Evidence map›Paper›PMID 10024507›Full record

ArticleThe Biochemical journal1999

Complete sequence of the human mucin MUC4: a putative cell membrane-associated mucin.

N Moniaux, S Nollet, N Porchet, P Degand, A Laine, J P Aubert

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed, 2 pooled it
9.9field-weighted citation impact, top 1% 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

80 citing papers in PubMed, 2 syntheses or guidelines pooled it, 256 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Mucolytic bacteria: prevalence in various pathological diseases.World journal of microbiology & biotechnology · 2021
    Review
  12. Review
  13. Article
  14. Identification of proteins in the adhesive trails of the diatom Amphora coffeaeformis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Article
  15. Article
  16. Article
  17. PRDM16 functions as a suppressor of lung adenocarcinoma metastasis.Journal of experimental & clinical cancer research : CR · 2019
    Article
  18. Article
  19. Review
  20. Review

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

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 3 institutions in 1 country.

N MoniauxUnité 377 INSERM, Place de Verdun, 59045 Lille Cedex, France.
S Nollet
N Porchet
P Degand
A Laine
J P Aubert
Inserm · FRHôpital Claude Huriez · FRUniversité de Lille · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The MUC4 gene, which encodes a human epithelial mucin, is expressed in various epithelial tissues, just as well in adult as in poorly differentiated cells in the embryo and fetus. Its N-terminus and central sequences have previously been reported as comprising a 27-residue peptide signal, followed by a large domain varying in length from 3285 to 7285 amino acid residues. The present study establishes the whole coding sequence of MUC4 in which the C-terminus is 1156 amino acid residues long and shares a high degree of similarity with the rat sialomucin complex (SMC). SMC is a heterodimeric glycoprotein complex composed of mucin (ascites sialoglycoprotein 1, ASGP-1) and transmembrane (ASGP-2) subunits. The same organization is found in MUC4, where the presence of a GlyAspProHis proteolytic site may cleave the large precursor into two subunits, MUC4alpha and MUC4beta. Like ASGP-2, which binds the receptor tyrosine kinase p185(neu), MUC4beta possesses two epidermal growth factor-like domains, a transmembrane sequence and a potential phosphorylated site. MUC4, the human homologue of rat SMC, may be a heterodimeric bifunctional cell-surface glycoprotein of 2.12 micrometers. These results confer a new biological role for MUC4 as a ligand for ErbB2 in cell signalling.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCloning, MolecularDNA, ComplementaryExonsHumansMembrane ProteinsMolecular Sequence DataMucin-4MucinsRatsRNASequence Homology, Amino AcidDNA, ComplementaryMembrane ProteinsMUC4 protein, humanMuc4 protein, ratMucin-4MucinsRNA

Identifiers

PMID10024507
PMCPMC1220057
OpenAlexW2126982924

What OpenQuestion holds

Texttitle and abstract
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.