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  • 1
    Online Resource
    Online Resource
    New York, NY : Landes Bioscience and Springer Science+Business Media, LLC
    UID:
    gbv_644978465
    Format: Online-Ressource , v.: digital
    Edition: Online-Ausg. Springer eBook Collection. Biomedical and Life Sciences Electronic reproduction; Available via World Wide Web
    ISBN: 1283074435 , 9781441963154 , 9781283074438
    Series Statement: Advances in Experimental Medicine and Biology 679
    Content: This book 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.
    Content: This book 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
    Note: Includes bibliographical references and index , Title Page; Copyright Page; PREFACE; ABOUT THE EDITORS...; ABOUT THE EDITORS...; PARTICIPANTS; Table of Contents; Chapter 1 Aquaporins: A Family of Highly Regulated Multifunctional Channels; Chapter 2 Phylogeny of Major Intrinsic Proteins; Chapter 3 Metalloids, Soil Chemistry and the Environment; Chapter 4 Arsenic Transport in Prokaryotes and Eukaryotic Microbes; Chapter 5 Metalloid Transport by Aquaglyceroporins: Consequences in the Treatment of Human Diseases; Chapter 6 Roles of Vertebrate Aquaglyceroporins in Arsenic Transport and Detoxification , Chapter 7 Molecular Mechanisms of Boron Transport in Plants: Involvement of Arabidopsis NIP51 and NIP6; 1; Chapter 8 Silicon Transporters in Higher Plants; Chapter 9 Major Intrinsic Proteins and Arsenic Transport in Plants: New Players and Their Potential Role; Chapter 10 Major Intrinsic Proteins in Biomimetic Membranes; Index , Electronic reproduction; Available via World Wide Web
    Additional Edition: ISBN 1283076071
    Additional Edition: ISBN 9781441963147
    Language: English
    URL: Volltext  (lizenzpflichtig)
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  • 2
    UID:
    almahu_9949419108102882
    Format: XVI, 146 p. 36 illus., 16 illus. in color. , online resource.
    Edition: 1st ed. 2010.
    ISBN: 9781441963154
    Series Statement: Advances in Experimental Medicine and Biology, 679
    Content: 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.
    Note: Aquaporins: A Family of Highly Regulated Multifunctional Channels -- Phylogeny of Major Intrinsic Proteins -- Metalloids, Soil Chemistry and the Environment -- Arsenic Transport in Prokaryotes and Eukaryotic Microbes -- Metalloid Transport by Aquaglyceroporins: Consequences in the Treatment of Human Diseases -- Roles of Vertebrate Aquaglyceroporins in Arsenic Transport and Detoxification -- Molecular Mechanisms of Boron Transport in Plants: Involvement of Arabidopsis NIP5;1 and NIP6;1 -- Silicon Transporters in Higher Plants -- Major Intrinsic Proteins and Arsenic Transport in Plants: New Players and Their Potential Role -- Major Intrinsic Proteins in Biomimetic Membranes.
    In: Springer Nature eBook
    Additional Edition: Printed edition: ISBN 9781441963147
    Additional Edition: Printed edition: ISBN 9781441963161
    Additional Edition: Printed edition: ISBN 9781493941001
    Language: English
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  • 3
    Book
    Book
    New York, NY : Springer-Verlag
    UID:
    kobvindex_ZLB15188614
    Format: XV, 145 Seiten , Ill., graph. Darst.
    Edition: 1st ed.
    ISBN: 9781441963147
    Series Statement: Advances in experimental medicine and biology 679
    Note: Text engl.
    Language: English
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