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Factor H binding and function in sialylated pathogenic neisseriae is influenced by gonococcal, but not meningococcal, porin.
Properdin is critical for antibody-dependent bactericidal activity against Neisseria gonorrhoeae that recruit C4b-binding protein.
Enhanced factor H binding to sialylated Gonococci is restricted to the sialylated lacto-N-neotetraose lipooligosaccharide species: implications for serum resistance and evidence for a bifunctional lipooligosaccharide sialyltransferase in Gonococci.
Human factor H interacts selectively with Neisseria gonorrhoeae and results in species-specific complement evasion.
Species-specificity of Neisseria gonorrhoeae infection: do human complement regulators contribute?
Factor H facilitates adherence of Neisseria gonorrhoeae to complement receptor 3 on eukaryotic cells.
Complement Factor H
A Novel Factor H-Fc Chimeric Immunotherapeutic Molecule against Neisseria gonorrhoeae.
Utilizing complement evasion strategies to design complement-based antibacterial immunotherapeutics: Lessons from the pathogenic Neisseriae.
Gonococcal lipooligosaccharide sialylation: virulence factor and target for novel immunotherapeutics.
Human Factor H Domains 6 and 7 Fused to IgG1 Fc Are Immunotherapeutic against Neisseria gonorrhoeae.
Complement alone drives efficacy of a chimeric antigonococcal monoclonal antibody.
Therapeutic CMP-Nonulosonates against Multidrug-Resistant Neisseria gonorrhoeae.
Development of Complement Factor H-Based Immunotherapeutic Molecules in Tobacco Plants Against Multidrug-Resistant Neisseria gonorrhoeae.
An optimized Factor H-Fc fusion protein against multidrug-resistant Neisseria gonorrhoeae.