Evidence map›Paper›PMID 32937952›Full record

ReviewMolecules (Basel, Switzerland)2020

Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional Diversity.

Thibault Annaval, Rebekka Wild, Yoann Crétinon, Rabia Sadir, Romain R Vivès, Hugues Lortat-Jacob

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

52 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
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  7. Review
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  14. Untangling Heparan Sulfate 3-Analytical chemistry · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Myeloid deficiency of heparan sulfate 6-O-endosulfatases impairs bone marrow hematopoiesis.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Article
  20. Review
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 1 institution in 1 country.

Thibault AnnavalInstitut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, 38000 Grenoble, France.
Rebekka WildInstitut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, 38000 Grenoble, France.ORCID 0000-0003-2025-7228
Yoann CrétinonInstitut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, 38000 Grenoble, France.
Rabia SadirInstitut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, 38000 Grenoble, France.
Romain R VivèsInstitut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, 38000 Grenoble, France.
Hugues Lortat-JacobInstitut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, CEA, 38000 Grenoble, France.ORCID 0000-0002-9772-0762
Centre National de la Recherche Scientifique · FR

Funding

Agence Nationale de la Recherche ANR-10-LABX-49-01 (Grenoble Alliance for Integrated Structural Cell Biology)Agence Nationale de la Recherche ANR-15-IDEX-02 (Glyco@Alps)Agence Nationale de la Recherche ANR-18-CE11-0006-01
6 · The paper itself

Abstract

Glycosylation is a common and widespread post-translational modification that affects a large majority of proteins. Of these, a small minority, about 20, are specifically modified by the addition of heparan sulfate, a linear polysaccharide from the glycosaminoglycan family. The resulting molecules, heparan sulfate proteoglycans, nevertheless play a fundamental role in most biological functions by interacting with a myriad of proteins. This large functional repertoire stems from the ubiquitous presence of these molecules within the tissue and a tremendous structural variety of the heparan sulfate chains, generated through both biosynthesis and post synthesis mechanisms. The present review focusses on how proteoglycans are "gagosylated" and acquire structural complexity through the concerted action of Golgi-localized biosynthesis enzymes and extracellular modifying enzymes. It examines, in particular, the possibility that these enzymes form complexes of different modes of organization, leading to the synthesis of various oligosaccharide sequences.

Indexed as

AnimalsCell MembraneExtracellular MatrixGlycosaminoglycansGlycosylationGolgi ApparatusHeparan SulfateHeparan Sulfate ProteoglycansHumansMutationOligosaccharidesProtein BiosynthesisProtein DomainsProtein Processing, Post-TranslationalGlycosaminoglycansHeparan SulfateHeparan Sulfate ProteoglycansOligosaccharidesbiosynthesisbiosynthesis and post synthetic enzymesglycosaminoglycanglycosylationheparan sulfateproteoglycan

Identifiers

PMID32937952
PMCPMC7570499
OpenAlexW3086179567

What OpenQuestion holds

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LicenceCC BY
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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.