Evidence map›Paper›PMID 19488781›Full record

ArticlePlanta2009

Multiplicity of aspartic proteinases from Cynara cardunculus L.

Ana Cristina Sarmento, Henrique Lopes, Cláudia S Oliveira, Rui Vitorino, Bart Samyn, Kjell Sergeant, Griet Debyser, Jozef Van Beeumen, Pedro Domingues, Francisco Amado and 3 more

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 61 citations in OpenAlex.

  1. Production of Protein Hydrolysates Teff (Current issues in molecular biology · 2024
    Article
  2. Bioactive Compounds from Artichoke and Application Potential.Food technology and biotechnology · 2023
    Review
  3. Article
  4. Safety evaluation of the food enzyme phytepsin fromEFSA journal. European Food Safety Authority · 2023
    Article
  5. Safety evaluation of the food enzyme phytepsin fromEFSA journal. European Food Safety Authority · 2022
    Article
  6. Safety evaluation of the food enzyme phytepsin fromEFSA journal. European Food Safety Authority · 2022
    Article
  7. Safety evaluation of the food enzyme phytepsin fromEFSA journal. European Food Safety Authority · 2022
    Article
  8. The Employment of GeneraNutrients · 2022
    Review
  9. Plant Milk-Clotting Enzymes for Cheesemaking.Foods (Basel, Switzerland) · 2022
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. 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

13 authors at 4 institutions in 3 countries.

Ana Cristina SarmentoCESAM, Department of Biology, University of Aveiro, 3810-193, Aveiro, Portugal. acsarmento@ua.pt
Henrique Lopes
Cláudia S Oliveira
Rui Vitorino
Bart Samyn
Kjell Sergeant
Griet Debyser
Jozef Van Beeumen
Pedro Domingues
Francisco Amado
Euclides Pires
M Rosário M Domingues
Marlene T Barros
University of Aveiro · PTGhent University · BECentro de Neurociências e Biologia CelularUniversidade Católica Portuguesa · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aspartic proteinases (AP) play major roles in physiologic and pathologic scenarios in a wide range of organisms from vertebrates to plants or viruses. The present work deals with the purification and characterisation of four new APs from the cardoon Cynara cardunculus L., bringing the number of APs that have been isolated, purified and biochemically characterised from this organism to nine. This is, to our knowledge, one of the highest number of APs purified from a single organism, consistent with a specific and important biological function of these protein within C. cardunculus. These enzymes, cardosins E, F, G and H, are dimeric, glycosylated, pepstatin-sensitive APs, active at acidic pH, with a maximum activity around pH 4.3. Their primary structures were partially determined by N- and C-terminal sequence analysis, peptide mass fingerprint analysis on a MALDI-TOF/TOF instrument and by LC-MS/MS analysis on a Q-TRAP instrument. All four enzymes are present on C. cardunculus L. pistils, along with cyprosins and cardosins A and B. Their micro-heterogeneity was detected by 2D-electrophoresis and mass spectrometry. The enzymes resemble cardosin A more than they resemble cardosin B or cyprosin, with cardosin E and cardosin G being more active than cardosin A, towards the synthetic peptide KPAEFF(NO(2))AL. The specificity of these enzymes was investigated and it is shown that cardosin E, although closely related to cardosin A, exhibits different specificity.

Indexed as

Aspartic Acid EndopeptidasesChromatography, LiquidCynaraElectrophoresis, Gel, Two-DimensionalHydrogen-Ion ConcentrationPlant ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryAspartic Acid Endopeptidasesaspartic proteinases, Cynara cardunculusPlant Proteins

Identifiers

PMID19488781
OpenAlexW1996923588

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.