A revised mechanism for the activation of complement C3 to C3b: a molecular explanation of a disease-associated polymorphism.
Rodriguez, Elizabeth; Nan, Ruodan; Li, Keying; Gor, Jayesh; Perkins, Stephen J.
J Biol Chem
; 290(4): 2334-50, 2015 Jan 23.
Artigo em Inglês | MEDLINE | ID: mdl-25488663
Self-association and domain rearrangements between complement C3 and C3u provide insight into the activation mechanism of C3.
Crystallography: crystallographic evidence for deviating C3b structure.
Diversity in the C3b [corrected] contact residues and tertiary structures of the staphylococcal complement inhibitor (SCIN) protein family.
Structure of C3b in complex with CRIg gives insights into regulation of complement activation.
Structures of complement component C3 provide insights into the function and evolution of immunity.
Intracellular complement activation sustains T cell homeostasis and mediates effector differentiation.
Structural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitor.
Experimental confirmation of the C3 tickover hypothesis by studies with an Ab (S77) that inhibits tickover in whole serum.
Structural biology: origins of chemical biodefence.
Complement activation by heme as a secondary hit for atypical hemolytic uremic syndrome.