Bienert gerd (37 resultados)

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Librería: killarneybooks, Inagh, CLARE, Irlandakillarneybooks
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Hardcover. Condición: Very Good. Hardcover, xv + 145 pages, references, index. An uncirculated university library withdrawal. An external stamp on upper outer page edges, internal library markings on pastedowns & prelims. Else pages in unused condition: clean, bright, with unmarked text firm binding. Boards show scratches (front… panel), regular shelfwear. Issued without a dust jacket. -- 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.

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Librería: Brook Bookstore On Demand, Napoli, NA, ItaliaBrook Bookstore On Demand
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EUR 126,26
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Idioma: Inglés
Editorial: Springer-Verlag New York Inc., New York, NY, 2010
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Librería: Grand Eagle Retail, Bensenville, IL, Estados Unidos de AmericaGrand Eagle Retail
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EUR 139,80
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Hardcover. Condición: new. Hardcover. 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 o…f 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. 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. Shipping may be from multiple locations in the US or from the UK, depending on stock availability.

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Librería: Brook Bookstore, Milano, MI, ItaliaBrook Bookstore
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EUR 121,53
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Librería: Revaluation Books, Exeter, Reino UnidoRevaluation Books
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EUR 157,01
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Hardcover. Condición: Brand New. 1st edition. 146 pages. 10.50x7.00x0.75 inches. In Stock.

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Librería: GreatBookPrices, Columbia, MD, Estados Unidos de AmericaGreatBookPrices
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EUR 170,79
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Librería: Books Puddle, New York, NY, Estados Unidos de AmericaBooks Puddle
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EUR 180,29
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Condición: New. pp. 162 1st edition.

Peroxiporins : Redox Signal Mediators in and Between Cells
Medraño-fernandez, Iria (EDT); Bienert, Gerd Patrick (EDT); Sitia, Roberto (EDT)
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Librería: GreatBookPrices, Columbia, MD, Estados Unidos de AmericaGreatBookPrices
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EUR 184,74
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Librería: THE SAINT BOOKSTORE, Southport, Reino UnidoTHE SAINT BOOKSTORE
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EUR 179,38
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Librería: Majestic Books, Hounslow, Reino UnidoMajestic Books
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EUR 190,76
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Condición: New. pp. 162.

Peroxiporins : Redox Signal Mediators in and Between Cells
Medraño-fernandez, Iria (EDT); Bienert, Gerd Patrick (EDT); Sitia, Roberto (EDT)
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Librería: GreatBookPricesUK, Woodford Green, Reino UnidoGreatBookPricesUK
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Condición: As New. Unread book in perfect condition.

Peroxiporins : Redox Signal Mediators in and Between Cells
Medraño-fernandez, Iria (EDT); Bienert, Gerd Patrick (EDT); Sitia, Roberto (EDT)
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Librería: GreatBookPrices, Columbia, MD, Estados Unidos de AmericaGreatBookPrices
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Librería: Majestic Books, Hounslow, Reino UnidoMajestic Books
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EUR 196,66
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Librería: Books Puddle, New York, NY, Estados Unidos de AmericaBooks Puddle
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EUR 201,94
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Condición: New.

Peroxiporins : Redox Signal Mediators in and Between Cells
Medraño-fernandez, Iria (EDT); Bienert, Gerd Patrick (EDT); Sitia, Roberto (EDT)
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Librería: GreatBookPricesUK, Woodford Green, Reino UnidoGreatBookPricesUK
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EUR 192,77
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Librería: moluna, Greven, Alemaniamoluna
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EUR 157,19
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Condición: New.

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Librería: THE SAINT BOOKSTORE, Southport, Reino UnidoTHE SAINT BOOKSTORE
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EUR 192,79
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Librería: preigu, Osnabrück, Alemaniapreigu
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EUR 140,10
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Taschenbuch. Condición: Neu. MIPs and Their Roles in the Exchange of Metalloids | Thomas P. Jahn (u. a.) | Taschenbuch | xvi | Englisch | 2016 | Springer | EAN 9781493941001 | Verantwortliche Person für die EU: Springer Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg, juergen[dot]hartmann[at]springer[dot]com | Anbieter: preigu.

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Librería: Books Puddle, New York, NY, Estados Unidos de AmericaBooks Puddle
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EUR 213,77
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Condición: New. pp. 161.

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Librería: AHA-BUCH GmbH, Einbeck, AlemaniaAHA-BUCH GmbH
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EUR 167,14
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Taschenbuch. Condición: 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 iceber…g 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.

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Librería: Revaluation Books, Exeter, Reino UnidoRevaluation Books
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EUR 237,18
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Hardcover. Condición: Brand New. 1st edition. 146 pages. 10.50x7.00x0.75 inches. In Stock.

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Librería: Mispah books, Redhill, SURRE, Reino UnidoMispah books
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EUR 223,45
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hardcover. Condición: New. New. book.

Idioma: Inglés
Editorial: Springer-Verlag New York Inc., New York, NY, 2010
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Librería: AussieBookSeller, Truganina, VIC, AustraliaAussieBookSeller
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EUR 220,43
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Hardcover. Condición: new. Hardcover. 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 o…f 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. 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. Shipping may be from our Sydney, NSW warehouse or from our UK or US warehouse, depending on stock availability.

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Librería: Buchpark, Trebbin, AlemaniaBuchpark
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EUR 144,03
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Condición: Sehr gut. Zustand: Sehr gut | Sprache: Englisch | Produktart: Bücher | 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 iceber…g 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.

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Librería: Revaluation Books, Exeter, Reino UnidoRevaluation Books
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EUR 249,79
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Paperback. Condición: Brand New. reprint edition. 145 pages. 9.61x6.69x0.37 inches. In Stock.

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Librería: Mispah books, Redhill, SURRE, Reino UnidoMispah books
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EUR 242,78
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Hardcover. Condición: Like New. LIKE NEW. SHIPS FROM MULTIPLE LOCATIONS. book.

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Librería: GreatBookPrices, Columbia, MD, Estados Unidos de AmericaGreatBookPrices
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EUR 276,88
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Condición: As New. Unread book in perfect condition.

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Librería: Mispah books, Redhill, SURRE, Reino UnidoMispah books
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EUR 262,10
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Paperback. Condición: Like New. LIKE NEW. SHIPS FROM MULTIPLE LOCATIONS. book.

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- Edición internacional
Librería: UK BOOKS STORE, London, LONDO, Reino UnidoUK BOOKS STORE
Contactar con el vendedorVendedor de 5 estrellasEdición internacionalCondición: Nuevo
EUR 311,91
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Condición: New. Brand New! Fast Delivery This is an International Edition and ship within 24-48 hours. Deliver by FedEx and Dhl, & Aramex, UPS, & USPS and we do accept APO and PO BOX Addresses. Order can be delivered worldwide within 6-10 days and we do have flat rate for up to 2LB. Extra shipping charges will be requested if th…e Book weight is more than 5 LB. This Item May be shipped from India, United states & United Kingdom. Depending on your location and availability.

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- Impresión bajo demanda
Librería: Brook Bookstore On Demand, Napoli, NA, ItaliaBrook Bookstore On Demand
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EUR 126,26
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Condición: new. Questo è un articolo print on demand.