Evidence map›Paper›PMID 25120197›Full record

ArticleNature communications2014

Documentation and localization of force-mediated filamin A domain perturbations in moving cells.

Fumihiko Nakamura, Mia Song, John H Hartwig, Thomas P Stossel

Abstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Review
  2. Intermediate filaments and their associated molecules.Journal of biomedical research · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Role of chaperone-assisted selective autophagy (CASA) in mechanical stress protection of periodontal ligament cells.Journal of orofacial orthopedics = Fortschritte der Kieferorthopadie : Organ/official journal Deutsche Gesellschaft fur Kieferorthopadie · 2022
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Proteome Analysis of Isolated Podocytes Reveals Stress Responses in Glomerular Sclerosis.Journal of the American Society of Nephrology : JASN · 2020
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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.

Fumihiko NakamuraTranslational Medicine Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02445, USA.
Mia SongTranslational Medicine Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02445, USA.
John H HartwigTranslational Medicine Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02445, USA.
Thomas P StosselTranslational Medicine Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02445, USA.

Funding

PHAGOCYTOSIS--PULMONARY ALVEOLAR MACROPHAGESR01HL019429 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI STOSSEL, THOMAS PETER · 1985 to 2015
$10.1M
NHLBI NIH HHS HL19749NHLBI NIH HHS R01 HL019429
6 · The paper itself

Abstract

Endogenously and externally generated mechanical forces influence diverse cellular activities, a phenomenon defined as mechanotransduction. Deformation of protein domains by application of stress, previously documented to alter macromolecular interactions in vitro, could mediate these effects. We engineered a photon-emitting system responsive to unfolding of two repeat domains of the actin filament (F-actin) crosslinker protein filamin A (FLNA) that binds multiple partners involved in cell signalling reactions and validated the system using F-actin networks subjected to myosin-based contraction. Expressed in cultured cells, the sensor-containing FLNA construct reproducibly reported FLNA domain unfolding strikingly localized to dynamic, actively protruding, leading cell edges. The unfolding signal depends upon coherence of F-actin-FLNA networks and is enhanced by stimulating cell contractility. The results establish protein domain distortion as a bona fide mechanism for mechanotransduction in vivo.

Indexed as

ActinsAnimalsBiomechanical PhenomenaCell MovementCells, CulturedChlorocebus aethiopsCOS CellsFilaminsFluorescence Resonance Energy TransferIn Vitro TechniquesKidneyMechanotransduction, CellularOptics and PhotonicsActinsFilamins

Identifiers

PMID25120197
PMCPMC4139033

What OpenQuestion holds

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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.