Evidence map›Paper›PMID 18643977›Full record

ArticleThe Plant journal : for cell and molecular biology2008

Proteolytic processing of a precursor protein for a growth-promoting peptide by a subtilisin serine protease in Arabidopsis.

Renu Srivastava, Jian-Xiang Liu, Stephen H Howell

Open access · bronzeAbstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

86 citing papers in PubMed, 166 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Processing and release of endogenous immunogenic peptide signals.The Plant journal : for cell and molecular biology · 2026
    Review
  6. Plant subtilases as key initiators of peptide ligand-receptor signaling.The Plant journal : for cell and molecular biology · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Peptide hormones in plants.Molecular horticulture · 2025
    Review
  13. Tobacco (Frontiers in plant science · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Characterization of the Serine Protease TlSP1 fromJournal of fungi (Basel, Switzerland) · 2024
    Article
  18. Review
  19. Review
  20. Article

26 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

3 authors at 1 institution in 1 country.

Renu SrivastavaPlant Sciences Institute, Iowa State University, Ames, IA 50011, USA.
Jian-Xiang LiuPlant Sciences Institute, Iowa State University, Ames, IA 50011, USA.
Stephen H HowellPlant Sciences Institute, Iowa State University, Ames, IA 50011, USA.
Iowa State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phytosulfokines (PSKs) are secreted, sulfated peptide hormones derived from larger prepropeptide precursors. Proteolytic processing of one of the precursors, AtPSK4, was demonstrated by cleavage of a preproAtPSK4-myc transgene product to AtPSK4-myc. Cleavage of proAtPSK4 was induced by placing root explants in tissue culture. The processing of proAtPSK4 was dependent on AtSBT1.1, a subtilisin-like serine protease, encoded by one of 56 subtilase genes in Arabidopsis. The gene encoding AtSBT1.1 was up-regulated following the transfer of root explants to tissue culture, suggesting that activation of the proteolytic machinery that cleaves proAtPSK4 is dependent on AtSBT1.1 expression. We also demonstrated that a fluorogenic peptide representing the putative subtilase recognition site in proAtPSK4 is cleaved in vitro by affinity-purified AtSBT1.1. An alanine scan through the recognition site peptide indicated that AtSBT1.1 is fairly specific for the AtPSK4 precursor. Thus, this peptide growth factor, which promotes callus formation in culture, is proteolytically cleaved from its precursor by a specific plant subtilase encoded by a gene that is up-regulated during the process of transferring root explants to tissue culture.

Indexed as

ArabidopsisArabidopsis ProteinsDNA, BacterialGene Expression ProfilingGene Expression Regulation, PlantMicroscopy, ConfocalMutagenesis, InsertionalPlant RootsPlants, Genetically ModifiedPlasmidsProtein PrecursorsProtein Processing, Post-TranslationalRNA, PlantSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSubstrate SpecificitySubtilisinsArabidopsis ProteinsDNA, BacterialProtein PrecursorsRNA, Plantsubtilase, plantSubtilisinsT-DNA

Identifiers

PMID18643977
PMCPMC2667306
OpenAlexW2052595164

What OpenQuestion holds

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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.