Titlebook: Cell and Muscle Motility; Robert M. Dowben,Jerry W. Shay Book 1981 Plenum Press, New York 1981 Volume.biology.boundary element method.card

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Lars Willnat,Ven-hwei Lo,Annette Aw observed by electron and immunofluorescence miscroscopy as a loss of large bundles of actin microfilaments called “stress fibers.” Recent technical innovations for visualizing the cytoskeleton have revealed that actin structure in normal fibroblasts is much more complex than was originally supposed

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Fine-Structural and Related Aspects of Nonmuscle-Cell Motility,toplasmic ground substance. Then, since a better understanding of the microtubule-dynein and muscle-cell systems required identification of the proteins in their interacting components, it is planned to outline what is known at present of the protein identities of the various filamentous elements of

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The Role of Intermediate (10-nm) Filaments in the Development and Integration of the Myofibrillar Cion is unresolved at present. The intermediate filaments were initially regarded as a disaggregation, or degradation product, or myosin and/or microtubules and thus until recently attracted little attention. Current biochemical and immunofluorescent methods have established the intermediate filament

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Polymorphic Assemblies of Tubulin,s of binding interactions between dimers and possible conformational states of the molecule. The kinds of structures that can be formed, and their stability, can provide clues to the tubulin polymorphs that may exist . in normal and diseased or aged cells, even though there is always uncertainty ass

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Actin Structure in Fibroblasts,ransforming genes code for proteins that may directly induce transformation and tumorigenesis. Considerable progress has been made in recent years toward the identification of these proteins. Although the transforming proteins encoded by different viruses are distinct, they share certain properties