A Critical Survey of Biomineralization: Control, Mechanisms, by Jürgen Engel

By Jürgen Engel

This monograph presents a finished and updated procedure on biomineralization. The topical concentration of the publication lies at the query of the way matrix proteins and cells catalyze and keep watch over mineralization in organisms. fresh advances within the knowing of biomineralization support to higher comprehend biomaterials, specifically their mechanical houses. the objective viewers basically contains practitioners and learn specialists within the box, however the e-book can also be worthwhile for graduate scholars.

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Extra resources for A Critical Survey of Biomineralization: Control, Mechanisms, Functions and Material Properties

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From nature to application, vol 4. Wiley, pp 1–35 2. Haeckel E (1974) Art forms in nature (Dover Pictorial Archive) Paperback 3. Javaheri N, Dries R, Burson A, Stal LJ, Sloot PM, Kaandorp JA (2015) Temperature affects the silicate morphology in a diatom. Sci Rep 5:11652. 1038/srep11652 4. Hildebrand M (2000) Silicic acid transport and its control during cell wall silicification in diatoms. In: Baeuerlein E (ed) Biomineralization, from biology to biotechnology and medical applications. Wiley-VCH, pp 172–1885 5.

The microtubules, actin, and other cytoskeletal components may be involved in the changes in the shape of the plasma membrane, and regulated processes at the plasma membrane may model the formation of the siliceous cell wall. The nascent siliceous cell wall and the site of its formation are in very close neighborhood and are arranged in parallel by the membrane. In the scheme of Fig. 4, the distances between the cell membrane and the cell wall are too large to allow a clear distinction. In reality, electron microcopy shows that the distances are extremely small and the membrane and cell wall touch each other [10].

Marie B, Jackson DJ, Ramos-Silva P, Zanella-Cleon I, Guichard N, Marin F (2013) The shell-forming proteome of Lottia gigantea reveals both deep conservations and lineage-specific novelties. FEBS J 280(1):214–232. 12062 6. Mann K, Edsinger E (2014) The Lottia gigantea shell matrix proteome: re-analysis including MaxQuant iBAQ quantitation and phosphoproteome analysis. Proteome Sci 12:28. doi:10. 1186/1477-5956-12-28 7. Liang J, Xu G, Xie J, Lee I, Xiang L, Wang H, … Zhang R (2015) Dual roles of the lysine-rich matrix protein (KRMP)-3 in shell formation of pearl oyster, Pinctada fucata.

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