Evidence map›Paper›PMID 18618271›Full record

ArticlePlant molecular biology2008

Evolutionary relationship between defensins in the Poaceae family strengthened by the characterization of new sugarcane defensins.

V S De-Paula, G Razzera, L Medeiros, C A Miyamoto, M S Almeida, E Kurtenbach, F C L Almeida, A P Valente

Abstract read
PubMed Publisher
In one paragraph

Article in Plant molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
0.8field-weighted citation impact, top 28% 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

14 citing papers in PubMed, 1 synthesis or guideline pooled it, 36 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. The antimicrobial activity of ETD151 defensin is dictated by the presence of glycosphingolipids in the targeted organisms.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Membrane-Interacting Antifungal Peptides.Frontiers in cell and developmental biology · 2021
    Review
  10. Article
  11. Review
  12. Article
  13. Crystallization and preliminary X-ray crystallographic analysis of the plant defensin NaD1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  14. Antibacterial Activity of Tris NaCl and PBS Buffer Protein Extract ofDose-response : a publication of International Hormesis Society
    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

8 authors at 1 institution in 1 country.

V S De-PaulaCentro Nacional de Ressonância Magnética Nuclear, Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Av. Brigadeiro Trompowski, s/n, CCS Bloco E sala 10, Rio de Janeiro, RJ, Brazil.
G Razzera
L Medeiros
C A Miyamoto
M S Almeida
E Kurtenbach
F C L Almeida
A P Valente
Universidade Federal do Rio de Janeiro · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant defensins are small (45-54 amino acids), highly basic, cysteine-rich peptides structurally related to defensins of other organisms, including insects and mammals. Small putative proteins (MW < 10 kDa) containing eight cysteines were screened based on the sugarcane expressed sequence tag (EST) database. We selected ORFs that exhibited 25-100% similarity in primary sequence with other defensins in the NCBI database and that contained eight cysteines. This similarity is sufficient for folding prediction, but not enough for biological activity inference. Six putative defensins (Sd1-6) were selected, and activity assays showed that recombinant Sd1, Sd3 and Sd5 are active against fungi, but not against bacteria. Structural characterization, based on circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy showed that the structures of these Sds were compatible with alpha/beta proteins, a feature expected for plant defensins. Phylogenetic analysis revealed that sugarcane defensins could clearly be grouped within defensins from Poaceae family and Andropogoneae tribe. Our work demonstrates that defensins show strong conservation in the Poaceae family and may indicate that the same conservation occurs in other families. We suggest that evolutionary relationships within plant families can be used as a procedure to predict and annotate new defensins in genomes and group them in evolutionary classes to help in the investigation of their biological function.

Indexed as

Evolution, MolecularSaccharumAmino Acid SequenceAntifungal AgentsChromatography, High Pressure LiquidCloning, MolecularConserved SequenceDefensinsElectrophoresis, Polyacrylamide GelEscherichia coliFungiMagnetic Resonance SpectroscopyMicrobial Sensitivity TestsMolecular Sequence DataPhylogenyPlant ProteinsAntifungal AgentsDefensinsPlant ProteinsRecombinant Proteins

Identifiers

PMID18618271
OpenAlexW2066859945

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.