Evidence map›Paper›PMID 8358229›Full record

ArticleGlycoconjugate journal1993

The roles of enteric bacterial sialidase, sialate O-acetyl esterase and glycosulfatase in the degradation of human colonic mucin.

A P Corfield, S A Wagner, L J O'Donnell, P Durdey, R A Mountford, J R Clamp

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Glycoconjugate journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

41 citing papers in PubMed, 114 citations in OpenAlex.

  1. Loss of sialic acid side-chainProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. "Tissue barriers · 2019
    Review
  11. Article
  12. Review
  13. Review
  14. 3-Sulfogalactosyl-dependent adhesion ofThe Journal of biological chemistry · 2017
    Article
  15. The sialateThe Journal of biological chemistry · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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.

A P CorfieldUniversity Department of Medicine, Bristol Royal Infirmary, UK.
S A Wagner
L J O'Donnell
P Durdey
R A Mountford
J R Clamp
Bristol Royal Infirmary · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sialidase activity in normal faecal extracts showed a preference for mucin-related glycoprotein and oligosaccharide substrates, but the presence of two or more O-acetyl esters at positions C7-C9 on the sialic acids retarded the rate of hydrolysis. A specific sialate O-acetyl esterase was detected with a lower total activity relative to sialidase with mucin substrates and having a pH optimum of 7.8 and a KM of approximately 1 mM sialate O-acetyl ester. A specific glycosulfatase activity was found in faecal extracts using the substrate lactit-[3H]ol 6-O-sulfate with a pH optimum of pH 5.0 and a KM of approximately 1 mM. Faecal extracts from ulcerative colitis (UC) patients had higher sialate O-acetyl esterase and glycosulfatase activity, while mucin sialidase activity was unchanged. Metabolically labelled mucin isolated from UC patients contained less sulfate and had lower sialic acid O-acetylation compared with normal mucin. Colonic mucin was degraded more efficiently by faecal extracts from UC patients compared with normal extracts. The UC mucin was degraded more rapidly than the normal mucin by faecal enzyme extracts from both normal and UC subjects.

Indexed as

AcetylationAcetylesteraseCarbohydrate SequenceCarboxylic Ester HydrolasesColitis, UlcerativeColonEnterobacteriaceaeFecesHumansMolecular Sequence DataMucinsNeuraminidaseSialic AcidsSulfatases9-O-acetyl-N-acetylneuraminic acidAcetylesteraseCarboxylic Ester HydrolasesglycosulphataseMucinsNeuraminidasesialate O-acetylesteraseSialic AcidsSulfatases

Identifiers

PMID8358229
OpenAlexW1966233840

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.