Abstract
The most truly fibrous components of cytoplasm, namely α-helical polypeptides that pair into a coiled-coil arrangement, are found in many situations. Being long rod-shaped molecules, they are ideal for contributing tensile strength to the cytoskeleton. Rod-shaped molecules can each make many more side-to-side bonds when assembled into filaments than do globular subunits like actin and tubulin.
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Further reading
Some reviews
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Some original papers
Aebi, U., Fowler, W. E., Rew, P. and Sun, T.-T. (1983). The fibrillar substructure of keratin filaments unraveled. J. Cell Biol. 97, 1131–1143.
Aebi, U., Cohn, J., Buhle, L. & Gerace, L. (1986). The nuclear lamina is a meshwork of intermediate-type filaments. Nature 323, 560–564.
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Goldman, R. D., Goldman, A. E., Green, K., Jones, J. C. R., Jones, S. M. & Yang, H.-Y. (1986). Intermediate filament networks: organization and possible functions of a diverse group of cytoskeletal elements. J. Cell. Sci. Suppl. 5, 69–97.
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© 1991 L. A. Amos and W. B. Amos
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Amos, L.A., Amos, W.B. (1991). Intermediate Filaments and other Alpha-Helical Proteins. In: Molecules of the Cytoskeleton. Macmillan Molecular Biology Series. Palgrave, London. https://doi.org/10.1007/978-1-349-21739-7_2
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DOI: https://doi.org/10.1007/978-1-349-21739-7_2
Publisher Name: Palgrave, London
Print ISBN: 978-0-333-49595-7
Online ISBN: 978-1-349-21739-7
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