Research Center Borstel - Leibniz-Center for Medicine and Biosciences-ko ikertzaileekin lankidetzan egindako argitalpenak (11)

2011

  1. Biophysical mechanisms of endotoxin neutralization by cationic amphiphilic peptides

    Biophysical Journal, Vol. 100, Núm. 11, pp. 2652-2661

  2. Structural features governing the activity of lactoferricin-derived peptides that act in synergy with antibiotics against Pseudomonas aeruginosa in vitro and in vivo

    Antimicrobial Agents and Chemotherapy, Vol. 55, Núm. 1, pp. 218-228

2010

  1. Physicochemical and biological characterization of anti-endotoxin peptides and their influence on lipid properties

    Protein and Peptide Letters, Vol. 17, Núm. 11, pp. 1328-1333

  2. Structural prerequisites for endotoxic activity in the Limulus test as compared to cytokine production in mononuclear cells

    Innate Immunity, Vol. 16, Núm. 1, pp. 39-47

2008

  1. Comparative analysis of selected methods for the assessment of antimicrobial and membrane-permeabilizing activity: A case study for lactoferricin derived peptides

    BMC Microbiology, Vol. 8

2007

  1. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against gram-negative pathogens

    Journal of Biological Chemistry, Vol. 282, Núm. 20, pp. 14719-14728

  2. Thermodynamic analysis of the lipopolysaccharide-dependent resistance of Gram-negative bacteria against polymyxin B

    Biophysical Journal, Vol. 92, Núm. 8, pp. 2796-2805

2005

  1. The lipopolysaccharide of Brucella abortus BvrS/BvrR mutants contains lipid A modifications and has higher affinity for bactericidal cationic peptides

    Journal of Bacteriology, Vol. 187, Núm. 16, pp. 5631-5639

2003

  1. Pathogenic Yersinia enterocolitica strains increase the outer membrane permeability in response to environmental stimuli by modulating lipopolysaccharide fluidity and lipid A structure

    Infection and Immunity, Vol. 71, Núm. 4, pp. 2014-2021

2002

  1. Biophysical investigations into the interaction of lipopolysaccharide with polymyxins

    Thermochimica Acta

2000

  1. Brucella abortus and its closest phylogenetic relative, Ochrobactrum spp., differ in outer membrane permeability and cationic peptide resistance

    Infection and Immunity, Vol. 68, Núm. 6, pp. 3210-3218