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Article

The binding of factor H to a complex of physiological polyanions and C3b on cells is impaired in atypical hemolytic uremic syndrome.

Journal of immunology (Baltimore, Md. : 1950) - 1 Jun 2009

Ferreira Viviana P, Herbert Andrew P, Cortés Claudio, McKee Kristi A, Blaum Bärbel S, Esswein Stefan T, Uhrín Dusan, Barlow Paul N, Pangburn Michael K, Kavanagh David

Abstract excerpt

Factor H (fH) is essential for complement homeostasis in fluid-phase and on surfaces. Its two C-terminal domains (CCP 19-20) anchor fH to self-surfaces where it prevents C3b amplification in a process requiring its N-terminal four domains. In atypical hemolytic uremic syndrome (aHUS), mutations clustering toward the C terminus of fH may disrupt interactions with surface-associated C3b or polyanions and thereby...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19454698
DOI: 10.4049/jimmunol.0804031
PMCID: PMC2696619

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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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.PMID 19454698Read ↗

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