Evidence map›Paper›PMID 11743107›Full record

ArticlePlant physiology2001

A slow maturation of a cysteine protease with a granulin domain in the vacuoles of senescing Arabidopsis leaves.

K Yamada, R Matsushima, M Nishimura, I Hara-Nishimura

Open access · greenAbstract 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 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

76 citing papers in PubMed, 173 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. A Novel Senescence-Specific Gene (International journal of molecular sciences · 2022
    Article
  12. Transient proteolysis reduction ofFrontiers in plant science · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Papain-like cysteine proteases prepare plant cyclic peptide precursors for cyclization.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Do proteolytic cascades exist in plants?Journal of experimental botany · 2019
    Review
  18. Article
  19. Article
  20. Article

16 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

4 authors at 2 institutions in 1 country.

K YamadaDepartment of Botany, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.
R Matsushima
M Nishimura
I Hara-Nishimura
Kyoto University · JPNational Institute for Basic Biology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arabidopsis RD21 is a cysteine protease of the papain family. Unlike other members of the papain family, RD21 has a C-terminal extension sequence composed of two domains, a 2-kD proline-rich domain and a 10-kD domain homologous to animal epithelin/granulin family proteins. The RD21 protein was accumulated as 38- and 33-kD proteins in Arabidopsis leaves. An immunoblot showed that the 38-kD protein had the granulin domain, whereas the 33-kD protein did not. A pulse-chase experiment with Bright-Yellow 2 transformant cells expressing RD21 showed that RD21 was synthesized as a 57-kD precursor and was then slowly processed to make the 33-kD mature protein via the 38-kD intermediate. After a 12-h chase, the 38-kD intermediate was still detected in the cells. These results indicate that the N-terminal propeptide was first removed from the 57-kD precursor, and the C-terminal granulin domain was then slowly removed to yield the 33-kD mature protein. Subcellular fractionation of the Bright-Yellow 2 transformant showed that the intermediate and mature forms of RD21 were localized in the vacuoles. Under the acidic conditions of the vacuolar interior, the intermediate was found to be easily aggregated. The intermediate and the mature protein were accumulated in association with leaf senescence. Taken together, these results indicate that the intermediate of RD21 was accumulated in the vacuoles as an aggregate, and then slowly matured to make a soluble protease by removing the granulin domain during leaf senescence.

Indexed as

Intercellular Signaling Peptides and ProteinsAnimalsArabidopsisArabidopsis ProteinsChromosome MappingCloning, MolecularCysteine EndopeptidasesEnzyme PrecursorsExpressed Sequence TagsMaturation-Promoting FactorPlant LeavesProgranulinsVacuolesViral ProteinsArabidopsis ProteinsCysteine EndopeptidasesEnzyme PrecursorsIntercellular Signaling Peptides and ProteinsMaturation-Promoting FactorProgranulinsViral Proteins

Identifiers

PMID11743107
PMCPMC133567
OpenAlexW2134267576

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.