Evidence map›Paper›PMID 19664563›Full record

ArticleJournal of bioscience and bioengineering2009

Campesin, a thermostable antifungal peptide with highly potent antipathogenic activities.

Peng Lin, Jack Ho Wong, Lixin Xia, Tzi Bun Ng

Abstract read
In one paragraph

Article in Journal of bioscience and bioengineering, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Purification of an Antifungal Peptide from Seeds ofMolecules (Basel, Switzerland) · 2019
    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

4 authors.

Peng LinDepartment of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China.
Jack Ho Wong
Lixin Xia
Tzi Bun Ng

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An 9.4-kDa antifungal peptide designated as campesin was isolated from seeds of the cabbage Brassica campestris. The isolation procedure involved affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Q-Sepharose and Mono S, and gel filtration on Superdex 75 and Superdex Peptide. The peptide was adsorbed on the first three chromatographic media. It exerted an inhibitory action on mycelial growth including Fusarium oxysporum and Mycosphaerella arachidicola, with an IC(50) of 5.1 microM and 4.4 microM, respectively. The peptide was characterized by remarkable thermostability and pH stability. It inhibited proliferation of HepG2 and MCF cancer cells with an IC(50) of 6.4 microM and 1.8 microM, and the activity of HIV-1 reverse transcriptase with an IC(50) of 3.2 microM. It demonstrated lysolecithin binding activity.

Indexed as

Antineoplastic AgentsAscomycotaBrassicaCell Line, TumorChromatography, AffinityChromatography, GelChromatography, Ion ExchangeFusariumHIV IntegraseHIV Integrase InhibitorsHumansInhibitory Concentration 50LecithinsPeptidesPlant ExtractsPlant ProteinsAntineoplastic Agentscampesin, Brassica campestrisHIV IntegraseHIV Integrase InhibitorsLecithinsp31 integrase protein, Human immunodeficiency virus 1PeptidesPlant ExtractsPlant ProteinsReverse Transcriptase InhibitorsSepharose

Identifiers

PMID19664563
PMCPMC7106469

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.