Evidence map›Paper›PMID 25402769›Full record

ArticleNature chemical biology2015

Structural basis for sialic acid-mediated self-recognition by complement factor H.

Bärbel S Blaum, Jonathan P Hannan, Andrew P Herbert, David Kavanagh, Dušan Uhrín, Thilo Stehle

Abstract read
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In one paragraph

Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 164 papers.

0numbers the graph read from it
0cells of the map it votes in
164citing papers in PubMed
11.5field-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

164 citing papers in PubMed, 272 citations in OpenAlex.

  1. Glycosylation of the retina.Biochemical Society transactions · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Association of Complement Genetics with Outcomes in IgA Nephropathy.Clinical journal of the American Society of Nephrology : CJASN · 2026
    Article
  7. Review
  8. Review
  9. Sialylation in the nervous system: Functions and mechanisms.The Journal of biological chemistry · 2026
    Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Sialidases derived frombioRxiv : the preprint server for biology · 2025
    Article
  20. Review

104 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

6 authors at 5 institutions in 3 countries.

Bärbel S BlaumInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
Jonathan P HannanDepartment of Medicine, University of Colorado School of Medicine, Aurora, Colorado, USA.
Andrew P HerbertThe School of Chemistry, University of Edinburgh, Scotland, UK.
David KavanaghInstitute of Genetic Medicine, International Centre for Life, Newcastle upon Tyne, UK.
Dušan UhrínThe School of Chemistry, University of Edinburgh, Scotland, UK.
Thilo Stehle1] Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany. [2] Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, Tennessee, USA.
University of Edinburgh · GBCentre for Life · GBUniversity of Colorado Denver · USUniversity of Tübingen · DEVanderbilt University · US

Funding

Wellcome Trust
6 · The paper itself

Abstract

The serum protein complement factor H (FH) ensures downregulation of the complement alternative pathway, a branch of innate immunity, upon interaction with specific glycans on host cell surfaces. Using ligand-based NMR, we screened a comprehensive set of sialylated glycans for binding to FH and solved the crystal structure of a ternary complex formed by the two C-terminal domains of FH, a sialylated trisaccharide and the complement C3b thioester-containing domain. Key residues in the sialic acid binding site are conserved from mice to men, and residues linked to atypical hemolytic uremic syndrome cluster within this binding site, suggesting a possible role for sialic acid as a host marker also in other mammals and a critical role in human renal complement homeostasis. Unexpectedly, the FH sialic acid binding site is structurally homologous to the binding sites of two evolutionarily unrelated proteins. The crystal structure also advances our understanding of bacterial immune evasion strategies.

Indexed as

AnimalsBinding SitesCarbohydrate SequenceComplement C3bComplement Factor HComplement Pathway, AlternativeConserved SequenceHemolysisHemolytic-Uremic SyndromeHumansMiceModels, MolecularMolecular Sequence DataN-Acetylneuraminic AcidPolysaccharidesSheepComplement C3bComplement Factor HN-Acetylneuraminic AcidPolysaccharides

Identifiers

PMID25402769
OpenAlexW2135400491

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.