Evidence map›Paper›PMID 15064951›Full record

ArticlePlanta2004

Xylem sap protein composition is conserved among different plant species.

Anja Buhtz, Anna Kolasa, Kathleen Arlt, Christina Walz, Julia Kehr

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
9.6field-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

52 citing papers in PubMed, 172 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Lipid-Coated Nanobubbles in Plants.Nanomaterials (Basel, Switzerland) · 2023
    Review
  6. Review
  7. Article
  8. Identification of Diverse Stress-Responsive Xylem Sap Peptides in Soybean.International journal of molecular sciences · 2022
    Article
  9. Characterization of Oligopeptides inLife (Basel, Switzerland) · 2022
    Article
  10. Article
  11. Physiology and molecular biology of plants : an international journal of functional plant biology · 2021
    Article
  12. Article
  13. Appropriate NHFrontiers in plant science · 2021
    Article
  14. Comparative Proteomic Analysis ofMolecules (Basel, Switzerland) · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

5 authors at 2 institutions in 1 country.

Anja BuhtzMax-Planck-Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476, Golm, Germany.
Anna Kolasa
Kathleen Arlt
Christina Walz
Julia Kehr
Max Planck Society · DEMax Planck Institute of Molecular Plant Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xylem sap from broccoli (Brassica oleracea L. cv. Calabrais), rape (Brassica napus L. cv. Drakkar), pumpkin (Cucurbita maxima Duch. cv. gelber Zentner) and cucumber (Cucumis sativus L. cv. Hoffmanns Giganta) was collected by root pressure exudation from the surface of cut stems of healthy, adult plants. Total protein concentrations were in the range of 100 microg ml(-1). One-dimensional gel electrophoresis (SDS-PAGE) resulted in 10-20 visible protein bands in a molecular mass range from 10 to 100 kDa. The main bands were cut out, digested with trypsin, and analysed using tandem mass spectrometry. Fifty bands resulted in amino acid sequence information that was used to perform database similarity searches. Sequences from 30 bands showed high homology to proteins present in databases. Among them, we found mostly peroxidases, but could also identify the lectin-like xylem protein XSP30, a glycine-rich protein, serine proteases, an aspartyl protease family protein, chitinases, and a lipid transfer protein-like polypeptide. Sequence analysis predicted apoplastic secretion signals for all database entries similar to the partial xylem protein sequences. This and the lack of cross-reactivity with phloem protein-specific antibodies suggest that the proteins really originate from the xylem and do not result from phloem contamination. Most of the highly similar proteins probably function in repair and defence reactions. Some of the most abundant proteins (peroxidases, chitinases, serine proteases) were present in xylem exudate of all species analysed, often in more than one band. This indicates an important basic role of these proteins in maintaining xylem function.

Indexed as

Amino Acid SequenceBrassicaBrassica napusCucumis sativusCucurbitaElectrophoresis, Polyacrylamide GelMass SpectrometryMolecular Sequence DataPlant ProteinsPlantsPlant StructuresSequence Homology, Amino AcidSpecies SpecificityPlant Proteins

Identifiers

PMID15064951
OpenAlexW1978647138

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.