Evidence map›Paper›PMID 17893204›Full record

ArticleThe Journal of experimental medicine2007

Structural basis for complement factor H linked age-related macular degeneration.

Beverly E Prosser, Steven Johnson, Pietro Roversi, Andrew P Herbert, Bärbel S Blaum, Jess Tyrrell, Thomas A Jowitt, Simon J Clark, Edward Tarelli, Dusan Uhrín and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
17.4field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

109 citing papers in PubMed, 184 citations in OpenAlex.

  1. Evidence for the Pathogenicity of aMedicina (Kaunas, Lithuania) · 2025
    Article
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  12. Article
  13. The complement system in age-related macular degeneration.Cellular and molecular life sciences : CMLS · 2021
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. A genome-wide association study identifies key modulators of complement factor H binding to malondialdehyde-epitopes.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article

49 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors at 4 institutions in 1 country.

Beverly E ProsserSir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, England, UK.
Steven Johnson
Pietro Roversi
Andrew P Herbert
Bärbel S Blaum
Jess Tyrrell
Thomas A Jowitt
Simon J Clark
Edward Tarelli
Dusan Uhrín
Paul N Barlow
Robert B Sim
Anthony J Day
Susan M Lea
University of Edinburgh · GBWellcome Centre for Cell-Matrix Research · GBUniversity of Oxford · GBSt George's, University of London · GB

Funding

Medical Research Council G0001089Medical Research Council G0400389Medical Research Council G0400775Medical Research Council MC_U138274352Wellcome Trust 075415/z/04/zWellcome Trust 078780Wellcome Trust 078780/z/05/z
6 · The paper itself

Abstract

Nearly 50 million people worldwide suffer from age-related macular degeneration (AMD), which causes severe loss of central vision. A single-nucleotide polymorphism in the gene for the complement regulator factor H (FH), which causes a Tyr-to-His substitution at position 402, is linked to approximately 50% of attributable risks for AMD. We present the crystal structure of the region of FH containing the polymorphic amino acid His402 in complex with an analogue of the glycosaminoglycans (GAGs) that localize the complement regulator on the cell surface. The structure demonstrates direct coordination of ligand by the disease-associated polymorphic residue, providing a molecular explanation of the genetic observation. This glycan-binding site occupies the center of an extended interaction groove on the regulator's surface, implying multivalent binding of sulfated GAGs. This finding is confirmed by structure-based site-directed mutagenesis, nuclear magnetic resonance-monitored binding experiments performed for both H402 and Y402 variants with this and another model GAG, and analysis of an extended GAG-FH complex.

Indexed as

AgingBinding SitesComplement Factor HCrystallography, X-RayGene Products, gagLigandsModels, MolecularMutationPolysaccharidesProtein Structure, QuaternaryProtein Structure, TertiarySucroseSurface PropertiesComplement Factor HGene Products, gagLigandsPolysaccharidesSucrosesucrose octasulfate

Identifiers

PMID17893204
PMCPMC2118454
OpenAlexW2138610380

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.