Evidence map›Paper›PMID 11299370›Full record

ArticlePlant physiology2001

Chloroplast and mitochondrial proteases in Arabidopsis. A proposed nomenclature.

Z Adam, I Adamska, K Nakabayashi, O Ostersetzer, K Haussuhl, A Manuell, B Zheng, O Vallon, S R Rodermel, K Shinozaki and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
6.5field-weighted citation impact, top 2% 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

73 citing papers in PubMed, 216 citations in OpenAlex.

  1. Article
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  5. Transcriptome Analysis ofPlants (Basel, Switzerland) · 2021
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  7. International journal of molecular sciences · 2021
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  9. Structural basis for the N-degron specificity of ClpS1 from Arabidopsis thaliana.Protein science : a publication of the Protein Society · 2021
    Article
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  11. Co-Suppression ofPlants (Basel, Switzerland) · 2020
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  12. Article
  13. The Enigmatic Roles of PPR-SMR Proteins in Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

13 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

11 authors at 6 institutions in 5 countries.

Z AdamDepartment of Agricultural Botany, The Hebrew University of Jerusalem, Rehovot 76100, Israel. zach@agri.huji.ac.il
I Adamska
K Nakabayashi
O Ostersetzer
K Haussuhl
A Manuell
B Zheng
O Vallon
S R Rodermel
K Shinozaki
A K Clarke
Hebrew University of Jerusalem · ILIowa State University · USStockholm University · SEInstitut de Biologie Physico-Chimique · FRThe University of Tokyo · JPUmeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The identity and scope of chloroplast and mitochondrial proteases in higher plants has only started to become apparent in recent years. Biochemical and molecular studies suggested the existence of Clp, FtsH, and DegP proteases in chloroplasts, and a Lon protease in mitochondria, although currently the full extent of their role in organellar biogenesis and function remains poorly understood. Rapidly accumulating DNA sequence data, especially from Arabidopsis, has revealed that these proteolytic enzymes are found in plant cells in multiple isomeric forms. As a consequence, a systematic approach was taken to catalog all these isomers, to predict their intracellular location and putative processing sites, and to propose a standard nomenclature to avoid confusion and facilitate scientific communication. For the Clp protease most of the ClpP isomers are found in chloroplasts, whereas one is mitochondrial. Of the ATPase subunits, the one ClpD and two ClpC isomers are located in chloroplasts, whereas both ClpX isomers are present in mitochondria. Isomers of the Lon protease are predicted in both compartments, as are the different forms of FtsH protease. DegP, the least characterized protease in plant cells, has the most number of isomers and they are predicted to localize in several cell compartments. These predictions, along with the proposed nomenclature, will serve as a framework for future studies of all four families of proteases and their individual isomers.

Indexed as

Chromosome MappingArabidopsisChloroplastsEndopeptidasesMitochondriaTerminology as TopicEndopeptidases

Identifiers

PMID11299370
PMCPMC88846
OpenAlexW2123369982

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.