Evidence map›Paper›PMID 22791822›Full record

ArticleJournal of experimental botany2012

A cathepsin F-like peptidase involved in barley grain protein mobilization, HvPap-1, is modulated by its own propeptide and by cystatins.

Ines Cambra, Manuel Martinez, Beatriz Dáder, Pablo González-Melendi, Jacinto Gandullo, M Estrella Santamaría, Isabel Diaz

Open access · bronzeAbstract read
In one paragraph

Article in Journal of experimental botany, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

18 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. How Cysteine Protease GeneInternational journal of molecular sciences · 2021
    Article
  6. Review
  7. Article
  8. Insights on the Proteases Involved in Barley and Wheat Grain Germination.International journal of molecular sciences · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. 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

7 authors at 3 institutions in 2 countries.

Ines CambraCentro de Biotecnología y Genómica de Plantas (UPM-INIA), Campus Montegancedo, Universidad Politécnica de Madrid, Autovía M40 (Km 38), 28223-Pozuelo de Alarcón, Madrid, Spain.
Manuel Martinez
Beatriz Dáder
Pablo González-Melendi
Jacinto Gandullo
M Estrella Santamaría
Isabel Diaz
Centre for Plant Biotechnology and Genomics · ESConsejo Superior de Investigaciones Científicas · ESWestern University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Among the C1A cysteine proteases, the plant cathepsin F-like group has been poorly studied. This paper describes the molecular and functional characterization of the HvPap-1 cathepsin F-like protein from barley. This peptidase is N-glycosylated and has to be processed to become active by its own propeptide being an important modulator of the peptidase activity. The expression pattern of its mRNA and protein suggest that it is involved in different proteolytic processes in the barley plant. HvPap-1 peptidase has been purified in Escherichia coli and the recombinant protein is able to degrade different substrates, including barley grain proteins (hordeins, albumins, and globulins) stored in the barley endosperm. It has been localized in protein bodies and vesicles of the embryo and it is induced in aleurones by gibberellin treatment. These three features support the implication of HvPap-1 in storage protein mobilization during grain germination. In addition, a complex regulation exerted by the barley cystatins, which are cysteine protease inhibitors, and by its own propeptide, is also described.

Indexed as

AlbuminsAmino Acid SequenceBiological TransportCathepsin FCystatinsCysteine Proteinase InhibitorsEndospermEnzyme PrecursorsEscherichia coliGerminationGlobulinsGlutensGlycosylationHordeumMagnoliopsidaModels, MolecularAlbuminsCathepsin FCystatinsCysteine Proteinase InhibitorsEnzyme PrecursorsGlobulinsGlutensPlant ProteinsRecombinant Proteins

Identifiers

PMID22791822
PMCPMC3421991
OpenAlexW2115227167

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.