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

Structural and functional characterization of the product of disease-related factor H gene conversion.

Biochemistry - 6 Mar 2012

Herbert Andrew P, Kavanagh David, Johansson Conny, Morgan Hugh P, Blaum Bärbel S, Hannan Jonathan P, Barlow Paul N, Uhrín Dušan

Abstract excerpt

Numerous complement factor H (FH) mutations predispose patients to atypical hemolytic uremic syndrome (aHUS) and other disorders arising from inadequately regulated complement activation. No unifying structural or mechanistic consequences have been ascribed to these mutants beyond impaired self-cell protection. The S1191L and V1197A mutations toward the C-terminus of FH, which occur in patients singly or...

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 Crystallography, X-Ray

Share to Gene Conversion

Share to Pichia

Share to Recombinant Proteins

Share to Structure-Activity Relationship

Share to Temperature

Source

Identifiers

PMID: 22320225
DOI: 10.1021/bi201689j

Genes

CFH
CFHR1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and functional characterization of the product of disease-related factor H gene conversion.PMID 22320225Read ↗

Structural Analysis of the C-Terminal Region (Modules 18–20) of Complement Regulator Factor H (FH)Semantic proximity Read ↗

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

Crystallographic determination of the disease-associated T1184R variant of complement regulator factor H.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 ↗

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

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

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

Disease-linked mutations in factor H reveal pivotal role of cofactor activity in self-surface-selective regulation of complement activation.Semantic proximity Read ↗

Factor H family proteins: on complement, microbes and human diseases.Semantic proximity Read ↗

Functional Anatomy of Complement Factor HSemantic 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 ↗

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

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