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  • 1
    Online Resource
    Online Resource
    Recent Advances in Transthyretin Evolution, Structure and Biological Functions (2009)
    Berlin, Heidelberg :Springer Berlin Heidelberg :
    Details
    UID:
    almahu_9949419311702882
    Format: XIII, 362 p. , online resource.
    Edition: 1st ed. 2009.
    ISBN: 9783642006463
    Content: There is a strong interest in transthyretin (TTR) in connection with protein evolution, medical and clinical research. Thus, this is an exciting time for experts in TTR research to come together to write a monograph covering both the basic and the clinical research into TTR. Transthyretin is a protein found in human blood and cerebrospinal fluid. It is directly involved in the transport of thyroid hormones, and indirectly in that of retinol. These hormones are essential for normal growth and development, particularly that of the brain. Spontaneous and inherited diseases affecting transthyretin result in amyloidosis. More than 80 point mutations in transthyretin lead to a variety of illnesses. Liver transplants are the most common treatment, although much research is also being carried out in drug therapies. The evolution of transthyretin has been extensively investigated - from humans to bacteria, invertebrate animals and plants. The structure of the protein has not changed, but its function has changed significantly. This is a most exciting example for the study of the evolution of protein structure-function relationships. This monograph will bring the reader up to date on the latest developments and discoveries.
    Note: Mechanisms of Molecular Recognition: Structural Characteristics of Transthyretin Ligand Interactions -- Transthyretin Synthesis During Development and Evolution: What the Marsupials Revealed -- Evolution of Transthyretin Gene Structure -- Evolutionary Insights from Fish Transthyretin -- The Salmonella sp. TLP: A Periplasmic 5-Hydroxyisourate Hydrolase -- Vertebrate 5-Hydroxyisourate Hydrolase Identification, Function, Structure, and Evolutionary Relationship with Transthyretin -- Transthyretin-Related and Transthyretin-like Proteins -- The Transthyretin-Retinol-Binding Protein Complex -- Transthyretin and Retinol-Binding Protein: Implications in Fish Physiology -- Transthyretin and Endocrine Disruptors -- Genetics: Clinical Implications of Transthyretin Amyloidosis -- Molecular Pathogenesis Associated with Familial Amyloidotic Polyneuropathy -- Histidine 31: The Achilles' Heel of Human Transthyretin. Microheterogeneity is Not Enough to Understand the Molecular Causes of Amyloidogenicity -- New Therapeutic Approaches for Familial Amyloidotic Polyneuropathy (FAP) -- Liver Transplantation for Transthyretin Amyloidosis -- Mouse Models of Transthyretin Amyloidosis -- What Have We Learned from Transthyretin-Null Mice: Novel Functions for Transthyretin? -- Transthyretin Null Mice: Developmental Phenotypes -- Transthyretin Null Mice as a Model to Study the Involvement of Transthyretin in Neurobiology: From Neuropeptide Processing to Nerve Regeneration -- Plasma Transthyretin Reflects the Fluctuations of Lean Body Mass in Health and Disease -- Erratum to.
    In: Springer Nature eBook
    Additional Edition: Printed edition: ISBN 9783642006937
    Additional Edition: Printed edition: ISBN 9783642006456
    Additional Edition: Printed edition: ISBN 9783642420719
    Language: English
    DOI: 10.1007/978-3-642-00646-3
    URL: https://doi.org/10.1007/978-3-642-00646-3
    Library Location Call Number Volume/Issue/Year Availability
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    Online Resource
    Open Access Request
    HU Berlin
  • 2
    Online Resource
    Online Resource
    Recent Advances in Transthyretin Evolution, Structure and Biological Functions (2009)
    Berlin, Heidelberg : Springer-Verlag Berlin Heidelberg
    Details
    UID:
    gbv_1648370349
    Format: Online-Ressource (digital)
    ISBN: 9783642006463 , 9783642006456
    Series Statement: SpringerLink
    Content: There is a strong interest in transthyretin (TTR) in connection with protein evolution, medical and clinical research. Thus, this is an exciting time for experts in TTR research to come together to write a monograph covering both the basic and the clinical research into TTR. Transthyretin is a protein found in human blood and cerebrospinal fluid. It is directly involved in the transport of thyroid hormones, and indirectly in that of retinol. These hormones are essential for normal growth and development, particularly that of the brain. Spontaneous and inherited diseases affecting transthyretin result in amyloidosis. More than 80 point mutations in transthyretin lead to a variety of illnesses. Liver transplants are the most common treatment, although much research is also being carried out in drug therapies. The evolution of transthyretin has been extensively investigated from humans to bacteria, invertebrate animals and plants. The structure of the protein has not changed, but its function has changed significantly. This is a most exciting example for the study of the evolution of protein structure-function relationships. This monograph will bring the reader up to date on the latest developments and discoveries.
    Note: Includes bibliographical references and index , 177150_1_En_FM1_OnlinePDF; 177150_1_En_1_Chapter_OnlinePDF; 177150_1_En_2_Chapter_OnlinePDF; 177150_1_En_3_Chapter_OnlinePDF; 177150_1_En_4_Chapter_OnlinePDF; 177150_1_En_5_Chapter_OnlinePDF; 177150_1_En_6_Chapter_OnlinePDF; 177150_1_En_7_Chapter_OnlinePDF; 177150_1_En_8_Chapter_OnlinePDF; 177150_1_En_9_Chapter_OnlinePDF; 177150_1_En_10_Chapter_OnlinePDF; 177150_1_En_11_Chapter_OnlinePDF; 177150_1_En_12_Chapter_OnlinePDF; 177150_1_En_13_Chapter_OnlinePDF; 177150_1_En_14_Chapter_OnlinePDF; 177150_1_En_15_Chapter_OnlinePDF; 177150_1_En_16_Chapter_OnlinePDF; 177150_1_En_17_Chapter_OnlinePDF , 177150_1_En_18_Chapter_OnlinePDF177150_1_En_19_Chapter_OnlinePDF; 177150_1_En_20_Chapter_OnlinePDF; 177150_1_En_BM2_Chapter_OnlinePDF
    Additional Edition: ISBN 9783642006456
    Additional Edition: Buchausg. u.d.T. Recent advances in transthyretin evolution, structure and biological functions Dordrecht : Springer, 2009 ISBN 9783642006456
    Language: English
    Subjects: Biology
    RVK:
    WD 5100
    Keywords: Präalbumin ; Amyloidose ; Präalbumin ; Aufsatzsammlung
    DOI: 10.1007/978-3-642-00646-3
    URL: Volltext
    URL: Volltext  (lizenzpflichtig)
    URL: Cover
    URL: Inhaltsverzeichnis
    Library Location Call Number Volume/Issue/Year Availability
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    Online Resource
    Online Access
    Open Access Request
    UB Potsdam
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