Evidence map›Paper›PMID 37828045›Full record

ArticleNature communications2023

Molecular mechanism of decision-making in glycosaminoglycan biosynthesis.

Douglas Sammon, Anja Krueger, Marta Busse-Wicher, Rhodri Marc Morgan, Stuart M Haslam, Benjamin Schumann, David C Briggs, Erhard Hohenester

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
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  3. Airway macrophage specific glycocalyx expression and remodeling following viral infection.Matrix biology : journal of the International Society for Matrix Biology · 2026
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  7. Review
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  13. Mucin-typebioRxiv : the preprint server for biology · 2025
    Article
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  19. Review
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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

8 authors at 4 institutions in 2 countries.

Douglas SammonDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK.ORCID 0000-0002-5014-1165
Anja KruegerDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK.ORCID 0000-0003-0227-8674
Marta Busse-WicherDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK.ORCID 0000-0001-6290-2462
Rhodri Marc MorganDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK.ORCID 0000-0002-9760-3638
Stuart M HaslamDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK.ORCID 0000-0002-5563-679X
Benjamin SchumannDepartment of Chemistry, Imperial College London, London, W12 0BZ, UK.ORCID 0000-0001-5504-0147
David C BriggsDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK. david.briggs@crick.ac.uk.ORCID 0000-0002-9793-7339
Erhard HohenesterDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK. e.hohenester@imperial.ac.uk.ORCID 0000-0002-0813-7218
Imperial College London · GBThe Francis Crick Institute · GBBabraham Institute · GBNaturalis Biodiversity Center · NL

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust CC2127
6 · The paper itself

Abstract

Two major glycosaminoglycan types, heparan sulfate (HS) and chondroitin sulfate (CS), control many aspects of development and physiology in a type-specific manner. HS and CS are attached to core proteins via a common linker tetrasaccharide, but differ in their polymer backbones. How core proteins are specifically modified with HS or CS has been an enduring mystery. By reconstituting glycosaminoglycan biosynthesis in vitro, we establish that the CS-initiating N-acetylgalactosaminyltransferase CSGALNACT2 modifies all glycopeptide substrates equally, whereas the HS-initiating N-acetylglucosaminyltransferase EXTL3 is selective. Structure-function analysis reveals that acidic residues in the glycopeptide substrate and a basic exosite in EXTL3 are critical for specifying HS biosynthesis. Linker phosphorylation by the xylose kinase FAM20B accelerates linker synthesis and initiation of both HS and CS, but has no effect on the subsequent polymerisation of the backbone. Our results demonstrate that modification with CS occurs by default and must be overridden by EXTL3 to produce HS.

Indexed as

Chondroitin SulfatesGlycosaminoglycansGlycopeptidesHeparan SulfatePhosphorylationChondroitin SulfatesGlycopeptidesGlycosaminoglycansHeparan Sulfate

Identifiers

PMID37828045
PMCPMC10570366
OpenAlexW4387599871

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.