Evidence map›Paper›PMID 19025119›Full record

ReviewAdvances in experimental medicine and biology2008

Complement factor H: using atomic resolution structure to illuminate disease mechanisms.

Paul N Barlow, Gregory S Hageman, Susan M Lea

Abstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
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

3 authors.

Paul N BarlowSchool of Chemistry and Biological Sciences, Joseph Black Chemistry Building, University of Edinburgh, Edinburgh EH9 2PB, UK. Paul.Barlow@ed.ac.uk
Gregory S Hageman
Susan M Lea

Funding

AGE-RELATED MACULOPATHY: CELLULAR AND MOLECULAR ANALYSESR01EY011515 · NEI · UNIVERSITY OF IOWA · PI HAGEMAN, GREGORY S · 1996 to 2005
$3.2M
Medical Research Council G0001089NEI NIH HHS R01 EY011515
6 · The paper itself

Abstract

Complement Factor H has recently come to the fore with variant forms implicated in a range of serious disease states. This review aims to bring together recent data concerning the structure and biological activity of this molecule to highlight the way in which a molecular understanding of function may open novel therapeutic possibilities. In particular we examine the evidence for and against the hypothesis that sequence variations in factor H may predispose to disease if they perturb its ability to recognise and respond appropriately to polyanionic carbohydrates on host surfaces that require protection from complement-mediated damage.

Indexed as

Binding SitesComplement Factor HCrystallography, X-RayGlomerulonephritis, MembranoproliferativeHemolytic-Uremic SyndromeHumansMacular DegenerationModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsScattering, Small AngleStatic ElectricityComplement Factor HRecombinant Proteins

Identifiers

PMID19025119
PMCPMC4863441

What OpenQuestion holds

Textmetadata
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.