Evidence map›Paper›PMID 22520048›Full record

ArticleBMC plant biology2012

The family of Deg/HtrA proteases in plants.

Holger Schuhmann, Pitter F Huesgen, Iwona Adamska

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
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  7. ThePlant physiology · 2019
    Article
  8. Article
  9. Article
  10. Article
  11. Metabolic Reprogramming in Chloroplasts under Heat Stress in Plants.International journal of molecular sciences · 2018
    Review
  12. Review
  13. Article
  14. Review
  15. DEG9, a serine protease, modulates cytokinin and light signaling by regulating the level of ARABIDOPSIS RESPONSE REGULATOR 4.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Article
  17. Article
  18. Article
  19. The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases.Acta crystallographica. Section D, Biological crystallography · 2013
    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

3 authors at 1 institution in 2 countries.

Holger SchuhmannDepartment of Plant Physiology and Biochemistry, University of Konstanz, Universitätsstr, 10, 78457, Konstanz, Germany.
Pitter F Huesgen
Iwona Adamska
University of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe Deg/HtrA family of ATP-independent serine endopeptidases is present in nearly all organisms from bacteria to human and vascular plants. In recent years, multiple deg/htrA protease genes were identified in various plant genomes. During genome annotations most proteases were named according to the order of discovery, hence the same names were sometimes given to different types of Deg/HtrA enzymes in different plant species. This can easily lead to false inference of individual protease functions based solely on a shared name. Therefore, the existing names and classification of these proteolytic enzymes does not meet our current needs and a phylogeny-based standardized nomenclature is required.

resultsUsing phylogenetic and domain arrangement analysis, we improved the nomenclature of the Deg/HtrA protease family, standardized protease names based on their well-established nomenclature in Arabidopsis thaliana, and clarified the evolutionary relationship between orthologous enzymes from various photosynthetic organisms across several divergent systematic groups, including dicots, a monocot, a moss and a green alga. Furthermore, we identified a "core set" of eight proteases shared by all organisms examined here that might provide all the proteolytic potential of Deg/HtrA proteases necessary for a hypothetical plant cell.

conclusionsIn our proposed nomenclature, the evolutionarily closest orthologs have the same protease name, simplifying scientific communication when comparing different plant species and allowing for more reliable inference of protease functions. Further, we proposed that the high number of Deg/HtrA proteases in plants is mainly due to gene duplications unique to the respective organism.

Indexed as

Amino Acid SequenceCatalytic DomainDatabases, ProteinGene DuplicationGenes, PlantHeat-Shock ProteinsMolecular Sequence DataPDZ DomainsPeriplasmic ProteinsPhylogenyPlant ProteinsPlantsSequence AlignmentSerine EndopeptidasesDegP proteaseHeat-Shock ProteinsPeriplasmic ProteinsPlant ProteinsSerine Endopeptidases

Identifiers

PMID22520048
PMCPMC3473262
OpenAlexW2152451071

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.