Evidence map›Paper›PMID 26968704›Full record

ArticleInvestigational new drugs2016

Microtubule-stabilizing properties of the avocado-derived toxins (+)-(R)-persin and (+)-(R)-tetrahydropersin in cancer cells and activity of related synthetic analogs.

Jessica J Field, Arun Kanakkanthara, Darby G Brooke, Saptarshi Sinha, Sushila D Pillai, William A Denny, Alison J Butt, John H Miller

Abstract read
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In one paragraph

Article in Investigational new drugs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Review
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 5 institutions in 3 countries.

Jessica J FieldCentre for Biodiscovery, School of Biological Sciences, Victoria University of Wellington, PO Box 600, Wellington, 6140, New Zealand.
Arun KanakkantharaCentre for Biodiscovery, School of Biological Sciences, Victoria University of Wellington, PO Box 600, Wellington, 6140, New Zealand.
Darby G BrookeCawthron Institute, Private Bag 2, Nelson, New Zealand.
Saptarshi SinhaCentre for Biodiscovery, School of Biological Sciences, Victoria University of Wellington, PO Box 600, Wellington, 6140, New Zealand.
Sushila D PillaiCentre for Biodiscovery, School of Biological Sciences, Victoria University of Wellington, PO Box 600, Wellington, 6140, New Zealand.
William A DennyAuckland Cancer Society Research Centre, The University of Auckland, Auckland, New Zealand.
Alison J ButtCancer Research Program, Garvan Institute of Medical Research, St. Vincent's Hospital, Darlinghurst, New South Wales, Australia.
John H MillerCentre for Biodiscovery, School of Biological Sciences, Victoria University of Wellington, PO Box 600, Wellington, 6140, New Zealand. john.h.miller@vuw.ac.nz.
Victoria University of Wellington · NZCancer Society of New Zealand · NZCawthron Institute · NZGarvan Institute of Medical Research · AUMayo Clinic in Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The avocado toxin (+)-R-persin (persin) is active at low micromolar concentrations against breast cancer cells and synergizes with the estrogen receptor modulator 4-hydroxytamoxifen. Previous studies in the estrogen receptor-positive breast cancer cell line MCF-7 indicate that persin acts as a microtubule-stabilizing agent. In the present study, we further characterize the properties of persin and several new synthetic analogues in human ovarian cancer cells. Persin and tetrahydropersin cause G2M cell cycle arrest and increase intracellular microtubule polymerization. One analog (4-nitrophenyl)-deshydroxypersin prevents cell proliferation and blocks cells in G1 of the cell cycle rather than G2M, suggesting an additional mode of action of these compounds independent of microtubules. Persin can synergize with other microtubule-stabilizing agents, and is active against cancer cells that overexpress the P-glycoprotein drug efflux pump. Evidence from Flutax-1 competition experiments suggests that while the persin binding site on β-tubulin overlaps the classical taxoid site where paclitaxel and epothilone bind, persin retains activity in cell lines with single amino acid mutations that affect these other taxoid site ligands. This implies the existence of a unique binding location for persin at the taxoid site.

Indexed as

AcetatesAntineoplastic Agents, PhytogenicATP Binding Cassette Transporter, Subfamily B, Member 1Binding, CompetitiveBinding SitesCell CycleCell Line, TumorCell ProliferationDrug SynergismFatty AlcoholsFemaleG2 Phase Cell Cycle CheckpointsHumansMicrotubulesM Phase Cell Cycle CheckpointsNitrobenzoates(4-nitrophenyl)deshydroxypersinAcetatesAntineoplastic Agents, PhytogenicATP Binding Cassette Transporter, Subfamily B, Member 1Fatty AlcoholsNitrobenzoatespersintetrahydropersinCancerFlutax-1Microtubule-stabilizing agentMultidrug resistancePelorusidePersinSynergyTaxoid binding siteTetrahydropersin

Identifiers

PMID26968704
OpenAlexW2296420484

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.