Evidence map›Paper›PMID 26192331›Full record

ArticleNature structural & molecular biology2015

Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation.

Gesa Volkers, Liam J Worrall, David H Kwan, Ching-Ching Yu, Lars Baumann, Emilie Lameignere, Gregory A Wasney, Nichollas E Scott, Warren Wakarchuk, Leonard J Foster and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

39 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Polysialic Acid in the Immune System.Frontiers in immunology · 2021
    Review
  16. Review
  17. Article
  18. Article
  19. Vertebrate Alpha2,8-Sialyltransferases (ST8Sia): A Teleost Perspective.International journal of molecular sciences · 2020
    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

12 authors at 2 institutions in 1 country.

Gesa Volkers1] Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
Liam J Worrall1] Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
David H Kwan1] Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for High-Throughput Biology, University of British Columbia, Vancouver, British Columbia, Canada.
Ching-Ching Yu1] Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for High-Throughput Biology, University of British Columbia, Vancouver, British Columbia, Canada.
Lars Baumann1] Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for High-Throughput Biology, University of British Columbia, Vancouver, British Columbia, Canada.
Emilie Lameignere1] Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
Gregory A Wasney1] Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
Nichollas E Scott1] Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for High-Throughput Biology, University of British Columbia, Vancouver, British Columbia, Canada.
Warren WakarchukDepartment of Chemistry and Biology, Ryerson University, Toronto, Ontario, Canada.
Leonard J Foster1] Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for High-Throughput Biology, University of British Columbia, Vancouver, British Columbia, Canada.
Stephen G Withers1] Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for High-Throughput Biology, University of British Columbia, Vancouver, British Columbia, Canada.
Natalie C J Strynadka1] Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada. [2] Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
University of British Columbia · CAToronto Metropolitan University · CA

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI ALVAREZ, RICHARD · 2001 to 2010
$80.3M
Protein-Glycan Interaction Resource of the CFGR24GM098791 · NIGMS · EMORY UNIVERSITY · PI CUMMINGS, RICHARD D, PAULSON, JAMES C · 2011 to 2013
$2.6M
Canadian Institutes of Health ResearchNIGMS NIH HHS GM098791NIGMS NIH HHS GM62116
6 · The paper itself

Abstract

Sialyltransferases of the mammalian ST8Sia family catalyze oligo- and polysialylation of surface-localized glycoproteins and glycolipids through transfer of sialic acids from CMP-sialic acid to the nonreducing ends of sialic acid acceptors. The crystal structure of human ST8SiaIII at 1.85-Å resolution presented here is, to our knowledge, the first solved structure of a polysialyltransferase from any species, and it reveals a cluster of polysialyltransferase-specific structural motifs that collectively provide an extended electropositive surface groove for binding of oligo-polysialic acid chain products. The ternary complex of ST8SiaIII with a donor sugar analog and a sulfated glycan acceptor identified with a sialyltransferase glycan array provides insight into the residues involved in substrate binding, specificity and sialyl transfer.

Indexed as

Protein Structure, TertiaryAmino Acid SequenceAnimalsBinding SitesCells, CulturedChromatography, Thin LayerCrystallography, X-RayElectrophoresis, Polyacrylamide GelGlycosylationHumansKineticsMass SpectrometryModels, MolecularMolecular Sequence DataMutationNeural Cell Adhesion MoleculesNeural Cell Adhesion MoleculesPolysaccharidespolysialic acidRecombinant ProteinsSia(alpha2,3)Gal(beta1,4)GlcNAc alpha-2,8-sialyltransferaseSialic AcidsSialyltransferases

Identifiers

PMID26192331
OpenAlexW2203239155

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.