Evidence map›Paper›PMID 18758940›Full record

ArticleGlycoconjugate journal2009

Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces.

Birgit Sauerzapfe, Karel Krenek, Judith Schmiedel, Warren W Wakarchuk, Helena Pelantová, Vladimir Kren, Lothar Elling

Abstract read
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In one paragraph

Article in Glycoconjugate journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

29 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
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  7. Review
  8. Article
  9. Cell-free systems for accelerating glycoprotein expression and biomanufacturing.Journal of industrial microbiology & biotechnology · 2020
    Review
  10. Enzymatic Cascades for TailoredMolecules (Basel, Switzerland) · 2019
    Article
  11. The β-Molecules (Basel, Switzerland) · 2019
    Article
  12. Article
  13. Machine-Driven Enzymatic Oligosaccharide Synthesis by Using a Peptide Synthesizer.Angewandte Chemie (International ed. in English) · 2018
    Article
  14. Article
  15. Article
  16. Article
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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

7 authors at 4 institutions in 3 countries.

Birgit SauerzapfeInstitute of Biotechnology and Helmholtz-Institute for Biomedical Engineering, RWTH Aachen University, Germany.
Karel Krenek
Judith Schmiedel
Warren W Wakarchuk
Helena Pelantová
Vladimir Kren
Lothar Elling
RWTH Aachen University · DECzech Academy of Sciences · CZCzech Academy of Sciences, Institute of Microbiology · CZNational Research Council Canada · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poly-N-acetyllactosamine (poly-LacNAc) structures have been identified as important ligands for galectin-mediated cell adhesion to extra-cellular matrix (ECM) proteins. We here present the biofunctionalization of surfaces with poly-LacNAc structures and subsequent binding of ECM glycoproteins. First, we synthesized beta-GlcNAc glycosides carrying a linker for controlled coupling onto chemically functionalized surfaces. Then we produced poly-LacNAc structures with defined lengths using human beta1,4-galactosyltransferase-1 and beta1,3-N-acetylglucosaminyltransferase from Helicobacter pylori. These compounds were also used for kinetic characterization of glycosyltransferases and lectin binding assays. A mixture of poly-LacNAc-structures covalently coupled to functionalized microtiter plates were identified for best binding to our model galectin His(6)CGL2. We further demonstrate for the first time that these poly-LacNAc surfaces are suitable for further galectin-mediated binding of the ECM glycoproteins laminin and fibronectin. This new technology should facilitate cell adhesion to biofunctionalized surfaces by imitating the natural ECM microenvironment.

Indexed as

AcetylglucosamineBiocompatible MaterialsExtracellular MatrixFungal ProteinsGalactosyltransferasesGalectin 2GalectinsGlycoproteinsGlycosidesHumansN-AcetylglucosaminyltransferasesPolysaccharidesAcetylglucosaminebeta1,4-galactosyltransferase, humanBiocompatible MaterialsCGL2 protein, Coprinus cinereusFungal ProteinsGalactosyltransferasesGalectin 2GalectinsGlycoproteinsGlycosidesN-Acetylglucosaminyltransferasespoly-N-acetyllactosaminePolysaccharides

Identifiers

PMID18758940
OpenAlexW2014388567

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.