Evidence map›Paper›PMID 22389686›Full record

ArticlePloS one2012

Structural analysis of the C-terminal region (modules 18-20) of complement regulator factor H (FH).

Hugh P Morgan, Haydyn D T Mertens, Mara Guariento, Christoph Q Schmidt, Dinesh C Soares, Dmitri I Svergun, Andrew P Herbert, Paul N Barlow, Jonathan P Hannan

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

24 citing papers in PubMed, 51 citations in OpenAlex.

  1. Phylogenetic Analysis and Structural Evaluation ofbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Deleterious Impact of a NovelFrontiers in genetics · 2019
    Article
  12. An Engineered Complement Factor H Construct for Treatment of C3 Glomerulopathy.Journal of the American Society of Nephrology : JASN · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Complement factor H in host defense and immune evasion.Cellular and molecular life sciences : CMLS · 2017
    Review
  17. Article
  18. Article
  19. Article
  20. 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

9 authors at 3 institutions in 2 countries.

Hugh P MorganInstitute of Structural and Molecular Biology, School of Biological Sciences, King's Buildings, University of Edinburgh, Edinburgh, United Kingdom.
Haydyn D T Mertens
Mara Guariento
Christoph Q Schmidt
Dinesh C Soares
Dmitri I Svergun
Andrew P Herbert
Paul N Barlow
Jonathan P Hannan
University of Edinburgh · GBEuropean Molecular Biology Laboratory · DEWestern General Hospital · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G0001089Wellcome TrustWellcome Trust 073131Wellcome Trust 088179
6 · The paper itself

Abstract

Factor H (FH) is a soluble regulator of the human complement system affording protection to host tissues. It selectively inhibits amplification of C3b, the activation-specific fragment of the abundant complement component C3, in fluid phase and on self-surfaces and accelerates the decay of the alternative pathway C3 convertase, C3bBb. We have determined the crystal structure of the three carboxyl-terminal complement control protein (CCP) modules of FH (FH18-20) that bind to C3b, and which additionally recognize polyanionic markers specific to self-surfaces. These CCPs harbour nearly 30 disease-linked missense mutations. We have also deployed small-angle X-ray scattering (SAXS) to investigate FH18-20 flexibility in solution using FH18-20 and FH19-20 constructs. In the crystal lattice FH18-20 adopts a "J"-shape: A ~122-degree tilt between the structurally highly similar modules 18 and 19 precedes an extended, linear arrangement of modules 19 and 20 as observed in previously determined structures of these two modules alone. However, under solution conditions FH18-20 adopts multiple conformations mediated by flexibility between CCPs 18 and 19. We also pinpoint the locations of disease-associated missense mutations on the module 18 surface and discuss our data in the context of the C3b:FH interaction.

Indexed as

Complement Factor HCrystallography, X-RayHumansProtein Structure, SecondaryScattering, Small AngleComplement Factor H

Identifiers

PMID22389686
PMCPMC3289644
OpenAlexW2052521611

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.