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
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Title
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
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 289, Issue 7, Pages 4295-4306
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2013-12-17
DOI
10.1074/jbc.m113.527416
References
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- (2011) T. Kajander et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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- (2010) Michael J. Duryee et al. FREE RADICAL BIOLOGY AND MEDICINE
- Modifying Apolipoprotein A-I by Malondialdehyde, but Not by an Array of Other Reactive Carbonyls, Blocks Cholesterol Efflux by the ABCA1 Pathway
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- Mutations of Factor H Impair Regulation of Surface-bound C3b by Three Mechanisms in Atypical Hemolytic Uremic Syndrome
- (2009) Markus J. Lehtinen et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Annexin-II, DNA, and Histones Serve as Factor H Ligands on the Surface of Apoptotic Cells
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- The Binding of Factor H to a Complex of Physiological Polyanions and C3b on Cells Is Impaired in Atypical Hemolytic Uremic Syndrome
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- Site-specific modification of positively-charged surfaces on human serum albumin by malondialdehyde
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