Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutations of factor H impair regulation of surface-bound C3b by three mechanisms in atypical hemolytic uremic syndrome.

The Journal of biological chemistry - 5 Jun 2009

Lehtinen Markus J, Rops Angelique L, Isenman David E, van der Vlag Johan, Jokiranta T Sakari

Abstract excerpt

Atypical hemolytic uremic syndrome (aHUS) is a thrombotic microangiopathy associated with mutations in complement proteins, most frequently in the main plasma alternative pathway regulator factor H (FH). The hotspot for the FH mutations is in domains 19-20 (FH19-20) that are indispensable for FH activity on C3b bound covalently to host cells. In aHUS, down-regulation of cell-bound C3b by FH is impaired, but it is...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Complement C3b
Share to Complement Factor H

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endothelial Cells

Share to Hemolytic-Uremic Syndrome

Share to Inflammation

Share to Kidney Glomerulus

Share to Mutagenesis

Share to Point Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 19351878
DOI: 10.1074/jbc.M900814200
PMCID: PMC2708861

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations of factor H impair regulation of surface-bound C3b by three mechanisms in atypical hemolytic uremic syndrome.PMID 19351878Read ↗

Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome.Semantic proximity Read ↗

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

Mutations in Complement Factor H Impair Alternative Pathway Regulation on Mouse Glomerular Endothelial Cells in Vitro.Semantic proximity Read ↗

Both domain 19 and domain 20 of factor H are involved in binding to complement C3b and C3d.Semantic proximity Read ↗

Dual interaction of factor H with C3d and glycosaminoglycans in host–nonhost discrimination by complementSemantic proximity Read ↗

Factor H and atypical hemolytic uremic syndrome: mutations in the C-terminus cause structural changes and defective recognition functions.Semantic proximity Read ↗

Structural and functional characterization of the product of disease-related factor H gene conversion.Semantic proximity Read ↗

Overall Neutralization of Complement Factor H by Autoantibodies in the Acute Phase of the Autoimmune Form of Atypical Hemolytic Uremic SyndromeSemantic proximity Read ↗

A prevalent C3 mutation in aHUS patients causes a direct C3 convertase gain of functionSemantic proximity Read ↗

Factor H dysfunction in patients with atypical hemolytic uremic syndrome contributes to complement deposition on platelets and their activation.Semantic proximity Read ↗

The major autoantibody epitope on factor H in atypical hemolytic uremic syndrome is structurally different from its homologous site in factor H-related protein 1, supporting a novel model for induction of autoimmunity in this disease.Semantic proximity Read ↗

Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.