Zinc-induced self-association of complement C3b and Factor H: implications for inflammation and age-related macular degeneration.
Nan, Ruodan; Tetchner, Stuart; Rodriguez, Elizabeth; Pao, Po-Jung; Gor, Jayesh; Lengyel, Imre; Perkins, Stephen J.
J Biol Chem
; 288(26): 19197-210, 2013 Jun 28.
Artigo em Inglês | MEDLINE | ID: mdl-23661701
The disease-protective complement factor H allotypic variant Ile62 shows increased binding affinity for C3b and enhanced cofactor activity.
Structure of complement fragment C3b-factor H and implications for host protection by complement regulators.
Interaction of uromodulin and complement factor H enhances C3b inactivation.
A novel factor I activity in Nipah virus inhibits human complement pathways through cleavage of C3b.
Bisretinoid-mediated complement activation on retinal pigment epithelial cells is dependent on complement factor H haplotype.
Whole-exome sequencing identifies rare, functional CFH variants in families with macular degeneration.
Disease-associated N-terminal complement factor H mutations perturb cofactor and decay-accelerating activities.
The binding of factor H to a complex of physiological polyanions and C3b on cells is impaired in atypical hemolytic uremic syndrome.
Crystallography: crystallographic evidence for deviating C3b structure.
Disturbed sialic acid recognition on endothelial cells and platelets in complement attack causes atypical hemolytic uremic syndrome.