Evidence map›Paper›PMID 24260279›Full record

ArticlePloS one2013

High resolution crystal structure of human β-glucuronidase reveals structural basis of lysosome targeting.

Md Imtaiyaz Hassan, Abdul Waheed, Jeffery H Grubb, Herbert E Klei, Sergey Korolev, William S Sly

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2013. 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 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Exploiting the Potential ofBiomedicines · 2021
    Review
  6. First Report of a Patient with MPS Type VII, Due to Novel Mutations inInternational journal of molecular sciences · 2019
    Article
  7. Article
  8. Oral manifestations in patients and dogs with mucopolysaccharidosis Type VII.American journal of medical genetics. Part A · 2019
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Epidemiology of mucopolysaccharidoses.Molecular genetics and metabolism · 2017
    Article
  14. Article
  15. Annexin-directed β-glucuronidase for the targeted treatment of solid tumors.Protein engineering, design & selection : PEDS · 2017
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Md Imtaiyaz HassanEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, Saint Louis, Missouri, United States of America ; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi, India.
Abdul Waheed
Jeffery H Grubb
Herbert E Klei
Sergey Korolev
William S Sly
Saint Louis University · USBristol-Myers Squibb (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human β-glucuronidase (GUS) cleaves β-D-glucuronic acid residues from the non-reducing termini of glycosaminoglycan and its deficiency leads to mucopolysaccharidosis type VII (MPSVII). Here we report a high resolution crystal structure of human GUS at 1.7 Å resolution and present an extensive analysis of the structural features, unifying recent findings in the field of lysosome targeting and glycosyl hydrolases. The structure revealed several new details including a new glycan chain at Asn272, in addition to that previously observed at Asn173, and coordination of the glycan chain at Asn173 with Lys197 of the lysosomal targeting motif which is essential for phosphotransferase recognition. Analysis of the high resolution structure not only provided new insights into the structural basis for lysosomal targeting but showed significant differences between human GUS, which is medically important in its own right, and E. coli GUS, which can be selectively inhibited in the human gut to prevent prodrug activation and is also widely used as a reporter gene by plant biologists. Despite these differences, both human and E. coli GUS share a high structure homology in all three domains with most of the glycosyl hydrolases, suggesting that they all evolved from a common ancestral gene.

Indexed as

Amino Acid SequenceCrystallography, X-RayGlucuronidaseGlycosaminoglycansHumansLysosomesMolecular Sequence DataGlucuronidaseGlycosaminoglycans

Identifiers

PMID24260279
PMCPMC3834196
OpenAlexW2063567876

What OpenQuestion holds

Textmetadata
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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.