The Role of Vimentin Intermediate Filaments in Cortical and Cytoplasmic Mechanics
Ming Guo,Allen J. Ehrlicher,Allen J. Ehrlicher,Saleemulla Mahammad,Hilary Fabich,Mikkel H. Jensen,Mikkel H. Jensen,Jeffrey R. Moore,Jeffrey J. Fredberg,Robert D. Goldman,David A. Weitz +10 more
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Studying mouse embryonic fibroblasts derived from wild-type or vimentin(-/-) mice shows that VIFs both increase the mechanical integrity of cells and localize intracellular components.About:
This article is published in Biophysical Journal.The article was published on 2013-10-01 and is currently open access. It has received 230 citations till now. The article focuses on the topics: Cytoskeleton & Intermediate filament.read more
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Microrheology for Hi-C Data Reveals the Spectrum of the Dynamic 3D Genome Organization
TL;DR: It is shown that biologically relevant boundaries between chromatin domains are more rigid than the inside at a particular time scale, which allows interpretation of static and population-averaged genome conformation data as dynamic and hierarchical 3D genome picture.
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TIS21/BTG2 inhibits doxorubicin-induced stress fiber-vimentin networks via Nox4-ROS-ABI2-DRF-linked signal cascade.
TL;DR: TIS21 attenuated Doxo-induced cancer cell senescence by inhibitinglinear actin nucleation via Nox4-ROS-ABI2-DRF signal cascade, implying that expression of TIS21 overcomes resistance of senescent cells to cancer chemotherapy via inhibiting linear actinucleation.
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A silk purse from a sow's ear — bioinspired materials based on α-helical coiled coils
TL;DR: This past few years have heralded remarkable times for intermediate filaments with new revelations of their structural properties that has included the first crystallographic-based model of vimentin to build on the experimental data of intra-filament interactions determined by chemical cross-linking.
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Vimentin protects the structural integrity of the nucleus and suppresses nuclear damage caused by large deformations
Alison E. Patteson,Alison E. Patteson,Amir Vahabikashi,Katarzyna Pogoda,Katarzyna Pogoda,Stephen A. Adam,Anne E. Goldman,Robert D. Goldman,Paul A. Janmey +8 more
TL;DR: The results show that loss of VIFs alters nuclear shape, reduces perinuclear stiffness, and enhances motility in 3D, which increases nuclear rupture and activation of DNA damage repair mechanisms, which are rescued by exogenous re-expression of vimentin.
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Mitochondrial DNA 3243A>G heteroplasmy is associated with changes in cytoskeletal protein expression and cell mechanics.
Judith Kandel,Martin Picard,Martin Picard,Douglas C. Wallace,Douglas C. Wallace,David M. Eckmann +5 more
TL;DR: The transcriptional and structural regulation of cytoskeletal components by mitochondrial function may explain why energetic and mechanical alterations often coexist in clinical conditions.
References
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Cell mechanics and the cytoskeleton
TL;DR: An important insight emerging from this work is that long-lived cytoskeletal structures may act as epigenetic determinants of cell shape, function and fate.
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Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus
TL;DR: The molecular mechanisms by which forces might act at a distance to induce mechanochemical conversion in the nucleus and alter gene activities are explored.
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Scaling the microrheology of living cells.
Ben Fabry,Geoffrey N. Maksym,James P. Butler,Michael Glogauer,Daniel Navajas,Jeffrey J. Fredberg +5 more
TL;DR: A scaling law is reported that governs both the elastic and frictional properties of a wide variety of living cell types, over a wide range of time scales and under a variety of biological interventions, and implies that cytoskeletal proteins may regulate cell mechanical properties mainly by modulating the effective noise temperature of the matrix.
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Nonequilibrium mechanics of active cytoskeletal networks.
Daisuke Mizuno,Catherine Tardin,Christoph F. Schmidt,Christoph F. Schmidt,Fred C. MacKintosh +4 more
TL;DR: A quantitative theoretical model is presented connecting the large-scale properties of this active gel to molecular force generation and qualitatively changing the viscoelastic response of the network in an adenosine triphosphate–dependent manner.