Legionella pneumophila major acid phosphatase and its role in intracellular infection
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Crystal Structures of the Histidine Acid Phosphatase from Francisella tularensis Provide Insight into Substrate RecognitionLegionella pneumophila type II secretion dampens the cytokine response of infected macrophages and epitheliaInositol phosphatase activity of the Escherichia coli agp-encoded acid glucose-1-phosphatase.Proteomic characterization of the whole secretome of Legionella pneumophila and functional analysis of outer membrane vesicles.Inhibition of AcpA phosphatase activity with ascorbate attenuates Francisella tularensis intramacrophage survivalAcid phosphatases do not contribute to the pathogenesis of type A Francisella tularensis.Characterization of the major secreted zinc metalloprotease- dependent glycerophospholipid:cholesterol acyltransferase, PlaC, of Legionella pneumophila.Molecular pathogenesis of infections caused by Legionella pneumophilaLegionella cardiaca sp. nov., isolated from a case of native valve endocarditis in a human heart.Legionella and Legionnaires' disease: 25 years of investigation.Type II protein secretion is a subset of the PilD-dependent processes that facilitate intracellular infection by Legionella pneumophila.Characterization of the gene encoding the major secreted lysophospholipase A of Legionella pneumophila and its role in detoxification of lysophosphatidylcholine.Purification and characterization of a UDP-glucosyltransferase produced by Legionella pneumophilaA type II secreted RNase of Legionella pneumophila facilitates optimal intracellular infection of Hartmannella vermiformis.Legionella pneumophila Mip, a surface-exposed peptidylproline cis-trans-isomerase, promotes the presence of phospholipase C-like activity in culture supernatantsThe surfactant of Legionella pneumophila Is secreted in a TolC-dependent manner and is antagonistic toward other Legionella speciesLegionella pneumophila type II secretome reveals unique exoproteins and a chitinase that promotes bacterial persistence in the lungCrystallization and preliminary crystallographic analysis of the major acid phosphatase from Legionella pneumophila.The acid phosphatase AcpA is secreted in vitro and in macrophages by Francisella spp.Legionella pneumophila type II protein secretion promotes virulence in the A/J mouse model of Legionnaires' disease pneumonia.Crystallization of a newly discovered histidine acid phosphatase from Francisella tularensis.The type II secretion system of Legionella pneumophila elaborates two aminopeptidases, as well as a metalloprotease that contributes to differential infection among protozoan hosts.Multiple Legionella pneumophila Type II secretion substrates, including a novel protein, contribute to differential infection of the amoebae Acanthamoeba castellanii, Hartmannella vermiformis, and Naegleria lovaniensisHost cell processes that influence the intracellular survival of Legionella pneumophila.Type II Secretion Is Necessary for Optimal Association of the Legionella-Containing Vacuole with Macrophage Rab1B but Enhances Intracellular Replication Mainly by Rab1B-Independent Mechanisms.Many substrates and functions of type II secretion: lessons learned from Legionella pneumophila.Life Stage-specific Proteomes of Legionella pneumophila Reveal a Highly Differential Abundance of Virulence-associated Dot/Icm effectors.The type II protein secretion system of Legionella pneumophila promotes growth at low temperatures.Disruption of the phagosomal membrane and egress of Legionella pneumophila into the cytoplasm during the last stages of intracellular infection of macrophages and Acanthamoeba polyphaga.The novel Legionella pneumophila type II secretion substrate NttC contributes to infection of amoebae Hartmannella vermiformis and Willaertia magna.Importance of type II secretion for survival of Legionella pneumophila in tap water and in amoebae at low temperaturesMoraxella catarrhalis synthesizes an autotransporter that is an acid phosphatase.Legionella pneumophila secretes an endoglucanase that belongs to the family-5 of glycosyl hydrolases and is dependent upon type II secretion.The Legionella pneumophila tatB gene facilitates secretion of phospholipase C, growth under iron-limiting conditions, and intracellular infection.Rapid escape of the dot/icm mutants of Legionella pneumophila into the cytosol of mammalian and protozoan cells.Surface translocation by Legionella pneumophila: a form of sliding motility that is dependent upon type II protein secretion.The global regulatory proteins LetA and RpoS control phospholipase A, lysophospholipase A, acyltransferase, and other hydrolytic activities of Legionella pneumophila JR32.Type II Secretion-Dependent Aminopeptidase LapA and Acyltransferase PlaC Are Redundant for Nutrient Acquisition during Legionella pneumophila Intracellular Infection of Amoebas.
P2860
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P2860
Legionella pneumophila major acid phosphatase and its role in intracellular infection
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին 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
Legionella pneumophila major acid phosphatase and its role in intracellular infection
@ast
Legionella pneumophila major acid phosphatase and its role in intracellular infection
@en
Legionella pneumophila major acid phosphatase and its role in intracellular infection
@nl
type
label
Legionella pneumophila major acid phosphatase and its role in intracellular infection
@ast
Legionella pneumophila major acid phosphatase and its role in intracellular infection
@en
Legionella pneumophila major acid phosphatase and its role in intracellular infection
@nl
prefLabel
Legionella pneumophila major acid phosphatase and its role in intracellular infection
@ast
Legionella pneumophila major acid phosphatase and its role in intracellular infection
@en
Legionella pneumophila major acid phosphatase and its role in intracellular infection
@nl
P2860
P1476
Legionella pneumophila major acid phosphatase and its role in intracellular infection
@en
P2093
N P Cianciotto
P2860
P304
P356
10.1128/IAI.69.1.177-185.2001
P407
P577
2001-01-01T00:00:00Z