Multimeric Interactions between Complement Factor H and Its C3d Ligand Provide New Insight on Complement Regulation

Journal of Molecular Biology

Volumn 391, Issue 1, 2009, Pages 119-135

  Okemefuna, Azubuike I ^a   Li, Keying ^a   Nan, Ruodan ^a   Ormsby, Rebecca J ^b   Sadlon, Tania ^b   Gordon, David L ^b   Perkins, Stephen J ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b FLINDERS UNIVERSITY   (Australia)

Author keywords

analytical ultracentrifugation; C3d; factor H; surface plasmon resonance; X ray scattering

Indexed keywords

COMPLEMENT COMPONENT C3B; COMPLEMENT COMPONENT C3D; COMPLEMENT FACTOR H; SODIUM CHLORIDE;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELL SURFACE; COMPLEMENT ACTIVATION; COMPLEMENT ALTERNATIVE PATHWAY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DISSOCIATION CONSTANT; HOST CELL; MOLECULAR MODEL; NONHUMAN; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; RADIATION SCATTERING; SIGNAL TRANSDUCTION; STOICHIOMETRY; SURFACE PLASMON RESONANCE; ULTRACENTRIFUGATION;

EID: 67651087153     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.06.013     Document Type: Article

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