Evidence map›Paper›PMID 24727899›Full record

ArticleNature chemical biology2014

Engineering the product profile of a polysialyltransferase.

Timothy G Keys, Hazel L S Fuchs, Jörg Ehrit, Jürgen Alves, Friedrich Freiberger, Rita Gerardy-Schahn

Abstract read
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In one paragraph

Article in Nature chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
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  3. Review
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  5. Review
  6. Article
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  9. Review
  10. Article
  11. Article
  12. Article
  13. Polysialylation at Early Stages of Oligodendrocyte Differentiation Promotes Myelin Repair.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  14. Article
  15. Engineering of complex protein sialylation in plants.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Glycosyltransferase engineering for carbohydrate synthesis.Biochemical Society transactions · 2016
    Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Timothy G KeysInstitute for Cellular Chemistry, Hannover Medical School, Hannover, Germany.
Hazel L S FuchsInstitute for Cellular Chemistry, Hannover Medical School, Hannover, Germany.
Jörg EhritInstitute for Cellular Chemistry, Hannover Medical School, Hannover, Germany.
Jürgen AlvesInstitute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.
Friedrich FreibergerInstitute for Cellular Chemistry, Hannover Medical School, Hannover, Germany.
Rita Gerardy-SchahnInstitute for Cellular Chemistry, Hannover Medical School, Hannover, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oligo- and polysaccharides have myriad applications as therapeutic reagents from glycoconjugate vaccines to matrices for tissue engineering. Polysaccharide length may vary over several orders of magnitude and is a critical determinant of both their physical properties and biological activities. Therefore, the tailored synthesis of oligo- and polysaccharides of defined size is a major goal for glycoengineering. By mutagenesis and screening of a bacterial polysialyltransferase (polyST), we identified a single-residue switch that controls the size distribution of polymeric products. Specific substitutions at this site yielded distributive enzymes that synthesize polysaccharides with narrow size distribution ideal for glycoengineering applications. Mechanistic investigation revealed that the wild-type enzyme has an extended binding site that accommodates at least 20 residues of the growing polymer; changes in affinity along this binding site allow fine-tuning of the enzyme's product distribution.

Indexed as

Protein EngineeringAmino Acid SubstitutionBinding SitesChromatography, High Pressure LiquidEscherichia coliGenes, SyntheticGenetic DriftKineticsMutagenesis, Site-DirectedNeisseria meningitidis, Serogroup BPolysaccharides, BacterialSialic AcidsSialyltransferasesPolysaccharides, Bacterialpolysialic acidSialic AcidsSialyltransferases

Identifiers

PMID24727899

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.