Streptococcus pneumoniae sheds syndecan-1 ectodomains through ZmpC, a metalloproteinase virulence factor.
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Surface Proteoglycans as Mediators in Bacterial Pathogens InfectionsA metalloproteinase secreted by Streptococcus pneumoniae removes membrane mucin MUC16 from the epithelial glycocalyx barrierImmunization with a ZmpB-based protein vaccine could protect against pneumococcal diseases in mice.Syndecan-1 promotes Staphylococcus aureus corneal infection by counteracting neutrophil-mediated host defense.Corruption of innate immunity by bacterial proteases.Syndecan-1 in the mouse parietal peritoneum microcirculation in inflammation.2-O-Sulfated Domains in Syndecan-1 Heparan Sulfate Inhibit Neutrophil Cathelicidin and Promote Staphylococcus aureus Corneal InfectionMolecular and cellular mechanisms of ectodomain sheddingRole of glycosaminoglycans in infectious diseaseProteoglycans in host-pathogen interactions: molecular mechanisms and therapeutic implicationsSyndecan-1 (CD138) deficiency increases Staphylococcus aureus infection but has no effect on pathology in a mouse model of peritoneal dialysis.Identification of an atypical zinc metalloproteinase, ZmpC, from an epidemic conjunctivitis-causing strain of Streptococcus pneumoniae.Staphylococcus aureus beta-toxin induces lung injury through syndecan-1.Glycosaminoglycans and infection.Syndecan-1 shedding facilitates the resolution of neutrophilic inflammation by removing sequestered CXC chemokines.Cell surface-anchored syndecan-1 ameliorates intestinal inflammation and neutrophil transmigration in ulcerative colitis.Molecular functions of syndecan-1 in disease.Shedding of cell membrane-bound proteoglycans.Syndecans as modulators and potential pharmacological targets in cancer progression.Streptococcal toxins: role in pathogenesis and disease.Shed syndecan-1 restricts neutrophil elastase from alpha1-antitrypsin in neutrophilic airway inflammation.Syndecan-1 ectodomain shedding is regulated by the small GTPase Rab5Zinc metalloproteinase ZmpC suppresses experimental pneumococcal meningitis by inhibiting bacterial invasion of central nervous systems.Occurrence and evolution of the paralogous zinc metalloproteases IgA1 protease, ZmpB, ZmpC, and ZmpD in Streptococcus pneumoniae and related commensal speciesPneumococcal immune evasion: ZmpC inhibits neutrophil influx.Soluble Syndecan-1: A Novel Biomarker of Small Bowel Mucosal Damage in Children with Celiac Disease.Syndecan-1 and heparanase: potential markers for activity evaluation and differential diagnosis of Crohn's disease.
P2860
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P2860
Streptococcus pneumoniae sheds syndecan-1 ectodomains through ZmpC, a metalloproteinase virulence factor.
description
2006 nî lūn-bûn
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2006年の論文
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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name
Streptococcus pneumoniae sheds ...... loproteinase virulence factor.
@en
Streptococcus pneumoniae sheds ...... loproteinase virulence factor.
@nl
type
label
Streptococcus pneumoniae sheds ...... loproteinase virulence factor.
@en
Streptococcus pneumoniae sheds ...... loproteinase virulence factor.
@nl
prefLabel
Streptococcus pneumoniae sheds ...... loproteinase virulence factor.
@en
Streptococcus pneumoniae sheds ...... loproteinase virulence factor.
@nl
P2093
P2860
P356
P1476
Streptococcus pneumoniae sheds ...... loproteinase virulence factor.
@en
P2093
Allison E Bennett
Atsuko Hayashida
Pyong Woo Park
Susan K Hollingshead
P2860
P304
P356
10.1074/JBC.M608542200
P407
P577
2006-11-10T00:00:00Z