Mechanics of Elastic Biomolecules 2003
DOI: 10.1007/978-94-010-0147-2_13
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Mechanics of vimentin intermediate filaments

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Cited by 72 publications
(85 citation statements)
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“…It is abundantly expressed in fibroblasts and endothelial cells 44 . We used this typical mesenchymal marker to evaluate its expression in the flat TC covering the deeper areas of fistulae.…”
Section: Vimentinmentioning
confidence: 99%
“…It is abundantly expressed in fibroblasts and endothelial cells 44 . We used this typical mesenchymal marker to evaluate its expression in the flat TC covering the deeper areas of fistulae.…”
Section: Vimentinmentioning
confidence: 99%
“…While, this is true for a micrometer long IF, when a bending stress is applied locally over a short length ∼250 nm then vimentin IFs reveal a five times higher bending modulus. 21 Hence, even if the vimentin IF network does not seem to strongly determine the global mechanical properties of the cytoskeleton at small strain, 36 and that due to the higher radius of MTs (25 nm) with respect to the one of IFs (10 nm), the bending stiffness of MTs is still higher than the one of IFs; our data still indicate that IFs assemblies can be stiff enough to be involve in localized mechanotransduction events as expected from, for example, their binding to focal adhesion sites via the integrin complex. 37 …”
Section: Ifs and The Cytoskeletonmentioning
confidence: 99%
“…According to 2-D gel analysis, 6 isoforms of vimentin were downregulated in kojic acid-treated A375 melanoma cells. It is well known that vimentin regulates cell migration, membrane trafficking, granular secretion, protein kinase activation and regulation of stress response proteins 48 . The modification of vimentin isoforms might be caused by phosphorylation, which has a central role in regulating the dynamics of vimentin assembly into polymers as well as in regulating the connections between intermediate filament (IF) and IF-associated proteins 49 .…”
Section: Discussionmentioning
confidence: 99%
“…Although one gene makes one protein, protein modifications leading to changes in biological and physiological functions may not be caused by gene modifications. To examine the effects of kojic acid on protein expression levels in A375 melanoma cells, the same concentration of kojic acid (8 μg/ml) as in the microarray study, which is compliant with the safety recommendation in human skin care products, and various treatment times (24,48 and 72 h) were used in this study. 2-D PAGE identified 30 differentially expressed proteins that showed a significant change in expression levels following 72 h of drug treatment.…”
Section: Discussionmentioning
confidence: 99%