
@ast
Siderophores: structure and function of microbial iron transport compounds.
@en
Siderophores: structure and function of microbial iron transport compounds.
@nl
P2860
P356
P1476
Siderophores: structure and function of microbial iron transport compounds.
@en
P2093
Neilands JB
P2860
P304
26723-26726
P356
10.1074/JBC.270.45.26723
P407
P577
1995-11-01T00:00:00Z