OmpT Outer Membrane Proteases of Enterohemorrhagic and Enteropathogenic Escherichia coli Contribute Differently to the Degradation of Human LL-37

Paneth cells, antimicrobial peptides and maintenance of intestinal homeostasis

(2011) Charles L. Bevins et al.   NATURE REVIEWS MICROBIOLOGY

The Omptins of Yersinia pestis and Salmonella enterica Cleave the Reactive Center Loop of Plasminogen Activator Inhibitor 1

(2010) J. Haiko et al.   JOURNAL OF BACTERIOLOGY

An Active Site Water Network in the Plasminogen Activator Pla from Yersinia pestis

(2010) Elif Eren et al.   STRUCTURE

Uropathogenic Escherichia coli Modulates Immune Responses and Its Curli Fimbriae Interact with the Antimicrobial Peptide LL-37

(2010) Ylva Kai-Larsen et al.   PLoS Pathogens

Invited review: Breaking barriers — attack on innate immune defences by omptin surface proteases of enterobacterial pathogens

(2009) Johanna Haiko et al.   Innate Immunity

Inhibition of cathelicidin activity by bacterial exopolysaccharides

(2009) Michela Foschiatti et al.   MOLECULAR MICROBIOLOGY

An outer membrane protease of the omptin family prevents activation of theCitrobacter rodentiumPhoPQ two-component system by antimicrobial peptides

(2009) Valerie Le Sage et al.   MOLECULAR MICROBIOLOGY

The chemistry and biology of LL-37

(2009) Matthew F. Burton et al.   NATURAL PRODUCT REPORTS

The roles of cathelicidin LL-37 in immune defences and novel clinical applications

(2008) Anastasia Nijnik et al.   CURRENT OPINION IN HEMATOLOGY

Capsular Antigen Fraction 1 and Pla Modulate the Susceptibility of Yersinia pestis to Pulmonary Antimicrobial Peptides Such as Cathelicidin

(2008) E. M. Galvan et al.   INFECTION AND IMMUNITY

Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances

(2008) Irith Wiegand et al.   Nature Protocols