Evidence map›Paper›PMID 22474571›Full record

ReviewToxins2012

Host-defense activities of cyclotides.

David J Craik

Open access · goldAbstract readReview
In one paragraph

Review in Toxins, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 116 citations in OpenAlex.

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  17. Structural and functional studies ofThe Journal of biological chemistry · 2020
    Article
  18. Suppressive role of Viola odorata extract on malignant characters of mammosphere-derived breast cancer stem cells.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2020
    Article
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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

1 author at 1 institution in 1 country.

David J CraikInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia. d.craik@imb.uq.edu.au
University of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclotides are plant mini-proteins whose natural function is thought to be to protect plants from pest or pathogens, particularly insect pests. They are approximately 30 amino acids in size and are characterized by a cyclic peptide backbone and a cystine knot arrangement of three conserved disulfide bonds. This article provides an overview of the reported pesticidal or toxic activities of cyclotides, discusses a possible common mechanism of action involving disruption of biological membranes in pest species, and describes methods that can be used to produce cyclotides for potential applications as novel pesticidal agents.

Indexed as

Host-Pathogen InteractionsPesticidesAmino Acid SequenceAnimalsCell MembraneCell SurvivalCyclotidesCystine Knot MotifsErythrocytesHemolysisHumansInsectaMolecular Sequence DataPest Control, BiologicalPlant ProteinsCyclotidesPesticidesPlant Proteinscircular proteincyclic peptidecyclotidecystine knotinsecticidekalata B1

Identifiers

PMID22474571
PMCPMC3317112
OpenAlexW2025405581

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.