Evidence map›Paper›PMID 28467631›Full record

ReviewThe New phytologist2018

From structure to function - a family portrait of plant subtilases.

Andreas Schaller, Annick Stintzi, Susana Rivas, Irene Serrano, Nina V Chichkova, Andrey B Vartapetian, Dana Martínez, Juan J Guiamét, Daniela J Sueldo, Renier A L van der Hoorn and 2 more

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in The New phytologist, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed, 1 pooled it
21.8field-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

77 citing papers in PubMed, 1 synthesis or guideline pooled it, 140 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Natural Variation of NAR5 Determines Nitrogenase Activity and the Yield in Soybean.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Article
  6. Article
  7. Processing and release of endogenous immunogenic peptide signals.The Plant journal : for cell and molecular biology · 2026
    Review
  8. Article
  9. Journal of agricultural and food chemistry · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Long-Term Phytaspase Responses inInternational journal of molecular sciences · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The peptide hormoneProceedings of the National Academy of Sciences of the United States of America · 2024
    Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 9 institutions in 6 countries.

Andreas SchallerInstitute of Plant Physiology and Biotechnology, University of Hohenheim, Stuttgart, 70593, Germany.
Annick StintziInstitute of Plant Physiology and Biotechnology, University of Hohenheim, Stuttgart, 70593, Germany.
Susana RivasLaboratoire des Interactions Plantes-Microorganismes, LIPM, Université de Toulouse, INRA, CNRS, Castanet-Tolosan, 31326, France.
Irene SerranoLaboratoire des Interactions Plantes-Microorganismes, LIPM, Université de Toulouse, INRA, CNRS, Castanet-Tolosan, 31326, France.
Nina V ChichkovaBelozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119991, Russia.
Andrey B VartapetianBelozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119991, Russia.
Dana MartínezInstituto de Fisiología Vegetal, Universidad Nacional de La Plata, La Plata, 1900, Argentina.
Juan J GuiamétInstituto de Fisiología Vegetal, Universidad Nacional de La Plata, La Plata, 1900, Argentina.
Daniela J SueldoThe Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford, OX1 3RB, UK.
Renier A L van der HoornThe Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, Oxford, OX1 3RB, UK.
Vicente RamírezInstitute for Plant Cell Biology and Biotechnology, Heinrich-Heine University, Düsseldorf, 40225, Germany.
Pablo VeraInstitute for Plant Molecular and Cell Biology, Universidad Politécnica de Valencia-CSIC, Valencia, 46022, Spain.
Lomonosov Moscow State University · RUUniversity of Hohenheim · DEUniversity of Oxford · GBHeinrich Heine University Düsseldorf · DEInstituto de Fisiología Vegetal · ARLaboratoire des Interactions Plantes Micro-Organismes · FRUniversidad Nacional de La Plata · ARUniversitat Politècnica de València · ESUniversité de Toulouse · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Contents Summary 901 I. Introduction 901 II. Biochemistry and structure of plant SBTs 902 III. Phylogeny of plant SBTs and family organization 903 IV. Physiological roles of plant SBTs 905 V. Conclusions and outlook 911 Acknowledgements 912 References 912 SUMMARY: Subtilases (SBTs) are serine peptidases that are found in all three domains of life. As compared with homologs in other Eucarya, plant SBTs are more closely related to archaeal and bacterial SBTs, with which they share many biochemical and structural features. However, in the course of evolution, functional diversification led to the acquisition of novel, plant-specific functions, resulting in the present-day complexity of the plant SBT family. SBTs are much more numerous in plants than in any other organism, and include enzymes involved in general proteolysis as well as highly specific processing proteases. Most SBTs are targeted to the cell wall, where they contribute to the control of growth and development by regulating the properties of the cell wall and the activity of extracellular signaling molecules. Plant SBTs affect all stages of the life cycle as they contribute to embryogenesis, seed development and germination, cuticle formation and epidermal patterning, vascular development, programmed cell death, organ abscission, senescence, and plant responses to their biotic and abiotic environments. In this article we provide a comprehensive picture of SBT structure and function in plants.

Indexed as

Cell DeathPhylogenyPlant Physiological PhenomenaPlantsSubtilisinssubtilase, plantSubtilisinscell deathpeptide signalingplant defenseplant developmentprecursor processingproteolysisstructure-function relationshipsubtilisin-like proteinase

Identifiers

PMID28467631
OpenAlexW2611363539

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.