Siderocalins: siderophore-binding proteins of the innate immune system.
about
Structure of a Burkholderia pseudomallei trimeric autotransporter adhesin headTowards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson's, Huntington's, Alzheimer's, prions, bactericides, chemical toxicology and others as examplesRoles of bacterial and mammalian siderophores in host-pathogen interactionsA new crystal form of human tear lipocalin reveals high flexibility in the loop region and induced fit in the ligand cavityThe v-myc-induced Q83 Lipocalin Is a SiderocalinGalline Ex-FABP Is an Antibacterial Siderocalin and a Lysophosphatidic Acid Sensor Functioning through Dual Ligand SpecificitiesCombining functional and structural genomics to sample the essential Burkholderia structomeAn extracellular siderophore is required to maintain the mutualistic interaction of Epichloë festucae with Lolium perenneThe role of iron in the immune response to bacterial infectionMammalian siderophores, siderophore-binding lipocalins, and the labile iron poolSiderocalins: Siderophore binding proteins evolved for primary pathogen host defenseThe dormant blood microbiome in chronic, inflammatory diseases.Computational design of protein-small molecule interfaces.Microbial iron acquisition: marine and terrestrial siderophores.Iron homeostasis and the inflammatory responseKlebsiella pneumoniae yersiniabactin promotes respiratory tract infection through evasion of lipocalin 2Iron metabolism in aerobes: managing ferric iron hydrolysis and ferrous iron autoxidation.Trihydroxamate siderophore-fluoroquinolone conjugates are selective sideromycin antibiotics that target Staphylococcus aureus.Cellular iron metabolism in prognosis and therapy of breast cancer.Human Metabolome-derived Cofactors Are Required for the Antibacterial Activity of Siderocalin in Urine.War-Fe-re: iron at the core of fungal virulence and host immunity.Prawn lipocalin: characterization of a color shift induced by gene knockdown and ligand binding assay.The Yin and Yang of copper during infection.Siderophores as "Trojan Horses": tackling multidrug resistance?Extracellular heme uptake and the challenges of bacterial cell membranes.Measurement of neutrophil gelatinase-associated lipocalin (NGAL) in patients with non-communicable diseases: any additional benefit?
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P2860
Siderocalins: siderophore-binding proteins of the innate immune system.
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Siderocalins: siderophore-binding proteins of the innate immune system.
@ast
Siderocalins: siderophore-binding proteins of the innate immune system.
@en
Siderocalins: siderophore-binding proteins of the innate immune system.
@nl
type
label
Siderocalins: siderophore-binding proteins of the innate immune system.
@ast
Siderocalins: siderophore-binding proteins of the innate immune system.
@en
Siderocalins: siderophore-binding proteins of the innate immune system.
@nl
prefLabel
Siderocalins: siderophore-binding proteins of the innate immune system.
@ast
Siderocalins: siderophore-binding proteins of the innate immune system.
@en
Siderocalins: siderophore-binding proteins of the innate immune system.
@nl
P2093
P2860
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P1476
Siderocalins: siderophore-binding proteins of the innate immune system.
@en
P2093
Colin Corrent
Matthew C Clifton
Roland K Strong
P2860
P2888
P304
P356
10.1007/S10534-009-9207-6
P577
2009-01-30T00:00:00Z
P5875
P6179
1048298476