Evidence map›Paper›PMID 21317894›Full record

ArticleNature structural & molecular biology2011

Structural basis for engagement by complement factor H of C3b on a self surface.

Hugh P Morgan, Christoph Q Schmidt, Mara Guariento, Bärbel S Blaum, Dominic Gillespie, Andrew P Herbert, David Kavanagh, Haydyn D T Mertens, Dmitri I Svergun, Conny M Johansson and 3 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

137 citing papers in PubMed, 238 citations in OpenAlex.

  1. Clinical Manifestation of Patients With Atypical Hemolytic Uremic Syndrome With the C3 p.I1157T Variation in the Kinki Region of Japan.Clinical and applied thrombosis/hemostasis : official journal of the International Academy of Clinical and Applied Thrombosis/Hemostasis · 2018
    Trial
  2. Association of Complement Genetics with Outcomes in IgA Nephropathy.Clinical journal of the American Society of Nephrology : CJASN · 2026
    Article
  3. Article
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  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Unveiling the impact ofInfection and immunity · 2024
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. The human factor H protein family - an update.Frontiers in immunology · 2024
    Review
  17. Article
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 2 countries.

Hugh P MorganInstitute of Structural and Molecular Biology, School of Biological Sciences, King's Buildings, University of Edinburgh, Edinburgh, UK.
Christoph Q Schmidt
Mara Guariento
Bärbel S Blaum
Dominic Gillespie
Andrew P Herbert
David Kavanagh
Haydyn D T Mertens
Dmitri I Svergun
Conny M Johansson
Dušan Uhrín
Paul N Barlow
Jonathan P Hannan
University of Edinburgh · GBEuropean Molecular Biology Laboratory · DEInstitute of Structural and Molecular Biology · GBNewcastle University · GBUniversity of Liverpool · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G0001089Wellcome Trust 078780/Z/05/ZWellcome Trust 081179
6 · The paper itself

Abstract

Complement factor H (FH) attenuates C3b molecules tethered by their thioester domains to self surfaces and thereby protects host tissues. Factor H is a cofactor for initial C3b proteolysis that ultimately yields a surface-attached fragment (C3d) corresponding to the thioester domain. We used NMR and X-ray crystallography to study the C3d-FH19-20 complex in atomic detail and identify glycosaminoglycan-binding residues in factor H module 20 of the C3d-FH19-20 complex. Mutagenesis justified the merging of the C3d-FH19-20 structure with an existing C3b-FH1-4 crystal structure. We concatenated the merged structure with the available FH6-8 crystal structure and new SAXS-derived FH1-4, FH8-15 and FH15-19 envelopes. The combined data are consistent with a bent-back factor H molecule that binds through its termini to two sites on one C3b molecule and simultaneously to adjacent polyanionic host-surface markers.

Indexed as

Binding SitesComplement C3bComplement Factor HCrystallography, X-RayModels, MolecularMutagenesisNuclear Magnetic Resonance, BiomolecularProtein ConformationComplement C3bComplement Factor H

Identifiers

PMID21317894
PMCPMC3512577
OpenAlexW2042777883

What OpenQuestion holds

Textmetadata
LicenceTDM
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.