Evidence map›Paper›PMID 17726719›Full record

ArticleJournal of peptide science : an official publication of the European Peptide Society2007

Lipid transfer proteins from Brassica campestris and mung bean surpass mung bean chitinase in exploitability.

Peng Lin, Lixin Xia, Jack H Wong, T B Ng, Xiuyun Ye, Shaoyun Wang, Xiangzhu Shi

Abstract read
In one paragraph

Article in Journal of peptide science : an official publication of the European Peptide Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Purification of an Antifungal Peptide from Seeds ofMolecules (Basel, Switzerland) · 2019
    Article
  12. Article
  13. Antimicrobial Peptides from Plants.Pharmaceuticals (Basel, Switzerland) · 2015
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

7 authors.

Peng LinDepartment of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China.
Lixin Xia
Jack H Wong
T B Ng
Xiuyun Ye
Shaoyun Wang
Xiangzhu Shi

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antifungal peptides with a molecular mass of 9 kDa and an N-terminal sequence demonstrating remarkable similarity to those of nonspecific lipid transfer proteins (nsLTPs) were isolated from seeds of the vegetable Brassica campestris and the mung bean. The purified peptides exerted an inhibitory action on mycelial growth in various fungal species. The antifungal activity of Brassica and mung bean nsLTPs were thermostable, pH-stable, and stable after treatment with pepsin and trypsin. In contrast, the antifungal activity of mung bean chitinase was much less stable to changes in pH and temperature. Brassica LTP inhibited proliferation of hepatoma Hep G2 cells and breast cancer MCF 7 cells with an IC(50) of 5.8 and 1.6 microM, respectively, and the activity of HIV-1 reverse transcriptase with an IC(50) of 4 microM. However, mung bean LTP and chitinase were devoid of antiproliferative and HIV-1 reverse transcriptase inhibitory activities. In contrast to the mung bean LTP, which exhibited antibacterial activity, Brassica LTP was inactive. All three antifungal peptides lacked mitogenic activity toward splenocytes. These results indicate that the two LTPs have more desirable activities than the chitinase and that there is a dissociation between the antifungal and other activities of these antifungal proteins.

Indexed as

Amino Acid SequenceAntifungal AgentsAntigens, PlantBrassicaCarrier ProteinsCell Line, TumorCell ProliferationChitinasesHIV Integrase InhibitorsHIV Reverse TranscriptaseHot TemperatureHumansHydrogen-Ion ConcentrationMolecular Sequence DataPhaseolusPlant ProteinsAntifungal AgentsAntigens, PlantCarrier ProteinsChitinasesHIV Integrase InhibitorsHIV Reverse Transcriptaselipid transfer proteins, plantPlant Proteins

Identifiers

PMID17726719
PMCPMC7167883

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.