Evidence map›Paper›PMID 21210197›Full record

ArticleThe protein journal2011

Identification of botryticidal proteins with similarity to NBS-LRR proteins in rosemary pepper (Lippia sidoides Cham.) flowers.

João S Moreira, Renato G Almeida, Letícia S Tavares, Marcelo O Santos, Lyderson F Viccini, Ilka M Vasconcelos, José T A Oliveira, Nádia R B Raposo, Simoni C Dias, Octavio L Franco

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Article in The protein journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed, 1 pooled it
1.1field-weighted citation impact, top 25% 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

3 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. 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

10 authors at 3 institutions in 1 country.

João S MoreiraCentro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília, SGAN Quadra 916, Módulo B, Av. W5 Norte 70. 790-160 Asa Norte, Brasília, DF-Brazil. josuender@gmail.com
Renato G Almeida
Letícia S Tavares
Marcelo O Santos
Lyderson F Viccini
Ilka M Vasconcelos
José T A Oliveira
Nádia R B Raposo
Simoni C Dias
Octavio L Franco
Universidade Federal de Juiz de Fora · BRUniversidade Católica de Brasília · BRUniversidade Federal do Ceará · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heavy agricultural losses are closely related to attacks by insect-pests and phytopathogens such as bacteria and fungi. Among them, the fungus Botrytis cinerea can cause gray mold in more than 200 different species of plants, and is considered a challenging problem for agribusiness. Fungicides are commonly used to control this pathogen because they are fast-working and easy to apply. However, the continuous use of fungicides may promote the selection of resistant fungi and can also cause profound contamination in ecosystems. Aiming to find alternative strategies to solve these problems, several studies have focused on searching for plant proteins and peptides with antifungal activities (AFPs). With this in mind, this report shows the isolation and characterization of two novels antifungal proteins from flowers of rosemary pepper (Lippia sidoides Cham.) with 10 and 15 kDa. Isolation was performed by using an Octyl-Sepharose hydrophobic column. In vitro bioassays indicated that isolated proteins were able to inhibit B. cinerea development, but were not effective against all bacteria tested. Moreover, N-termini sequences indicate that both proteins showed sequence homology with NBS-LRR R proteins with a lower molecular mass, suggesting possible protein fragmentation. Data reported here could help in the development of biotechnological products for crop protection against phytopathogenic fungi in the near future.

Indexed as

BotrytisAdenosine MonophosphateAmino Acid SequenceAnimalsBrazilFlowersFungicides, IndustrialLippiaMolecular Sequence DataPeptidesPlant ProteinsThionucleotidesadenosine 5'-phosphorothioateAdenosine Monophosphateantimicrobial peptide 1, Lippia sidoidesantimicrobial peptide 2, Lippia sidoidesFungicides, IndustrialPeptidesPlant ProteinsThionucleotides

Identifiers

PMID21210197
OpenAlexW1995650851

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.