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Induction of group A Streptococcus virulence by a human antimicrobial peptide.

Induction of group A Streptococcus virulence by a human antimicrobial peptide.

http://www.wikidata.org/entity/Q36954965

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Microevolution of group A streptococci in vivo: capturing regulatory networks engaged in sociomicrobiology, niche adaptation, and hypervirulence The group A Streptococcus small regulatory RNA FasX enhances streptokinase activity by increasing the stability of the ska mRNA transcript On the role of NMR spectroscopy for characterization of antimicrobial peptides Cationic antimicrobial peptides promote microbial mutagenesis and pathoadaptation in chronic infections Understanding the regulation of Group B Streptococcal virulence factors Thermoregulation of capsule production by Streptococcus pyogenes Distinct single amino acid replacements in the control of virulence regulator protein differentially impact streptococcal pathogenesis The Abi-domain protein Abx1 interacts with the CovS histidine kinase to control virulence gene expression in group B Streptococcus.A combination of independent transcriptional regulators shapes bacterial virulence gene expression during infection CcpA and LacD.1 affect temporal regulation of Streptococcus pyogenes virulence genes.Clindamycin-induced CovS-mediated regulation of the production of virulent exoproteins streptolysin O, NAD glycohydrolase, and streptokinase in Streptococcus pyogenes.Wiring the streptococcal network for alternative lifestyles Inhibition of Inflammasome-Dependent Interleukin 1β Production by Streptococcal NAD+-Glycohydrolase: Evidence for Extracellular Activity.The 4.5S RNA component of the signal recognition particle is required for group A Streptococcus virulence Two group A streptococcal peptide pheromones act through opposing Rgg regulators to control biofilm development.Signal transduction through CsrRS confers an invasive phenotype in group A Streptococcus.M protein and hyaluronic acid capsule are essential for in vivo selection of covRS mutations characteristic of invasive serotype M1T1 group A Streptococcus.Streptolysin O and NAD-glycohydrolase prevent phagolysosome acidification and promote group A Streptococcus survival in macrophages.A bacterial pathogen co-opts host plasmin to resist killing by cathelicidin antimicrobial peptides Regioselective Benzylation of 2-Deoxy-2-Aminosugars Using Crown Ethers: Application to a Shortened Synthesis of Hyaluronic Acid Oligomers.The human antimicrobial peptide LL-37 binds directly to CsrS, a sensor histidine kinase of group A Streptococcus, to activate expression of virulence factors.Counteractive balancing of transcriptome expression involving CodY and CovRS in Streptococcus pyogenes.Innate immune response to Streptococcus pyogenes depends on the combined activation of TLR13 and TLR2.Peroxide stimulon and role of PerR in group A Streptococcus.Cationic antimicrobial peptide resistance mechanisms of streptococcal pathogens.Vitamin D and the human antimicrobial peptide LL-37 enhance group a streptococcus resistance to killing by human cells A Bioengineered Human Skin Tissue for the Treatment of Infected Wounds.Cationic antimicrobial peptides disrupt the Streptococcus pyogenes ExPortal.Exopolysaccharides of Lactobacillus rhamnosus GG form a protective shield against innate immune factors in the intestine CsrRS regulates group B Streptococcus virulence gene expression in response to environmental pH: a new perspective on vaccine development On the physiology and pathophysiology of antimicrobial peptides.Streptococcus adherence and colonization.Focal targeting by human β-defensin 2 disrupts localized virulence factor assembly sites in Enterococcus faecalis.SpxA1 and SpxA2 Act Coordinately To Fine-Tune Stress Responses and Virulence in Streptococcus pyogenes Adaptation factors of the probiotic Lactobacillus rhamnosus GG.Antimicrobial peptides and their potential application in inflammation and sepsis Bacterial Mg2+ homeostasis, transport, and virulence.RocA Is an Accessory Protein to the Virulence-Regulating CovRS Two-Component System in Group A Streptococcus.Use of a Phosphorylation Site Mutant To Identify Distinct Modes of Gene Repression by the Control of Virulence Regulator (CovR) in Streptococcus pyogenes.Regulatory gene mutation: a driving force behind group a Streptococcus strain- and serotype-specific variation.

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P2860

Induction of group A Streptococcus virulence by a human antimicrobial peptide.

http://www.wikidata.org/entity/Q36954965

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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2008年论文

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name

Induction of group A Streptococcus virulence by a human antimicrobial peptide.

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type

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Induction of group A Streptococcus virulence by a human antimicrobial peptide.

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prefLabel

Induction of group A Streptococcus virulence by a human antimicrobial peptide.

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Proceedings of the National Academy of Sciences of the United States of America

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Induction of group A Streptococcus virulence by a human antimicrobial peptide.

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P2093

Hachung Chung

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Hien J Tran-Winkler

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Ioannis Gryllos

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Michael R Wessels

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Ming-Fang Cheng

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Robert Bolcome

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Robert I Lehrer

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Wuyuan Lu

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P2860

Hyaluronic acid capsule is a virulence factor for mucoid group A streptococci

C5a peptidase alters clearance and trafficking of group A streptococci by infected mice

A streptococcal protease that degrades CXC chemokines and impairs bacterial clearance from infected tissues

Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human beta-defensin 3

Genome-wide analysis of group a streptococci reveals a mutation that modulates global phenotype and disease specificity.

Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides

Cathelicidins: a family of endogenous antimicrobial peptides

Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse

IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G.

Salivary antimicrobial peptide expression and dental caries experience in children

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