Relevant bibliographies by topics / Cytoskeleton

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Cytoskeleton'

Author: Grafiati
Published: 4 June 2021
Last updated: 9 June 2025

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Journal articles on the topic "Cytoskeleton"

1

Smith, CM, SM Burris, GH Rao, and JG White. "Detergent-resistant cytoskeleton of the surface-activated platelet differs from the suspension-activated platelet cytoskeleton." Blood 80, no. 11 (December 1, 1992): 2774–80. http://dx.doi.org/10.1182/blood.v80.11.2774.2774.

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Abstract This study contrasts the protein composition of the detergent-resistant cytoskeleton of platelets fully spread on glass with the cytoskeletal composition of resting platelets and platelets aggregated in suspension with thrombin. Complete Triton X-100-insoluble cytoskeletons were isolated from spread, resting, and suspension-activated platelets in the presence of protease inhibitors, solubilized in sodium dodecyl sulfate/EDTA and analyzed on reduced, one-dimensional polyacrylamide gels. The protein composition of the cytoskeletons differed both qualitatively and quantitatively. Most notable were more extensive incorporation of total protein, talin, and vinculin into the cytoskeleton of spread platelets than the cytoskeleton of suspension- activated platelets. Varying the concentration and time of exposure to thrombin during suspension activation did not mimic the cytoskeletal changes of surface activation. Scanning electron microscopy, measurement of lipid phosphorus content, and varying the duration of Triton extraction did not show incomplete solubilization or nonspecific trapping of constituents in the spread platelet cytoskeleton. Proteolysis of talin was minimal in suspension-activated platelets and in platelets spread for 50 minutes. The differences in the detergent- resistant cytoskeletons of surface- and suspension-activated platelets indicate significant divergence in the physiologies of platelet spreading on surfaces and platelet activation in suspension.
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Smith, CM, SM Burris, GH Rao, and JG White. "Detergent-resistant cytoskeleton of the surface-activated platelet differs from the suspension-activated platelet cytoskeleton." Blood 80, no. 11 (December 1, 1992): 2774–80. http://dx.doi.org/10.1182/blood.v80.11.2774.bloodjournal80112774.

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This study contrasts the protein composition of the detergent-resistant cytoskeleton of platelets fully spread on glass with the cytoskeletal composition of resting platelets and platelets aggregated in suspension with thrombin. Complete Triton X-100-insoluble cytoskeletons were isolated from spread, resting, and suspension-activated platelets in the presence of protease inhibitors, solubilized in sodium dodecyl sulfate/EDTA and analyzed on reduced, one-dimensional polyacrylamide gels. The protein composition of the cytoskeletons differed both qualitatively and quantitatively. Most notable were more extensive incorporation of total protein, talin, and vinculin into the cytoskeleton of spread platelets than the cytoskeleton of suspension- activated platelets. Varying the concentration and time of exposure to thrombin during suspension activation did not mimic the cytoskeletal changes of surface activation. Scanning electron microscopy, measurement of lipid phosphorus content, and varying the duration of Triton extraction did not show incomplete solubilization or nonspecific trapping of constituents in the spread platelet cytoskeleton. Proteolysis of talin was minimal in suspension-activated platelets and in platelets spread for 50 minutes. The differences in the detergent- resistant cytoskeletons of surface- and suspension-activated platelets indicate significant divergence in the physiologies of platelet spreading on surfaces and platelet activation in suspension.
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Wiegant, F. A., F. J. Blok, L. H. Defize, W. A. Linnemans, A. J. Verkley, and J. Boonstra. "Epidermal growth factor receptors associated to cytoskeletal elements of epidermoid carcinoma (A431) cells." Journal of Cell Biology 103, no. 1 (July 1, 1986): 87–94. http://dx.doi.org/10.1083/jcb.103.1.87.

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The structural interaction of the epidermal growth factor (EGF) receptor and the cytoskeleton of A431 cells has been studied using a monoclonal anti-EGF receptor antibody. This has been done with immunogold labeling using a variety of electron microscopical preparation procedures and EGF binding studies. By providing an image of the membrane-associated cytoskeleton, the dry cleavage method reveals a preferential localization of EGF receptors superimposed upon cytoskeletal filaments. The colocalization of gold particles with cytoskeletal filaments is not affected when pre-labeled cells are extracted with the non-ionic detergent Triton X-100, as visualized by dry cleavage. Using surface replication, this treatment results in visualization of the cytoskeleton. In these latter preparations, it is also observed that EGF receptor-coupled gold particles remain associated with cytoskeletal elements. Moreover, Triton extraction performed before immunogold labeling of EGF receptors demonstrates that isolated cytoskeletons contained binding sites for anti-EGF receptor antibodies. Using stereo micrographs of replica's obtained from these isolated cytoskeletons, it is shown that gold-labeled EGF receptors are exclusively present on the cortical membrane-associated region of the cytoskeleton and not on more intracellular-located filaments. Scatchard analysis of EGF binding to cells fixed with glutaraldehyde and treated with Triton X-100 before and after EGF binding indicates that a high affinity EGF binding site is associated with the Triton X-100 insoluble cytoskeleton.
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Breuer, David, Alexander Ivakov, Arun Sampathkumar, Florian Hollandt, Staffan Persson, and Zoran Nikoloski. "Quantitative analyses of the plant cytoskeleton reveal underlying organizational principles." Journal of The Royal Society Interface 11, no. 97 (August 6, 2014): 20140362. http://dx.doi.org/10.1098/rsif.2014.0362.

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The actin and microtubule (MT) cytoskeletons are vital structures for cell growth and development across all species. While individual molecular mechanisms underpinning actin and MT dynamics have been intensively studied, principles that govern the cytoskeleton organization remain largely unexplored. Here, we captured biologically relevant characteristics of the plant cytoskeleton through a network-driven imaging-based approach allowing us to quantitatively assess dynamic features of the cytoskeleton. By introducing suitable null models, we demonstrate that the plant cytoskeletal networks exhibit properties required for efficient transport, namely, short average path lengths and high robustness. We further show that these advantageous features are maintained during temporal cytoskeletal rearrangements. Interestingly, man-made transportation networks exhibit similar properties, suggesting general laws of network organization supporting diverse transport processes. The proposed network-driven analysis can be readily used to identify organizational principles of cytoskeletons in other organisms.
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Bezanilla, Magdalena, Amy S. Gladfelter, David R. Kovar, and Wei-Lih Lee. "Cytoskeletal dynamics: A view from the membrane." Journal of Cell Biology 209, no. 3 (May 11, 2015): 329–37. http://dx.doi.org/10.1083/jcb.201502062.

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Many aspects of cytoskeletal assembly and dynamics can be recapitulated in vitro; yet, how the cytoskeleton integrates signals in vivo across cellular membranes is far less understood. Recent work has demonstrated that the membrane alone, or through membrane-associated proteins, can effect dynamic changes to the cytoskeleton, thereby impacting cell physiology. Having identified mechanistic links between membranes and the actin, microtubule, and septin cytoskeletons, these studies highlight the membrane’s central role in coordinating these cytoskeletal systems to carry out essential processes, such as endocytosis, spindle positioning, and cellular compartmentalization.
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Benoit, Béatrice, Anita Baillet, and Christian Poüs. "Cytoskeleton and Associated Proteins: Pleiotropic JNK Substrates and Regulators." International Journal of Molecular Sciences 22, no. 16 (August 4, 2021): 8375. http://dx.doi.org/10.3390/ijms22168375.

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This review extensively reports data from the literature concerning the complex relationships between the stress-induced c-Jun N-terminal kinases (JNKs) and the four main cytoskeleton elements, which are actin filaments, microtubules, intermediate filaments, and septins. To a lesser extent, we also focused on the two membrane-associated cytoskeletons spectrin and ESCRT-III. We gather the mechanisms controlling cytoskeleton-associated JNK activation and the known cytoskeleton-related substrates directly phosphorylated by JNK. We also point out specific locations of the JNK upstream regulators at cytoskeletal components. We finally compile available techniques and tools that could allow a better characterization of the interplay between the different types of cytoskeleton filaments upon JNK-mediated stress and during development. This overview may bring new important information for applied medical research.
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Wickstead, Bill, and Keith Gull. "The evolution of the cytoskeleton." Journal of Cell Biology 194, no. 4 (August 22, 2011): 513–25. http://dx.doi.org/10.1083/jcb.201102065.

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The cytoskeleton is a system of intracellular filaments crucial for cell shape, division, and function in all three domains of life. The simple cytoskeletons of prokaryotes show surprising plasticity in composition, with none of the core filament-forming proteins conserved in all lineages. In contrast, eukaryotic cytoskeletal function has been hugely elaborated by the addition of accessory proteins and extensive gene duplication and specialization. Much of this complexity evolved before the last common ancestor of eukaryotes. The distribution of cytoskeletal filaments puts constraints on the likely prokaryotic line that made this leap of eukaryogenesis.
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Jones, Steven L., and Tatyana M. Svitkina. "Axon Initial Segment Cytoskeleton: Architecture, Development, and Role in Neuron Polarity." Neural Plasticity 2016 (2016): 1–19. http://dx.doi.org/10.1155/2016/6808293.

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The axon initial segment (AIS) is a specialized structure in neurons that resides in between axonal and somatodendritic domains. The localization of the AIS in neurons is ideal for its two major functions: it serves as the site of action potential firing and helps to maintain neuron polarity. It has become increasingly clear that the AIS cytoskeleton is fundamental to AIS functions. In this review, we discuss current understanding of the AIS cytoskeleton with particular interest in its unique architecture and role in maintenance of neuron polarity. The AIS cytoskeleton is divided into two parts, submembrane and cytoplasmic, based on localization, function, and molecular composition. Recent studies using electron and subdiffraction fluorescence microscopy indicate that submembrane cytoskeletal components (ankyrin G,βIV-spectrin, and actin filaments) form a sophisticated network in the AIS that is conceptually similar to the polygonal/triangular network of erythrocytes, with some important differences. Components of the AIS cytoplasmic cytoskeleton (microtubules, actin filaments, and neurofilaments) reside deeper within the AIS shaft and display structural features distinct from other neuronal domains. We discuss how the AIS submembrane and cytoplasmic cytoskeletons contribute to different aspects of AIS polarity function and highlight recent advances in understanding their AIS cytoskeletal assembly and stability.
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Durand-Smet, Pauline, Tamsin A. Spelman, Elliot M. Meyerowitz, and Henrik Jönsson. "Cytoskeletal organization in isolated plant cells under geometry control." Proceedings of the National Academy of Sciences 117, no. 29 (July 8, 2020): 17399–408. http://dx.doi.org/10.1073/pnas.2003184117.

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The cytoskeleton plays a key role in establishing robust cell shape. In animals, it is well established that cell shape can also influence cytoskeletal organization. Cytoskeletal proteins are well conserved between animal and plant kingdoms; nevertheless, because plant cells exhibit major structural differences to animal cells, the question arises whether the plant cytoskeleton also responds to geometrical cues. Recent numerical simulations predicted that a geometry-based rule is sufficient to explain the microtubule (MT) organization observed in cells. Due to their high flexural rigidity and persistence length of the order of a few millimeters, MTs are rigid over cellular dimensions and are thus expected to align along their long axis if constrained in specific geometries. This hypothesis remains to be testedin cellulo. Here, we explore the relative contribution of geometry to the final organization of actin and MT cytoskeletons in single plant cells ofArabidopsis thaliana. We show that the cytoskeleton aligns with the long axis of the cells. We find that actin organization relies on MTs but not the opposite. We develop a model of self-organizing MTs in three dimensions, which predicts the importance of MT severing, which we confirm experimentally. This work is a first step toward assessing quantitatively how cellular geometry contributes to the control of cytoskeletal organization in living plant cells.
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Jack, R. M., R. M. Ezzell, J. Hartwig, and D. T. Fearon. "Differential interaction of the C3b/C4b receptor and MHC class I with the cytoskeleton of human neutrophils." Journal of Immunology 137, no. 12 (December 15, 1986): 3996–4003. http://dx.doi.org/10.4049/jimmunol.137.12.3996.

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Abstract As measured by fluorescence microscopy and radioligand binding, C3b/C4b receptors (CR1) became attached to the detergent-insoluble cytoskeleton of human neutrophils when receptors were cross-linked by affinity-purified polyclonal F(ab')2 anti-CR1, dimeric C3b, or Fab monoclonal anti-CR1 followed by F(ab')2 goat anti-mouse F(ab')2. CR1 on neutrophils bearing monovalent anti-CR1 was not attached to the cytoskeleton. In contrast, cross-linked CR1 on erythrocytes and cross-linked MHC Class I on neutrophils were not cytoskeleton associated. A possible role for filamentous actin (F-actin) in the binding of cross-linked CR1 to neutrophil cytoskeleton was suggested by three observations. When neutrophils were differentially extracted with either Low Salt-detergent buffer or High Salt-detergent buffer, stained with FITC-phalloidin, and examined by fluorescent flow cytometry, the residual cytoskeletons generated with the former buffer were shown to contain polymerized F-actin, whereas cytoskeletons generated with the latter buffer were found to be depleted of F-actin. In parallel experiments, High Salt-detergent buffer was also found to release cross-linked CR1 from neutrophils. Second, depolymerization of F-actin by DNAse I released half of the cytoskeletal-associated cross-linked CR1. Third, immunoadsorbed neutrophil CR1, but not MHC Class I or erythrocyte CR1, specifically bound soluble 125I-actin. In addition, Fc receptor and CR3, other phagocytic membrane proteins of neutrophils, specifically bound 125I-actin. These data demonstrate that CR1 cross-linked on neutrophils becomes associated with detergent-insoluble cytoskeleton and that this interaction is mediated either directly or indirectly by actin.
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Dissertations / Theses on the topic "Cytoskeleton"

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Morgan, Rachel E. "Is the Cytoskeleton Necessary for Viral Replication?" Digital Archive @ GSU, 2012. http://digitalarchive.gsu.edu/biology_theses/38.

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The cytoskeleton plays an important role in trafficking proteins and other macromolecular moieties throughout the cell. Viruses have been thought to depend heavily on the cytoskeleton for their replication cycles. However, studies, including one in our lab, found that some viruses are not inhibited by anti-microtubule drugs. This study was undertaken to evaluate the replication of viruses from several families in the presence of cytoskeleton-inhibiting drugs and to examine the intracellular localization of the proteins of one of these viruses, Sindbis virus, to test the hypothesis that alternate pathways are used if the cytoskeleton is inhibited. We found that Sindbis virus (Togaviridae, positive-strand RNA), vesicular stomatitis virus (Rhabdoviridae, negative-strand RNA), and Herpes simplex virus 1 (Herpesviridae, DNA virus) were not inhibited by these drugs, contrary to expectation. Differences in the localization of the Sindbis virus were observed, suggesting the existence of alternate pathways for intracellular transport.
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McDermott, Joshua D. "The ovine lens cytoskeleton." Lincoln University, 2007. http://hdl.handle.net/10182/700.

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The lens of the eye is a vital tissue in the visual system, responsible for the collection and focusing of light on to the retina. Comprised of epithelial cells at differing stages of differentiation, the transparency of the lens is dependent on the highly ordered crystalline structure of lens proteins. The lens consists of several proteins including crystallins (α, β, γ) that make up 90% of the soluble protein, and the lens cytoskeletal proteins. Cytoskeletal proteins contribute only a fraction of the total lens protein, but are thought to play an important role in the establishment and maintenance of transparency. Calpain-induced degradation of these proteins may be involved in the development of cataracts. This has been an area of research at Lincoln University where a flock of sheep genetically predisposed to cataract maintained as a cataract development model. The aim of this research was to investigate the distribution of cytoskeletal proteins in the lens, and to examine the effects of calpain proteolysis on these proteins, with the goal of establishing the role of the lens cytoskeletal proteins in the ovine cataract model. A combination of techniques was used including immunohistochemistry, which required the development of a specific protocol for ovine lenses. Cytoskeletal proteins were identified using immunohistochemistry in lens tissue sections and exhibited characteristic distributions. Actin displayed preferential distribution in the short sides of the fibre cells in the cortex of the lens but was absent in the lens nucleus, while spectrin in the cortex and nucleus was associated with the fibre cell membrane. Filensin was observed in the outer cortex of lens sections associated with the fibre cell membrane and cytoplasm, although the pattern of localisation was indistinct due to the abundance of filensin breakdown products. Vimentin displayed membrane and cytoplasmic association in the outer cortex that diminished toward the lens nucleus, with membrane associated vimentin only persisting in the deeper regions of the cortex and nucleus. Additionally, the effect of novel calpain inhibitors (Cat0059 and Cat811) in preventing proteolysis of lens cytoskeletal protein was investigated and compared with calpain inhibitors developed elsewhere (SJA6017). The inhibitors were tested at between 10 and 0.1 μM (100 nM). All inhibitors were effective at 10 μM. SJA6017 provided significant protection to vimentin at 1 μM. Cat0059 was found to protect spectrin and filensin at 1 μM, but not vimentin, while inhibitor Cat811 was found to protect spectrin only. SJA6017 added to assays at 100 nM offered significant protection to spectrin, and Cat0059 was found to protect filensin and spectrin to a significant degree at 100 nM, indicating the novel inhibitors were comparable to those developed elsewhere in terms of their effectiveness. Taken together, the evidence presented in this thesis shows the cytoskeletal proteins as crucial elements in the lens. Their pervasive presence coupled with evidence that lens cytoskeletal proteins are sensitive to calpain-induced proteolysis that is inhibited with novel calpain inhibitors suggests that the lens cytoskeletal proteins may be useful targets in cataract prevention for future research.
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Snyder, Heidi Ghent. "Fiber type-specific desmin content in human single muscle fibers /." Diss., CLICK HERE for online access, 2006. http://contentdm.lib.byu.edu/ETD/image/etd1253.pdf.

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Fawell, E. H. "Studies on the microvillus cytoskeleton." Thesis, University of Leeds, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.355700.

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Schneider, André. "The cytoskeleton of Trypanosoma brucei /." [S.l.] : [s.n.], 1988. http://www.ub.unibe.ch/content/bibliotheken_sammlungen/sondersammlungen/dissen_bestellformular/index_ger.html.

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McCarthy, David James. "Analysis of the novel Lyn-associated cytoskeletal modular protein, LACM." University of Western Australia. School of Medicine and Pharmacology, 2009. http://theses.library.uwa.edu.au/adt-WU2009.0180.

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A yeast-two hybrid screen with Lyn identified a novel 130 kDa multidomain protein with a 36% identity to Actin Filament Associated Protein (AFAP) 110 and similar domains, including PH domains, potential sites of tyrosine and serine/threonine phosphorylation, a leucine-zipper domain, a potential actin binding site and multimerization site. AFAP110 has been shown to have a role in modulating actin filament integrity and induce lamellipodia formation, and is known to interact with Src family kinases. The aim of this thesis was to characterize this novel protein named Lyn-Associated Cytoskeletal Modulator (LACM) and determine any molecular interactions in order to attempt to elucidate a role for the protein in cell signaling through Lyn. LACM is encoded by a gene consisting of 18 exons and is located on human chromosome 5q33.1 and mouse chromosome 18 E1. LACM protein is expressed through a number of cell types including the R11 erythroid cell line, and mouse tissues including brain, lung, heart and embryos. LACM was shown to multimerize, and subcellular localization of the protein was observed to concentrate around the cell membrane at sites of filamentous actin in filopodia, lamellipodia and stress fibres. The carboxy-terminus of LACM was observed to localize the protein to sites at the cell membrane and through the cytoplasm. Removal of this terminal region resulted in all LACM protein localizing to the nucleus in punctuate spots. LACM protein was observed in heart muscle and potentially has a role at sites of nerve junctions on cardiac myocytes. LACM was shown to interact with the SH3 domain of Lyn at a polyproline motif on LACM. LACM was observed to co-localize and co-immunoprecipitate with Lyn and was tyrosine phosphorylated by the kinase domain of Lyn. Interestingly, the consititutively active Lyn and LACM caused transfected cells to
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Tharmann, Rainer. "Mechanical properties of complex cytoskeleton networks." [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=97998002X.

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Brown, Jennifer. "Investigating the actin cytoskeleton in cancer." Thesis, University of Glasgow, 2016. http://theses.gla.ac.uk/7266/.

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Dynamic alterations in the actin cytoskeleton, under the regulation of the Rho/ROCK pathway, permit cell motility, cell-to-cell and cell-to-matrix adhesion, and have also been shown to participate in apoptosis and cell proliferation. These facets of cellular behaviour all have the capacity to become dysregulated in cancer; components of the Rho/ROCK pathway are known to play varying roles in these processes, both within primary tumours and within the tumour microenvironment. The LIM kinases are phosphorylated and activated by ROCK, leading to inactivation of cofilin and subsequent stabilisation of actin filaments. In addition, LIM kinase 2 serves as a p53 target and is upregulated in response to DNA damage. In some solid tumours (e.g. breast and prostate), LIM kinase levels are elevated. However, we found that LIM kinase 2 expression is downregulated in colon cancer, with a progressive reduction noted with advancing tumour stage. I found that LIMK2 expression in colon cancer is under epigenetic regulation, with hypermethylation of the promoters leading to transcriptional silencing; this implicates LIMK2 as a tumour suppressor gene in this context. This has potential translational implications as loss of LIMK2 could be utilised as a biomarker to stratify patients in the future. Elevated mechanical tension within the tumour microenvironment is known to be an adverse prognostic indicator due to its association with desmoplasia. ROCK activation has previously been shown to increase epidermal tissue stiffness and thickness, but little was known about the mechanisms by which this occurs. I found that ROCK activation leads to the deposition of extracellular matrix components, with a presumed consequent further increase in stromal stiffness. This indicates that a positive feedback cycle is established in the tumour microenvironment, maintaining a fibrotic stromal reaction that permits tumour progression. These results highlight the disparate roles that the actin cytoskeleton and constituents of the Rho/ROCK pathway play in tumour initiation and propagation, indicating the need for further research.
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Balanda, Matthew L. "The use of cytoskeletal inhibitors to determine the role of the cytoskeleton in the activation of hypertonicity-induced currents in xenopus oocytes /." View abstract, 1999. http://library.ctstateu.edu/ccsu%5Ftheses/1561.html.

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Thesis (M.A.)--Central Connecticut State University, 1999.<br>Thesis advisor: Kathy Martin. " ... in partial fulfillment of the requirements for the degree of Master of Arts in Biological Sciences." Includes bibliographical references (leaves 42-44).
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Huber, Florian. "Emergent structure formation of the actin cytoskeleton." Doctoral thesis, Universitätsbibliothek Leipzig, 2012. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-86666.

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Anders als menschengemachte Maschinen verfügen Zellen über keinen festgeschriebenen Bauplan und die Positionen einzelner Elemente sind häufig nicht genau festgelegt, da die Moleküle diffusiven Zufallsbewegungen unterworfen sind. Darüber hinaus sind einzelne Bauteile auch nicht auf eine einzelne Funktion festgelegt, sondern können parallel in verschiedene Prozesse einbezogen sein. Basierend auf Selbstorganisation und Selbstassemblierung muß die Organisation von Anordnung und Funktion einer lebenden Zelle also bereits in ihren einzelnen Komponenten inhärent enthalten sein. Die intrazelluläre Organisation wird zum großen Teil durch ein internes Biopolymergerüst reguliert, das Zytoskelett. Biopolymer-Netzwerke und –Fasern durchdringen die gesamte Zelle und sind verantworlich für mechanische Integrität und die funktionale Architektur. Unzählige essentielle biologische Prozesse hängen direkt von einem funktionierenden Zytoskelett ab. Die vorliegende Arbeit zielt auf ein besser Verständnis und den Nachbau zweier verschiedener funktionaler Module lebender Zellen anhand stark reduzierter Modellsysteme. Als zentrales Element wurde Aktin gewählt, da dieses Biopolymer eine herausragende Rolle in nahezu allen eukaryotischen Zellen spielt. Mit dem ersten Modellsystem wird der bewegliche Aktin-Polymerfilm an der Vorderkante migrierender Zellen betrachtet. Die wichtigsten Elemente dieser hochdynamischen Netzwerke sind bereits bekannt und wurden in dieser Arbeit benutzt um ein experimentelles Modellsystem zu etablieren. Vor allem aber lieferten detailierte Computersimulationen und ein mathematisches Modell neue Erkenntnisse über grundlegende Organisationsprinzipien dieser Aktinnetzwerke. Damit war es nicht nur möglich, experimentelle Daten erfolgreich zu reproduzieren, sondern das Entstehen von Substrukturen und deren Charakteristika auf proteinunabhängige, generelle Mechanismen zurückzuführen. Das zweite studierte System betrachtet die Selbstassemblierung von Aktinnetzwerken durch entropische Kräfte. Aktinfilamente aggregieren hierbei durch Kondensation multivalenter Ionen oder durch Volumenausschluss hochkonzentrierter inerter Polymere. Ein neu entwickelter Experimentalaufbau bietet die Möglichkeit in gut definierten zellähnlichen Volumina, Konvektionseinflüsse zu umgehen und Aggregationseffekte gezielt einzuschalten. Hierbei wurden neuartige, regelmäßige Netzwerkstrukturen entdeckt, die bislang nur im Zusammenhang mit molekularen Motoren bekannt waren. Es konnte ferner gezeigt werden, dass die Physik der Flüssigkristalle entscheidend zu weiteren Variationen dieser Netzwerke beiträgt. Dabei wird ersichtlich, dass entstehende Netzwerke in ihrer Architektur direkt die zuvor herrschenden Anisotropien der Filamentlösung widerspiegeln.
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Books on the topic "Cytoskeleton"

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Bishr, Omary M., and Coulombe Pierre A, eds. Intermediate filament cytoskeleton. San Diego: Elsevier Academic Press, 2004.

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Gavin, Ray H., ed. Cytoskeleton. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1661-1.

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Bershadsky, Alexander D., and Juri M. Vasiliev. Cytoskeleton. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5278-5.

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M, Vasilʹev I͡U︡, ed. Cytoskeleton. New York: Plenum Press, 1988.

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Dermietzel, Rolf, ed. The Cytoskeleton. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-266-7.

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Clarkson, Thomas W., Polly R. Sager, and Tore L. M. Syversen, eds. The Cytoskeleton. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2161-3.

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Maiato, Helder, ed. Cytoskeleton Dynamics. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0219-5.

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Sahi, Vaidurya Pratap, and František Baluška, eds. The Cytoskeleton. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-33528-1.

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Schliwa, Manfred. The Cytoskeleton. Vienna: Springer Vienna, 1985. http://dx.doi.org/10.1007/978-3-7091-7667-2.

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Isenberg, Gerhard. Cytoskeleton Proteins. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79632-6.

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Book chapters on the topic "Cytoskeleton"

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Lima-de-Faria, A. "Cytoskeleton." In One Hundred Years of Chromosome Research and What Remains to be Learned, 91–92. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-017-0167-9_20.

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Rivero, Francisco, and Huajiang Xiong. "Cytoskeleton." In Encyclopedia of Cancer, 1–9. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_1491-9.

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Rovensky, Yury A. "Cytoskeleton." In Adhesive Interactions in Normal and Transformed Cells, 13–35. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-304-2_3.

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Mehlhorn, Heinz. "Cytoskeleton." In Encyclopedia of Parasitology, 645. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-43978-4_813.

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Kalmar, Jayne M., Brigid M. Lynch, Christine M. Friedenreich, Lee W. Jones, A. N. Bosch, Alessandro Blandino, Elisabetta Toso, et al. "Cytoskeleton." In Encyclopedia of Exercise Medicine in Health and Disease, 229. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_12282.

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Rivero, Francisco, and Huajiang Xiong. "Cytoskeleton." In Encyclopedia of Cancer, 1294–303. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-46875-3_1491.

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Mehlhorn, Heinz. "Cytoskeleton." In Encyclopedia of Parasitology, 1–2. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27769-6_813-2.

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French, Samuel W., Monique Cadrin, Hiromu Kawahara, and Kazutomo Kachi. "Cytoskeleton." In Molecular & Cell Biology of the Liver, 143–80. Boca Raton: CRC Press, 2024. https://doi.org/10.1201/9781003575160-8.

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Bershadsky, Alexander D., and Juri M. Vasiliev. "Introduction." In Cytoskeleton, 1–10. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5278-5_1.

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Bershadsky, Alexander D., and Juri M. Vasiliev. "Neoplastic Transformations." In Cytoskeleton, 267–83. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5278-5_10.

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Conference papers on the topic "Cytoskeleton"

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Liu, Yi, and Juan Ren. "Modeling and Control of Dynamic Cellular Mechanotransduction: Part I — Actin Cytoskeleton Quantification." In ASME 2018 Dynamic Systems and Control Conference. American Society of Mechanical Engineers, 2018. http://dx.doi.org/10.1115/dscc2018-9180.

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Living cells respond to external stimuli through the reorganization of the actin cytoskeleton, and the actin cytoskeleton significantly affects the cellular mechanical behavior. However, due to the lack of approaches to actin cytoskeleton quantification, the dynamics of mechanotransduction is still poorly understood. In this study, we propose an image recognition-based quantification (IRQ) approach to actin cytoskeleton quantification. IRQ quantifies the actin cytoskeleton through three parameters: the partial actin-cytoskeletal deviation (PAD), the total actin-cytoskeletal deviation (TAD) and the average actin-cytoskeletal intensity (AAI). First, Canny and Sobel edge detectors are applied to skeletonize the actin cytoskeleton images, then PAD and TAD are quantified using the direction of lines detected by Hough transform, and AAI is calculated through the summational brightness over the detected cell area. For validation, six different actin cytoskeleton meshwork models were generated to verify the quantification accuracy of IRQ. The average error for both the quantified PAD and TAD was less than 1.22°. Then IRQ was implemented to quantify the actin cytoskeleton of NIH/3T3 cells treated with an F-actin inhibitor. The quantification results suggest that the local and total actin-cytoskeletal organization of treated cells were more disordered than untreated cells, and the quantity of the actin cytoskeleton decreased significantly after the F-actin treatment.
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Horvåth, A., G. M. Asyee, A. Sturk, and L. Muszbek. "ASSOCIATION OF VINCULIN TO THE PLATELET CYTOSKELET0N DURING RELEASE REACTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643901.

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Vinculin is an Mr 130 kD protein, which in various cell types is located at the membrane attachment site of microfilaments and has been implicated in membrane-cytoskeleton interaction. Though we have previously verified its presence in platelets and showed that in resting platelets it is localized submembra-neously and around the ±-granules, its relation to the cytos-keleton is still to be elucidated. It has been also revealed by biochemical studies that in resting bovine gel filtered platelets vinculin is not cytoskeletal component, however about 50% of the total vinculin content became incorporated into the cytoskeleton during thrombin activation. To establish if its association to the cytoskeleton occured during pseudopode formation, aggregation or release reaction, cytoskeletons were prepared from platelets activated in various conditions and the time course of vinculin incorporation was analyzed by immuno-blotting. When pseudopode formation was inhibited by cytochalasin B pretreatment but neither aggregation nor release reaction induced by thrombin was prevented, the amount of vinculin in the Triton insoluble residue even increased. Phorbol myristate acetate (PMA), which induces pseudopode but not contractile gel formation, is a strong stimulus for aggregation, but induces only a slight release of the granule content. In parallel, only a low amount of vinculin was recovered in the cytoskeletal fraction following PMA induced aggregation. In contrast, when release reaction elicited by thrombin occured in the absence of aggregation the association of vinculin did not diminished.The results clearly demonstrate, that platelet shape change and pseudopode formation are not prerequisites of the incorporation of vinculin into the cytoskeleton, which occurs parallel to the release reaction.
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Kiran, Kranthi, Sanjay Govindjee, and Mohammad R. K. Mofrad. "On the Cytoskeleton and Soft Glassy Rheology." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176736.

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Cytoskeleton is an integrated system of biomolecules, providing the cell with shape, integrity, and internal spatial organization. Cytoskeleton is a three-dimensional (3-D) network consisting of a complex mixture of actin filaments, intermediate filaments and microtubules that are collectively responsible for the main structural properties and motilities of the cell. A wide range of theoretical models have been proposed for cytoskeletal mechanics, ranging from continuum models for cell deformation to actin filament-based models for cell motility [1]. Numerous experimental techniques have also been developed to quantify cytoskeletal mechanics, typically involving a mechanical perturbation to the cell in the form of either an imposed deformation or force and observation of the static and dynamic response of the cell. These experimental measurements along with new theoretical approaches have given rise to several theories for describing the mechanics of living cells, modeling the cytoskeleton as a simple mechanical elastic, viscoelastic, or poro-viscoelastic continuum, tensegrity (tension integrity) network incorporating discrete structural elements that bear compression, porous gel or most recently soft glassy material. In this paper, we will revisit cytoskeleton as a soft glassy material and give insights in to new dynamic relationships for cytoskeleton.
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Wen, Shin-Min, and Pen-hsiu Grace Chao. "Spatial Actin Structure Does Not Correlate With Nuclear Organization." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14167.

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Cells in situ exhibit a great variety of morphologies that intimately relates to phenotypic controls. Cell morphology regulates cytoskeletal organization, which in turn influences nuclear shape and organization [1–4]. The actomyosin cytoskeleton is connected to a structure known as the linker of nucleoskeleton and cytoskeleton (LINC) complex located on the nuclear membrane. LINC is believed to transmit deformation of the actin cytoskeleton into the nucleus and nucleoskeleton, change nuclear shape as well as chromatin conformation, and modulate gene expression [5, 6]. Khatau and coworkers reported a structure of apical actin dome, called the actin cap, that controls nuclear deformation through LINC [7]. In addition, actin stress fibers hves been shown to compress the nucleus laterally and increase chromatin condensation [4]. Based on these findings, we hypothesize that there is a spatial correlation between the actin cytoskeleton and chromatin density. In the current study, we investigated the role of actin cytoskeleton in nuclear deformation with respect to the z-axis. We found no spatial relationships between actin structure and nuclear deformation or chromatin condensation, suggesting that the actomyosin cytoskeleton acts globally to influence nuclear structure and additional structural components may contribute to the actin-nucleus mechanical coupling.
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Pryse, Kenneth M., Teresa M. Abney, Guy M. Genin, and Elliot L. Elson. "Probing Cytoskeletal Mechanics Using Biochemical Inhibitors." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19451.

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Quantifying the mechanics of the cytoskeletons of living cells is important for understanding several physiologic and pathologic cellular functions, such as wound healing and cellular migration in cancer. Our laboratory develops three-dimensional tissue constructs for assaying cytoskeletal mechanics in controlled conditions. These tissue constructs consist of defined components such as chick embryo fibroblasts and reconstituted rat tail collagen; fibroblasts remodel the collagen extracellular matrix (ECM) and develop a structural environment representative of that which would exist in a natural tissue. Our protocol for quantifying the microscale mechanics of the proteins that comprise the cytoskeleton involves mechanical testing of a tissue construct first in a bath that contains nutrition medium to support the active physiologic functioning of the cells, and next in the presence of inhibitors that selectively eliminate specific cytoskeletal structures. By solving an inverse homogenization problem, the mechanical functioning of these proteins at the cellular level can be estimated. Here, we present a combination of mechanical testing and imaging results to quantify the effects of specific inhibitors on cytoskeletal and extracellular matrix form and function.
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Oswald, Elizabeth S., Pen-hsiu Grace Chao, J. Chloe Bulinski, Gerard A. Ateshian, and Clark T. Hung. "The Role of Microtubule Organization in Chondrocyte Response to Osmotic Loading." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176634.

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The cytoskeleton, including actin filaments and microtubules, provides chondrocytes with structure, cytoplasmic organization, and intracellular transport. The cytoskeleton is known to be involved in cellular responses to physiologic mechanical and osmotic loading signals, including morphological changes and mechanostransduction [1, 2]. Here, we examine microtubule (MT) involvement in volume response of chondrocytes to osmotic loading, as well as organization of stable MT with hypoosmotic loading. We also explore the hypothesis that chondrocytes from different zones of cartilage possess cytoskeletons with different properties, which help explain variations in their volume response to osmotic loading in situ and in vitro [3].
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Dutta, Surjendu Bikash, Anders Kokkvoll Engdahl, Stefan Belle, Wolfgang Hübner, Mark Schüttpelz, Thomas Huser, and Francesco Dell'Olio. "Waveguide chip based super-resolution microscopy for T cell imaging." In Integrated Photonics Research, Silicon and Nanophotonics. Washington, D.C.: Optica Publishing Group, 2022. http://dx.doi.org/10.1364/iprsn.2022.itu1b.6.

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Imaging and the quantitative estimation of T cell actin cytoskeletal dynamics are important to describe immunological processes. This study presents waveguide chip based super-resolution imaging of the filamentous actin cytoskeleton of Jurkat T cells.
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Dangaria, Jhanvi H., and Peter J. Butler. "Interaction of Shear Stress, Myosin II, and Actin in Dynamic Modulation of Endothelial Cell Microrheology." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192947.

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The endothelial cell (EC) cytoskeleton mediates several biological functions such as adhesion, migration, phagocytosis, cell division, and mechanosensitivity. These functions are carried out in part through dynamic cytoskeletal polymerization, modulation of crosslinking, and development of tension between intracellular organelles and the extracellular matrix via focal adhesion plaques. One important component of the cytoskeleton is actin which polymerizes into filaments and is thought to be prestressed by virtue of crosslinking proteins such as α-actinin, filamin and myosin II molecular motors. Additionally, actomyosin interaction has been hypothesized to act as a stress dissipation mechanism by virtue of dynamic crossbridging which facilitates actin diffusion through the polymer network of the cytoplasm (Humphrey et al., 2002).
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Sturm, Deborah, Mahdi Jawad, Alejandra Alonso, and Chris Corbo. "A cytoskeleton linearity measure." In 2012 IEEE Southwest Symposium on Image Analysis & Interpretation (SSIAI). IEEE, 2012. http://dx.doi.org/10.1109/ssiai.2012.6202449.

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Shin, Daehwan, John Schmitz, Tim Lee, and Kyriacos Athanasiou. "Substrate Effects on the Intrinsic Mechanical Properties of Individual Cells." In ASME 1997 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 1997. http://dx.doi.org/10.1115/imece1997-0285.

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Abstract Cells interact with specific molecular components of the extracellular matrix via cell surface receptors [1]. The principal cell surface receptors that mediate cell-extracellular matrix interactions are termed integrins [2, 3]. Integrins are transmembrane receptors that interact with several intracellular proteins, including elements of the cytoskeleton by cytoplasmic domains. Therefore, integrins serve as a molecular linkage between the extracellular matrix and the cytoskeleton. Some investigators have suggested that many of these vital cellular activities are regulated, at least in part, by intercellular and intracellular forces that are generated by a continuous molecular connection that includes components of the extracellular matrix, integrins, and cytoskeletal elements (i.e., f-actin, microtubules). It is believed that individual cells “sense” and generate forces transmitted through the extracellular environment by these intricate linkages [4]. Furthermore, this linkage, referred to as the “extended cytoskeleton,” could provide a mechanical signaling mechanism that may underlie many vital cellular activities, including gene expression. It is apparent that the physical properties of a cell may also be affected by this mechanism. Thus, cells grown on different extracellular matrix substrates should be expected to vary their cytoskeletal architecture and have concomitant changes in their biomechanical properties. The objectives of this study were 1) to obtain the intrinsic material properties of the individual cell as a function of the type of substrate matrix and therefore, 2) to investigate fundamental aspects of the response mechanism of individual cells to alterations in their biophysical environment.
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Reports on the topic "Cytoskeleton"

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Sadot, Einat, Christopher Staiger, and Zvi Kam Weizmann. functional genomic screen for new plant cytoskeletal proteins and the determination of their role in actin mediated functions and guard cells regulation. United States Department of Agriculture, January 2003. http://dx.doi.org/10.32747/2003.7587725.bard.

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The original objectives of the approved proposal were: 1. To construct a YFP fused Arabidopsis cDNA library in a mammalian expression vector. 2. To infect the library into a host fibroblast cell line and to screen for new cytoskeletal associated proteins using an automated microscope. 3. Isolate the new genes. 4. Characterize their role in plants. The project was approved as a feasibility study to allow proof of concept that would entail building the YFP library and picking up a couple of positive clones using the fluorescent screen. We report here on the construction of the YFP library, the development of the automatic microscope, the establishment of the screen and the isolation of positive clones that are plant cDNAs encoding cytoskeleton associated proteins. The rational underling a screen of plant library in fibroblasts is based on the high conservation of the cytoskeleton building blocks, actin and tubulin, between the two kingdoms (80-90% homology at the level of amino acids sequence). In addition, several publications demonstrated the recognition of mammalian cytoskeleton by plant cytoskeletal binding proteins and vice versa. The major achievements described here are: 1. The development of an automated microscope equipped with fast laser auto-focusing for high magnification and a software controlling 6 dimensions; X, Y position, auto focus, time, color, and the distribution and density of the fields acquired. This system is essential for the high throughput screen. 2. The construction of an extremely competent YFP library efficiently cloned (tens of thousands of clones collected, no empty vectors detected) with all inserts oriented 5't03'. These parameters render it well representative of the whole transcriptome and efficient in "in-frame" fusion to YFP. 3. The strategy developed for the screen allowing the isolation of individual positive cDNA clones following three rounds of microscopic scans. The major conclusion accomplished from the work described here is that the concept of using mammalian host cells for fishing new plant cytoskeletal proteins is feasible and that screening system developed is complete for addressing one of the major bottlenecks of the plant cytoskeleton field: the need for high throughput identification of functionally active cytoskeletal proteins. The new identified plant cytoskeletal proteins isolated in the pilot screen and additional new proteins which will be isolated in a comprehensive screen will shed light on cytoskeletal mediated processes playing a major role in cellular activities such as cell division, morphogenesis, and functioning such as chloroplast positioning, pollen tube and root hair elongation and the movement of guard cells. Therefore, in the long run the screen described here has clear agricultural implications.
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Trent, J. D., H. K. Kagawa, Takuro Yaoi, E. Olle, and N. J. Zaluzec. Chaperonin filaments: The archael cytoskeleton. Office of Scientific and Technical Information (OSTI), August 1997. http://dx.doi.org/10.2172/510354.

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Trent, J. D., H. K. Kagawa, and N. J. Zaluzec. Chaperonin polymers in archaea: The cytoskeleton of prokaryotes? Office of Scientific and Technical Information (OSTI), July 1997. http://dx.doi.org/10.2172/505321.

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Bresnick, Anne R. Mtsl: A Molecular Link Between the Cytoskeleton and Breast Tumor Metastasis. Fort Belvoir, VA: Defense Technical Information Center, July 2002. http://dx.doi.org/10.21236/ada408099.

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Ramesh, Vijaya. Neurofibromatosis 2 Tumor Suppressor Protein, Merlin, in Cellular Signaling to Actin Cytoskeleton. Fort Belvoir, VA: Defense Technical Information Center, October 2000. http://dx.doi.org/10.21236/ada395581.

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Bourguignon, Lilly Y. W. A New Invasion and Metastasis Molecule, Tiam1 and its Interaction with the Cytoskeleton are Involved in Human Breast Cancer Progression. Fort Belvoir, VA: Defense Technical Information Center, August 2001. http://dx.doi.org/10.21236/ada396857.

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Bourguignon, Lilly Y. A New Invasion and Metastasis Molecule, Tiaml and Its Interaction With the Cytoskeleton Are Involved in Human Breast Cancer Progression. Fort Belvoir, VA: Defense Technical Information Center, August 2000. http://dx.doi.org/10.21236/ada392244.

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Bourguignon, Lilly Y. A New Invasion and Metastasis Molecule, TIAMI1, and Its Interaction with the Cytoskeleton are Involved in Human Breast Cancer Progression. Fort Belvoir, VA: Defense Technical Information Center, August 1999. http://dx.doi.org/10.21236/ada376471.

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Syed, Aleem. Spatial and temporal dynamics of receptor for advanced glycation endproducts, integrins, and actin cytoskeleton as probed with fluorescence-based imaging techniques. Office of Scientific and Technical Information (OSTI), January 2016. http://dx.doi.org/10.2172/1342583.

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Stoyanova, Tihomira, Veselina Uzunova, Albena Momchilova, Rumiana Tzoneva, and Iva Ugrinova. The Treatment of Breast Cancer Cells with Erufosine Leads to Actin Cytoskeleton Reorganization, Inhibition of Cell Motility, Cell Cycle Arrest and Apoptosis. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, January 2021. http://dx.doi.org/10.7546/crabs.2021.01.11.

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