Evidence map›Paper›PMID 19883801›Full record

ArticleActa biomaterialia2010

Passive and active microrheology for cross-linked F-actin networks in vitro.

Hyungsuk Lee, Jorge M Ferrer, Fumihiko Nakamura, Matthew J Lang, Roger D Kamm

Open access · greenAbstract read
In one paragraph

Article in Acta biomaterialia, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 70 citations in OpenAlex.

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  13. Optical trapping microrheology in cultured human cells.The European physical journal. E, Soft matter · 2012
    Article
  14. Polymer physics of the cytoskeleton.Current opinion in solid state & materials science · 2011
    Article
  15. 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

5 authors at 2 institutions in 1 country.

Hyungsuk LeeDepartment of Mechanical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Jorge M Ferrer
Fumihiko Nakamura
Matthew J Lang
Roger D Kamm
Massachusetts Institute of Technology · USHarvard University · US

Funding

MSM-Multi-scale Analysis of Cellular Force Transmission and Biochemical ActivatioR01GM076689 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KAMM, ROGER D. · 2005 to 2007
$871k
NIGMS NIH HHS GM076689NIGMS NIH HHS R01 GM076689
6 · The paper itself

Abstract

Actin filament (F-actin) is one of the dominant structural constituents in the cytoskeleton. Orchestrated by various actin-binding proteins (ABPs), F-actin is assembled into higher-order structures such as bundles and networks that provide mechanical support for the cell and play important roles in numerous cellular processes. Although mechanical properties of F-actin networks have been extensively studied, the underlying mechanisms for network elasticity are not fully understood, in part because different measurements probe different length and force scales. Here, we developed both passive and active microrheology techniques using optical tweezers to estimate the mechanical properties of F-actin networks at a length scale comparable to cells. For the passive approach we tracked the motion of a thermally fluctuating colloidal sphere to estimate the frequency-dependent complex shear modulus of the network. In the active approach, we used an optical trap to oscillate an embedded microsphere and monitored the response in order to obtain network viscoelasticity over a physiologically relevant force range. While both active and passive measurements exhibit similar results at low strain, the F-actin network subject to high strain exhibits non-linear behavior which is analogous to the strain-hardening observed in macroscale measurements. Using confocal and total internal reflection fluorescent microscopy, we also characterize the microstructure of reconstituted F-actin networks in terms of filament length, mesh size and degree of bundling. Finally, we propose a model of network connectivity by investigating the effect of filament length on the mechanical properties and structure.

Indexed as

Actin CytoskeletonActinsAnimalsBiomechanical PhenomenaCross-Linking ReagentsElasticityGelsolinMicroscopy, ConfocalRabbitsRheologyActinsCross-Linking ReagentsGelsolin

Identifiers

PMID19883801
PMCPMC2830389
OpenAlexW1970512802

What OpenQuestion holds

Textmetadata
LicenceTDM
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.