Evidence map›Paper›PMID 26804624›Full record

ArticleScientific reports2016

A small molecule inhibitor of tropomyosin dissociates actin binding from tropomyosin-directed regulation of actin dynamics.

Teresa T Bonello, Miro Janco, Jeff Hook, Alex Byun, Mark Appaduray, Irina Dedova, Sarah Hitchcock-DeGregori, Edna C Hardeman, Justine R Stehn, Till Böcking and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. 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
4.0field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Alterations of actin in aging.Journal of cell science · 2026
    Review
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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

11 authors at 3 institutions in 2 countries.

Teresa T BonelloSchool of Medical Sciences, University of New South Wales, Sydney, NSW, 2052, Australia.
Miro JancoSchool of Medical Sciences and ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales, Sydney, NSW, 2052, Australia.
Jeff HookSchool of Medical Sciences, University of New South Wales, Sydney, NSW, 2052, Australia.
Alex ByunSchool of Medical Sciences, University of New South Wales, Sydney, NSW, 2052, Australia.
Mark AppaduraySchool of Medical Sciences, University of New South Wales, Sydney, NSW, 2052, Australia.
Irina DedovaSchool of Medical Sciences, University of New South Wales, Sydney, NSW, 2052, Australia.
Sarah Hitchcock-DeGregoriPathology &Laboratory Medicine, Robert Wood Johnson Medical School, Rutgers University, Piscataway, NJ 08854, USA.
Edna C HardemanSchool of Medical Sciences, University of New South Wales, Sydney, NSW, 2052, Australia.
Justine R StehnSchool of Medical Sciences, University of New South Wales, Sydney, NSW, 2052, Australia.
Till BöckingSchool of Medical Sciences and ARC Centre of Excellence in Advanced Molecular Imaging, University of New South Wales, Sydney, NSW, 2052, Australia.
Peter W GunningSchool of Medical Sciences, University of New South Wales, Sydney, NSW, 2052, Australia.
UNSW Sydney · AUARC Centre of Excellence in Advanced Molecular Imaging · AUJohnson University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tropomyosin family of proteins form end-to-end polymers along the actin filament. Tumour cells rely on specific tropomyosin-containing actin filament populations for growth and survival. To dissect out the role of tropomyosin in actin filament regulation we use the small molecule TR100 directed against the C terminus of the tropomyosin isoform Tpm3.1. TR100 nullifies the effect of Tpm3.1 on actin depolymerisation but surprisingly Tpm3.1 retains the capacity to bind F-actin in a cooperative manner. In vivo analysis also confirms that, in the presence of TR100, fluorescently tagged Tpm3.1 recovers normally into stress fibers. Assembling end-to-end along the actin filament is thereby not sufficient for tropomyosin to fulfil its function. Rather, regulation of F-actin stability by tropomyosin requires fidelity of information communicated at the barbed end of the actin filament. This distinction has significant implications for perturbing tropomyosin-dependent actin filament function in the context of anti-cancer drug development.

Indexed as

Actin CytoskeletonAnimalsHumansNeoplasmsProtein BindingProtein IsoformsProtein MultimerizationRabbitsSmall Molecule LibrariesTropomyosinProtein IsoformsSmall Molecule LibrariesTropomyosin

Identifiers

PMID26804624
PMCPMC4726228
OpenAlexW2412304225

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.