ISBN: 9781493941001 - mips and their roles in the exchange of metalloids: 679 (9 risultati)

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  • Lingua: Inglese

    Editore: Springer, 2016

    1493941003 / 9781493941001

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    Da: AHA-BUCH GmbH, Einbeck, GermaniaAHA-BUCH GmbH

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    Taschenbuch. Condizione: Neu. Druck auf Anfrage Neuware - Printed after ordering - Sixteen years have passed since human aquaporin-1 (AQP1) was discovered as the first water channel, facilitating trans-membrane water fluxes. Subsequent years of research showed that the water channel AQP1 was only the tip of an iceberg; the iceberg itself being the ubiquitous super family of membrane intrinsic proteins (MIPs) that facilitate trans-membrane transport of water and an increasing number of small, water-soluble and uncharged compounds. Here we introduce you to the superfamily of MIPs and provide a summary about our gradually refined understanding of the phylogenetic relationship of its members. This volume is dedicated to the metalloids, a recently discovered group of substrates for a number of specific MIPs in a diverse spectrum of organisms. Particular focus is given to the essential boron, the beneficial silicon and the highly toxic arsenic. The respective MIP isoforms that facilitate the transport of these metalloids include members from several clades of the phylogenetic tree, suggesting that metalloid transport is an ancient function within this family of channel proteins. Among all the various substrates that have been shown to be transported by MIPs, metalloids take an outstanding position. While water transport seems to be a common function of many MIPs, single isoforms in plants have been identified as being crucially important for the uptake of boric acid as well as silicic acid. Here, the function seems not to be redundant, as mutations in those genes render plants deficient in boron and silicon, respectively.…

  • Lingua: Inglese

    Editore: Springer, 2016

    1493941003 / 9781493941001

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    Da: Books Puddle, Woodside, NY, U.S.A.Books Puddle

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    Condizione: New. pp. 161.

  • Lingua: Inglese

    Editore: Springer, 2016

    1493941003 / 9781493941001

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    Da: Revaluation Books, Exeter, Regno UnitoRevaluation Books

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    Paperback. Condizione: Brand New. reprint edition. 145 pages. 9.61x6.69x0.37 inches. In Stock.

  • Lingua: Inglese

    Editore: Springer, 2016

    1493941003 / 9781493941001

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    Da: Brook Bookstore On Demand, Napoli, NA, ItaliaBrook Bookstore On Demand

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    Condizione: new. Questo è un articolo print on demand.

  • Lingua: Inglese

    Editore: Springer New York Aug 2016, 2016

    1493941003 / 9781493941001

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    Da: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, GermaniaBuchWeltWeit Ludwig Meier e.K.

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    EUR 160,49

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    Taschenbuch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Sixteen years have passed since human aquaporin-1 (AQP1) was discovered as the first water channel, facilitating trans-membrane water fluxes. Subsequent years of research showed that the water channel AQP1 was only the tip of an iceberg; the iceberg itself being the ubiquitous super family of membrane intrinsic proteins (MIPs) that facilitate trans-membrane transport of water and an increasing number of small, water-soluble and uncharged compounds. Here we introduce you to the superfamily of MIPs and provide a summary about our gradually refined understanding of the phylogenetic relationship of its members. This volume is dedicated to the metalloids, a recently discovered group of substrates for a number of specific MIPs in a diverse spectrum of organisms. Particular focus is given to the essential boron, the beneficial silicon and the highly toxic arsenic. The respective MIP isoforms that facilitate the transport of these metalloids include members from several clades of the phylogenetic tree, suggesting that metalloid transport is an ancient function within this family of channel proteins. Among all the various substrates that have been shown to be transported by MIPs, metalloids take an outstanding position. While water transport seems to be a common function of many MIPs, single isoforms in plants have been identified as being crucially important for the uptake of boric acid as well as silicic acid. Here, the function seems not to be redundant, as mutations in those genes render plants deficient in boron and silicon, respectively. 164 pp. Englisch.…

  • Lingua: Inglese

    Editore: Springer New York, 2016

    1493941003 / 9781493941001

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    Da: moluna, Greven, Germaniamoluna

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    Condizione: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Dedicated to the metalloids, a recently discovered group of substrates for a number of specific MIPs in a diverse spectrum of organismsAspects of the environmental chemistry of metalloids relevant to understand the role of MIPs in the exchange of metalloids.…

  • Lingua: Inglese

    Editore: Springer New York, Humana Aug 2016, 2016

    1493941003 / 9781493941001

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    Da: buchversandmimpf2000, Emtmannsberg, BAYE, Germaniabuchversandmimpf2000

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    Taschenbuch. Condizione: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Sixteen years have passed since human aquaporin-1 (AQP1) was discovered as the first water channel, facilitating trans-membrane water fluxes. Subsequent years of research showed that the water channel AQP1 was only the tip of an iceberg; the iceberg itself being the ubiquitous super family of membrane intrinsic proteins (MIPs) that facilitate trans-membrane transport of water and an increasing number of small, water-soluble and uncharged compounds. Here we introduce you to the superfamily of MIPs and provide a summary about our gradually refined understanding of the phylogenetic relationship of its members. This volume is dedicated to the metalloids, a recently discovered group of substrates for a number of specific MIPs in a diverse spectrum of organisms. Particular focus is given to the essential boron, the beneficial silicon and the highly toxic arsenic. The respective MIP isoforms that facilitate the transport of these metalloids include members from several clades of the phylogenetic tree, suggesting that metalloid transport is an ancient function within this family of channel proteins. Among all the various substrates that have been shown to be transported by MIPs, metalloids take an outstanding position. While water transport seems to be a common function of many MIPs, single isoforms in plants have been identified as being crucially important for the uptake of boric acid as well as silicic acid. Here, the function seems not to be redundant, as mutations in those genes render plants deficient in boron and silicon, respectively.Springer-Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg 164 pp. Englisch.…

  • Lingua: Inglese

    Editore: Springer, 2016

    1493941003 / 9781493941001

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    Da: Majestic Books, Hounslow, Regno UnitoMajestic Books

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    EUR 241,79

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    Condizione: New. Print on Demand pp. 161.

  • Lingua: Inglese

    Editore: Springer, 2016

    1493941003 / 9781493941001

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    Da: Biblios, frankfurt am main, HESSE, GermaniaBiblios

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    EUR 242,21

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    Condizione: New. PRINT ON DEMAND pp. 161.