Evidence map›Paper›PMID 26575439›Full record

ArticleNature structural & molecular biology2015

Structural characterization of human heparanase reveals insights into substrate recognition.

Liang Wu, Cristina M Viola, Andrzej M Brzozowski, Gideon J Davies

Erratum issuedOpen access · greenAbstract read
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. An erratum has been issued. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

85 citing papers in PubMed, 166 citations in OpenAlex.

  1. Review
  2. Integrated 3D-QSAR and cellular profiling of sulfated and hydrophobic aminoglycoside glycans to modulate heparanase activity.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. The Pathophysiological Functions of Heparanases: From Evolution, Structural and Tissue-Specific Perspectives.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Strategies ofFrontiers in cellular and infection microbiology · 2024
    Review
  18. Review
  19. Synthetic Heparanase Inhibitors Can Prevent Herpes Simplex Viral Spread.Angewandte Chemie (International ed. in English) · 2023
    Article
  20. Article

25 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Liang WuDepartment of Chemistry, University of York, York, UK.
Cristina M ViolaDepartment of Chemistry, University of York, York, UK.
Andrzej M BrzozowskiDepartment of Chemistry, University of York, York, UK.
Gideon J DaviesDepartment of Chemistry, University of York, York, UK.ORCID http://orcid.org/0000-0002-7343-776X
University of York · GB

Funding

ZINC DEFICIENCY &PROTEIN EXPRESSION IN RAT OLFACTORY BULBSP41RR005351 · NCRR · UNIVERSITY OF GEORGIA (UGA) · PI VENOT, ANDRE · 1989 to 2011
$18.4M
European Research Council 322942Medical Research Council MR/K000179/1NCRR NIH HHS P41 RR005351NCRR NIH HHS RR005351
6 · The paper itself

Abstract

Heparan sulfate (HS) is a glycosaminoglycan that forms a key component of the extracellular matrix (ECM). Breakdown of HS is carried out by heparanase (HPSE), an endo-β-glucuronidase of the glycoside hydrolase 79 (GH79) family. Overexpression of HPSE results in breakdown of extracellular HS and release of stored growth factors and hence is strongly linked to cancer metastasis. Here we present crystal structures of human HPSE at 1.6-Å to 1.9-Å resolution that reveal how an endo-acting binding cleft is exposed by proteolytic activation of latent proHPSE. We used oligosaccharide complexes to map the substrate-binding and sulfate-recognition motifs. These data shed light on the structure and interactions of a key enzyme involved in ECM maintenance and provide a starting point for the design of HPSE inhibitors for use as biochemical tools and anticancer therapeutics.

Indexed as

Crystallography, X-RayGlucuronidaseHeparanaseHeparan SulfateHumansProtein BindingProtein ConformationGlucuronidaseHeparanaseHeparan Sulfate

Identifiers

PMID26575439
PMCPMC5008439
OpenAlexW2200275279

What OpenQuestion holds

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LicenceTDM
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.