A PhoP-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to alpha-helical antimicrobial peptides.
about
Sap transporter mediated import and subsequent degradation of antimicrobial peptides in HaemophilusThe pleiotropic two-component regulatory system PhoP-PhoQCapsule polysaccharide mediates bacterial resistance to antimicrobial peptidesOmpT outer membrane proteases of enterohemorrhagic and enteropathogenic Escherichia coli contribute differently to the degradation of human LL-37The omptins of Yersinia pestis and Salmonella enterica cleave the reactive center loop of plasminogen activator inhibitor 1Lipid A modification systems in gram-negative bacteriaProteolytic inactivation of tissue factor pathway inhibitor by bacterial omptinsAntibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistanceHelicobacter and salmonella persistent infection strategiesTransfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteriaA protein important for antimicrobial peptide resistance, YdeI/OmdA, is in the periplasm and interacts with OmpD/NmpCMolecular basis of bacterial outer membrane permeability revisitedFibrinolytic and procoagulant activities of Yersinia pestis and Salmonella enterica.The single substitution I259T, conserved in the plasminogen activator Pla of pandemic Yersinia pestis branches, enhances fibrinolytic activity.Invited review: Breaking barriers--attack on innate immune defences by omptin surface proteases of enterobacterial pathogens.Structural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membraneOmptin proteins: an expanding family of outer membrane proteases in Gram-negative Enterobacteriaceae.Protein regions important for plasminogen activation and inactivation of alpha2-antiplasmin in the surface protease Pla of Yersinia pestis.Novel 45-kilodalton leptospiral protein that is processed to a 31-kilodalton growth-phase-regulated peripheral membrane protein.Cationic antimicrobial peptide resistance in Neisseria meningitidis.Successful identification of novel agents to control infectious diseases from screening mixture-based peptide combinatorial libraries in complex cell-based bioassays.Identification of Proteus mirabilis mutants with increased sensitivity to antimicrobial peptidesSubstrate specificity of the Escherichia coli outer membrane protease OmpT.Shield as signal: lipopolysaccharides and the evolution of immunity to gram-negative bacteria.The autodisplay story, from discovery to biotechnical and biomedical applications.Lysozyme M deficiency leads to an increased susceptibility to Streptococcus pneumoniae-induced otitis mediaEngineering next generation proteases.Feedback inhibition in the PhoQ/PhoP signaling system by a membrane peptideA mutation in the sap operon attenuates survival of nontypeable Haemophilus influenzae in a chinchilla model of otitis media.Salmonellae PhoPQ regulation of the outer membrane to resist innate immunity.CD4+ T cells and toll-like receptors recognize Salmonella antigens expressed in bacterial surface organelles.Identification of Legionella pneumophila rcp, a pagP-like gene that confers resistance to cationic antimicrobial peptides and promotes intracellular infection.Host defense peptide resistance contributes to colonization and maximal intestinal pathology by Crohn's disease-associated adherent-invasive Escherichia coli.Resolvase-in vivo expression technology analysis of the Salmonella enterica serovar Typhimurium PhoP and PmrA regulons in BALB/c miceGenome-based identification of chromosomal regions specific for Salmonella spp.Visualization of vacuolar acidification-induced transcription of genes of pathogens inside macrophages.mig-14 is a Salmonella gene that plays a role in bacterial resistance to antimicrobial peptidesTranscriptome of Salmonella enterica serovar Typhi within macrophages revealed through the selective capture of transcribed sequences.The host defense peptide beta-defensin 1 confers protection against Bordetella pertussis in newborn piglets.Antimicrobial peptides: therapeutic potential for the treatment of Candida infections.
P2860
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P2860
A PhoP-regulated outer membrane protease of Salmonella enterica serovar typhimurium promotes resistance to alpha-helical antimicrobial peptides.
description
2000 nî lūn-bûn
@nan
2000 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
A PhoP-regulated outer membran ...... elical antimicrobial peptides.
@ast
A PhoP-regulated outer membran ...... elical antimicrobial peptides.
@en
type
label
A PhoP-regulated outer membran ...... elical antimicrobial peptides.
@ast
A PhoP-regulated outer membran ...... elical antimicrobial peptides.
@en
prefLabel
A PhoP-regulated outer membran ...... elical antimicrobial peptides.
@ast
A PhoP-regulated outer membran ...... elical antimicrobial peptides.
@en
P2093
P2860
P921
P1476
A PhoP-regulated outer membran ...... helical antimicrobial peptides
@en
P2093
P2860
P304
P356
10.1128/JB.182.14.4077-4086.2000
P407
P50
P577
2000-07-01T00:00:00Z