Evidence map›Paper›PMID 22998218›Full record

ArticleMolecular plant pathology2013

The rust transferred proteins-a new family of effector proteins exhibiting protease inhibitor function.

Klara Pretsch, Ariane Kemen, Eric Kemen, Matthias Geiger, Kurt Mendgen, Ralf Voegele

Open access · bronzeAbstract read
In one paragraph

Article in Molecular plant pathology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
9.7field-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

32 citing papers in PubMed, 61 citations in OpenAlex.

  1. PtRTP1, an Effector ofPlants (Basel, Switzerland) · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. EffectorFrontiers in microbiology · 2025
    Article
  6. Journal of fungi (Basel, Switzerland) · 2023
    Article
  7. The Biological Roles ofBiomolecules · 2023
    Review
  8. Review
  9. Article
  10. Review
  11. Genome-Wide Analysis of Four Pathotypes of Wheat Rust Pathogen (Journal of fungi (Basel, Switzerland) · 2021
    Article
  12. Article
  13. Candidate Effectors FromFrontiers in plant science · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

6 authors at 2 institutions in 1 country.

Klara PretschPhytopathologie, Fachbereich Biologie, Universität Konstanz, 78457, Konstanz, Germany.
Ariane Kemen
Eric Kemen
Matthias Geiger
Kurt Mendgen
Ralf Voegele
University of Konstanz · DEUniversity of Hohenheim · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Only few fungal effectors have been described to be delivered into the host cell during obligate biotrophic interactions. RTP1p, from the rust fungi Uromyces fabae and U. striatus, was the first fungal protein for which localization within the host cytoplasm could be demonstrated directly. We investigated the occurrence of RTP1 homologues in rust fungi and examined the structural and biochemical characteristics of the corresponding gene products. The analysis of 28 homologues showed that members of the RTP family are most likely to occur ubiquitously in rust fungi and to be specific to the order Pucciniales. Sequence analyses indicated that the structure of the RTPp effectors is bipartite, consisting of a variable N-terminus and a conserved and structured C-terminus. The characterization of Uf-RTP1p mutants showed that four conserved cysteine residues sustain structural stability. Furthermore, the C-terminal domain exhibits similarities to that of cysteine protease inhibitors, and it was shown that Uf-RTP1p and Us-RTP1p are able to inhibit proteolytic activity in Pichia pastoris culture supernatants. We conclude that the RTP1p homologues constitute a rust fungi-specific family of modular effector proteins comprising an unstructured N-terminal domain and a structured C-terminal domain, which exhibit protease inhibitory activity possibly associated with effector function during biotrophic interactions.

Indexed as

Amino Acid SequenceBasidiomycotaCysteine Proteinase InhibitorsDisulfidesExonsFungal ProteinsIntronsMolecular Sequence DataPhylogenyPichiaProtease InhibitorsProtein StabilityProtein Structure, TertiaryProteolysisSequence AlignmentSequence Homology, Amino AcidCysteine Proteinase InhibitorsDisulfidesFungal ProteinsProtease Inhibitors

Identifiers

PMID22998218
PMCPMC6638633
OpenAlexW2165811315

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.