Recognition of malondialdehyde-modified proteins by the c terminus of complement factor h is mediated via the polyanion binding site and impaired by mutations found in atypical hemolytic uremic syndrome

Journal of Biological Chemistry

Volumn 289, Issue 7, 2014, Pages 4295-4306

  Hyvärinen, Satu ^a   Uchida, Koji ^b   Varjosalo, Markku ^c   Jokela, Reija ^d   Jokiranta, T Sakari ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

^b NAGOYA UNIVERSITY   (Japan)

^c UNIVERSITY OF HELSINKI   (Finland)

^d AALTO UNIVERSITY   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

AHUS; CFH; COMPLEMENT SYSTEM; INNATE IMMUNITY; MALONDIALDEHYDE; OXIDATIVE STRESS; PATHOGENESIS; PROTEIN CHEMICAL MODIFICATION; SURFACE RECOGNITION; THROMBOTIC MICROANGIOPATHY;

AMINES; ANIMALS; BINDING SITES; CATTLE; COMPLEMENT ACTIVATION; COMPLEMENT FACTOR H; HEMOLYTIC-UREMIC SYNDROME; HUMANS; MALONDIALDEHYDE; MUTATION; OXIDATIVE STRESS; PROTEIN PROCESSING, POST-TRANSLATIONAL; SERUM ALBUMIN, BOVINE;

EID: 84894207926     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.527416     Document Type: Article

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