Evidence map›Paper›PMID 10715321›Full record

ArticleThe Plant cell2000

A conserved domain of the arabidopsis GNOM protein mediates subunit interaction and cyclophilin 5 binding.

M Grebe, J Gadea, T Steinmann, M Kientz, J U Rahfeld, K Salchert, C Koncz, G Jürgens

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

62 citing papers in PubMed, 128 citations in OpenAlex.

  1. Extracellular Vesicles and Immune Activation in Solid Organ Transplantation: The Impact of Immunosuppression.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2025
    Review
  2. Sec7 regulatory domains scaffold autoinhibited and active conformations.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. The Shared Proteome of the Apomictic FernInternational journal of molecular sciences · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

2 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

8 authors at 2 institutions in 1 country.

M GrebeEntwicklungsgenetik, Zentrum für Molekularbiologie der Pflanzen, Universität Tübingen, Auf der Morgenstelle 1, D-72076 Tübingen, Germany.
J Gadea
T Steinmann
M Kientz
J U Rahfeld
K Salchert
C Koncz
G Jürgens
University of Tübingen · DEMax Planck Research Unit for Enzymology of Protein Folding · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Arabidopsis GNOM protein, a guanine nucleotide exchange factor (GEF) that acts on ADP ribosylation factor (ARF)-type G proteins, is required for coordination of cell polarity along the apical-basal embryo axis. Interallelic complementation of gnom mutants suggested that dimerization is involved in GNOM function. Here, direct interaction between GNOM molecules is demonstrated in vitro and by using a yeast two-hybrid system. Interaction was confined to an N-terminal domain conserved within a subgroup of large ARF GEFs. The same domain mediated in vitro binding to cyclophilin 5 (Cyp5), which was identified as a GNOM interactor in two-hybrid screening. Cyp5 displayed peptidylprolyl cis/trans-isomerase and protein refolding activities that were sensitive to cyclosporin A. Cyp5 protein accumulated in several plant organs and, like GNOM, was partitioned between cytosolic and membrane fractions. Cyp5 protein was also expressed in the developing embryo. Our results suggest that Cyp5 may regulate the ARF GEF function of the GNOM protein during embryogenesis.

Indexed as

ADP-Ribosylation FactorsAmino Acid SequenceArabidopsisBinding SitesCatalysisConserved SequenceCyclosporineDimerizationGuanine Nucleotide Exchange FactorsMolecular Sequence DataPeptidylprolyl IsomerasePlant ProteinsProtein BindingProtein FoldingProtein Structure, TertiaryRecombinant Fusion ProteinsADP-Ribosylation FactorsCyclosporineGuanine Nucleotide Exchange FactorsPeptidylprolyl IsomerasePlant ProteinsRecombinant Fusion Proteins

Identifiers

PMID10715321
PMCPMC139835
OpenAlexW2109498209

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.