Evidence map›Paper›PMID 30787180›Full record

ArticleThe Plant cell2019

AMP and GMP Catabolism in Arabidopsis Converge on Xanthosine, Which Is Degraded by a Nucleoside Hydrolase Heterocomplex.

Chiara Baccolini, Claus-Peter Witte

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Guanine storage vacuoles sequester guanine crystals and serve as nitrogen reserves inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Evolution of the biochemistry underpinning purine alkaloid metabolism in plants.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Binding asymmetry and conformational studies of the AtGSDA dimer.Computational and structural biotechnology journal · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Structure, Oligomerization and Activity Modulation in N-Ribohydrolases.International journal of molecular sciences · 2022
    Review
  16. Structure Characterization ofFrontiers in microbiology · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. Review
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

2 authors at 1 institution in 1 country.

Chiara BaccoliniDepartment of Molecular Nutrition and Biochemistry of Plants, Institute of Plant Nutrition, Leibniz University Hannover, Herrenhäuser Straße 2, 30419 Hannover, Germany.ORCID 0000-0002-0517-0100
Claus-Peter WitteDepartment of Molecular Nutrition and Biochemistry of Plants, Institute of Plant Nutrition, Leibniz University Hannover, Herrenhäuser Straße 2, 30419 Hannover, Germany cpwitte@pflern.uni-hannover.de.ORCID 0000-0002-3617-7807
Leibniz University Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants can fully catabolize purine nucleotides. A firmly established central intermediate is the purine base xanthine. In the current widely accepted model of plant purine nucleotide catabolism, xanthine can be generated in various ways involving either inosine and hypoxanthine or guanosine and xanthosine as intermediates. In a comprehensive mutant analysis involving single and multiple mutants of urate oxidase, xanthine dehydrogenase, nucleoside hydrolases, guanosine deaminase, and hypoxanthine guanine phosphoribosyltransferase, we demonstrate that purine nucleotide catabolism in Arabidopsis (

Indexed as

Adenosine MonophosphateArabidopsisArabidopsis ProteinsGuanosine MonophosphateMutationN-Glycosyl HydrolasesNucleoside DeaminasesPlants, Genetically ModifiedRibonucleosidesXanthinesAdenosine MonophosphateArabidopsis Proteinsguanosine deaminaseGuanosine MonophosphateN-Glycosyl HydrolasesNucleoside DeaminasesRibonucleosidesURH1 protein, ArabidopsisURH2 protein, ArabidopsisXanthinesxanthosine

Identifiers

PMID30787180
PMCPMC6482636
OpenAlexW2918042270

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.