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Publikationer (hämtat ur Lunds universitets publikationsdatabas)
- Binding of complement inhibitor C4b-binding protein to a highly virulent S. pyogenes M1 strain is mediated by protein H and enhances adhesion to and invasion of endothelial cells.
- Gram-positive anaerobic cocci - commensals and opportunistic pathogens.
- Surface proteins of the Group G Streptococcus in different phases of growth: patterns of production and implications for the host-bacteria relationship.
- Activation of the contact system at the surface of Fusobacterium necrophorum: a possible virulence mechanism in Lemierre's syndrome.
- Antibacterial activity of the contact and complement systems is blocked by SIC, a protein secreted by Streptococcus pyogenes.
- Binding of albumin promotes bacterial survival at the epithelial surface.
- Constitutive and Inflammation-Dependent Antimicrobial Peptides Produced by Epithelium Are Differentially Processed and Inactivated by the Commensal Finegoldia magna and the Pathogen Streptococcus pyogenes.
- Interaction of Bacteroides fragilis and Bacteroides thetaiotaomicron with the kallikrein-kinin system
- Interaction of Bacteroides spp. with the kallikrein-kinin system.
- Group G streptococcal IgG binding molecules FOG and protein G have different impacts on opsonization by C1q
- Identification of a streptococcal octapeptide motif involved in acute rheumatic fever
- M1 protein of Streptococcus pyogenes increases production of the antibacterial CXC chemokine MIG/CXCL9 in pharyngeal epithelial cells
- Protein FOG is a moderate inducer of MIG/CXCL9, and group G streptococci are more tolerant than group A streptococci to this chemokine's antibacterial effect
- SufA--a novel subtilisin-like serine proteinase of Finegoldia magna.
- The CXC Chemokine MIG/CXCL9 Is Important in Innate Immunity against Streptococcus pyogenes.
- The dual role of the contact system in bacterial infectious disease
- Evolutionary and functional studies of protein H: a surface molecule of Streptococcus pyogenes
- Helicobacter pylori adhesin binding fucosylated histo-blood group antigens revealed by retagging
- Size-selectivity of the glomerular barrier to high molecular weight proteins: upper size limitations of shunt pathways