Evidence map›Paper›PMID 9234752›Full record

ArticleInfection and immunity1997

Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus pathogenic to humans.

A Beauvais, M Monod, J Wyniger, J P Debeaupuis, E Grouzmann, N Brakch, J Svab, A G Hovanessian, J P Latgé

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

32 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. An anti-adhesive peptide found in extracellular vesicles fromCell surface (Amsterdam, Netherlands) · 2025
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  14. Review
  15. Allergens/Antigens, toxins and polyketides of important Aspergillus species.Indian journal of clinical biochemistry : IJCB · 2011
    Article
  16. Article
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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

9 authors at 1 institution in 1 country.

A BeauvaisLaboratoire des Aspergillus, Institut Pasteur, Paris, France.
M Monod
J Wyniger
J P Debeaupuis
E Grouzmann
N Brakch
J Svab
A G Hovanessian
J P Latgé
Institut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A dipeptidyl-peptidase IV was purified from the culture medium of the human-pathogenic fungus Aspergillus fumigatus. The enzyme has an apparent molecular mass of 95 kDa and contained approximately 10 kDa of N-linked carbohydrate. This glycoprotein is antigenic and has all characteristics of the class IV dipeptidyl-peptidases: removal of Xaa-Pro and to a lesser extent Xaa-Ala dipeptides from the N termini of peptides, including bioactive peptides such as neuropeptide Y, [des-Arg1] bradykinin, and glucagon-like peptide 1, activity at neutral pH, and presence in the amino acid sequence of the Gly-X-Ser-X-Gly consensus motif of the serine-hydrolases and the putative catalytic triad (Ser613, Asp690, His725) of the dipeptidyl-peptidases. Moreover, the last 200 amino acids displayed 60 to 65% similarity with the other dipeptidyl-peptidases IV from rat, mouse, human, and yeast. However, unlike the other dipeptidyl-peptidases, the dipeptidyl-peptidase IV of A. fumigatus is a secreted enzyme with a cleavable signal peptide. Expression of a recombinant dipeptidyl-peptidase IV of A. fumigatus has been attained in the yeast Pichia pastoris.

Indexed as

Amino Acid SequenceAnimalsAntigens, CDAspergillus fumigatusBase SequenceHumansMiceMolecular Sequence DataPichiaRatsRecombinant ProteinsAntigens, CDRecombinant Proteins

Identifiers

PMID9234752
PMCPMC175429
OpenAlexW2142889585

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.