Vivian cody (8 Ergebnisse)

Zustand: Good. Former library copy. Pages intact with minimal writing/highlighting. The binding may be loose and creased. Dust jackets/supplements are not included. Includes library markings. Stock photo provided. Product includes identifying sticker. Better World Books: Buy Books. Do Good.

Hardcover. Zustand: Near Fine. Hardcover, xiii + 360 pages, NOT ex-library. Not an economy/Indian edition. Mildly used, clean and bright throughout with unmarked text, free of inscriptions and stamps, firmly bound. Published without a dust jacket. -- Since its first description in 1942 in both serum and cerebrospinal fluid, transthyretin (TTR) has had an eventful history, including changes in name from 'prealbumin' to 'thyroxine-binding prealbumin' to 'transthyretin' as knowledge increased about its functions. TTR is synthesised in a wide range of tissues in humans and other eutherian mammals: the liver, choroid plexus (blood- cerebrospinal fluid barrier), retinal pigment epithelium of the eye, pancreas, intestine and meninges. However, its sites of synthesis are more restricted in other vertebrates. This implies that the number of tissues synthesising TTR during vertebrate evolution has increased, and raises questions about the selection pressures governing TTR synthesis. TTR is most widely known as a distributor of thyroid hormones. In addition, TTR binds retinol-binding protein, which binds retinol. In this way, TTR is also involved with retinoid distribution. More recently, TTR has been demonstrated to bind a wide variety of endocrine disruptors including drugs, pollutants, industrial compounds, heavy metals, and some naturally occurring plant flavonoids. These not only interfere with thyroid hormone delivery in the body, but also transport such endocrine disruptors into the brain, where they have the potential to accumulate. -- Contents: 1 Mechanisms of Molecular Recognition: Structural Characteristics of Transthyretin Ligand Interactions / Vivian Cody & Andrzej Wojtczak; 2 Transthyretin Synthesis During Development and Evolution: What the Marsupials Revealed / Samantha J. Richardson; 3 Evolution of Transthyretin Gene Structure / Porntip Prapunpoj; 4 Evolutionary Insights from Fish Transthyretin / Deborah M. Power; 5 Salmonella sp. TLP: A Periplasmic 5-Hydroxyisourate Hydrolase / Sarah Hennebry; 6 Vertebrate 5-Hydroxyisourate Hydrolase Identification, Function, Structure, and Evolutionary Relationship with Transthyretin / Giuseppe Zanotti; 7 Transthyretin-Related and Transthyretin-like Proteins / A. Elisabeth Sauer-Eriksson; 8 Transthyretin-Retinol-Binding Protein Complex / Hugo L. Monaco; 9 Transthyretin and Retinol-Binding Protein: Implications in Fish Physiology / Sancia Gaetani & Diana Bellovino; 10 Transthyretin and Endocrine Disruptors / Kiyoshi Yamauchi & Akinori Ishihara; 11 Genetics: Clinical Implications of Transthyretin Amyloidosis / Merrill D. Benson; 12 Molecular Pathogenesis Associated with Familial Amyloidotic Polyneuropathy / Maria Joào Saraiva; 13 Histidine 31: The Achilles' Heel of Human Transthyretin. Microheterogeneity is Not Enough to Understand the Molecular Causes of Amyloidogenicity / Klaus Altland & Samantha J. Richardson; 14 New Therapeutic Approaches for Familial Amyloidotic Polyneuropathy (FAP) / Yukio Ando; 15 Liver Transplantation for Transthyretin Amyloidosis / Bo-Goran Ericzon; 16 Mouse Models of Transthyretin Amyloidosis / Sadahiro Itoand Shuichiro Maeda; 17 What Have We Learned from Transthyretin-Null Mice: Novel Functions for Transthyretin? / Joâo Carlos Sousa & Joana Almeida Palha; 18 Transthyretin Null Mice: Developmental Phenotypes / Julie A. Monk & Samantha J. Richardson; 19 Transthyretin Null Mice as a Model to Study the Involvement of Transthyretin in Neurobiology: From Neuropeptide Processing to Nerve Regeneration / Carolina Estima Fleming; 20 Plasma Transthyretin Reflects the Fluctuations of Lean Body Mass in Health and Disease / Yves Ingenbleek; Index.…

Hardcover. Zustand: Good. 362 pp., illustrations, bibliography, index. 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. 0.0.…

Zustand: Sehr gut. Zustand: Sehr gut | Seiten: 380 | Sprache: Englisch | Produktart: Bücher | Since its ?rst description in 1942 in both serum and cerebrospinal ?uid, transthyretin (TTR) has had an eventful history, including changes in name from ¿prealbumin¿ to ¿thyroxine-binding prealbumin¿ to ¿transthyretin¿ as knowledge increased about its functions. TTR is synthesised in a wide range of tissues in humans and other eutherian mammals: the liver, choroid plexus (blood- cerebrospinal ?uid barrier), retinal pigment epithelium of the eye, pancreas, intestine and meninges. However, its sites of synthesis are more restricted in other vertebrates. This implies that the number of tissues synthesising TTR during vertebrate evolution has increased, and raises questions about the selection pressures governing TTR synthesis. TTR is most widely known as a distributor of thyroid hormones. In addition, TTR binds retinol-binding protein, which binds retinol. In this way, TTR is also involved with retinoid distribution. More recently, TTR has been demonstrated to bind a wide variety of endocrine disruptors including drugs, pollutants, industrial compounds, heavy metals, and some naturally occurring plant ?avonoids. These not only interfere with thyroid hormone delivery in the body, but also transport such endocrine disruptors into the brain, where they have the potential to accumulate.…

Zustand: Hervorragend. Zustand: Hervorragend | Seiten: 380 | Sprache: Englisch | Produktart: Bücher | Since its ?rst description in 1942 in both serum and cerebrospinal ?uid, transthyretin (TTR) has had an eventful history, including changes in name from ¿prealbumin¿ to ¿thyroxine-binding prealbumin¿ to ¿transthyretin¿ as knowledge increased about its functions. TTR is synthesised in a wide range of tissues in humans and other eutherian mammals: the liver, choroid plexus (blood- cerebrospinal ?uid barrier), retinal pigment epithelium of the eye, pancreas, intestine and meninges. However, its sites of synthesis are more restricted in other vertebrates. This implies that the number of tissues synthesising TTR during vertebrate evolution has increased, and raises questions about the selection pressures governing TTR synthesis. TTR is most widely known as a distributor of thyroid hormones. In addition, TTR binds retinol-binding protein, which binds retinol. In this way, TTR is also involved with retinoid distribution. More recently, TTR has been demonstrated to bind a wide variety of endocrine disruptors including drugs, pollutants, industrial compounds, heavy metals, and some naturally occurring plant ?avonoids. These not only interfere with thyroid hormone delivery in the body, but also transport such endocrine disruptors into the brain, where they have the potential to accumulate.…

Taschenbuch. Zustand: Neu. Druck auf Anfrage Neuware - Printed after ordering - Since its rst description in 1942 in both serum and cerebrospinal uid, transthyretin (TTR) has had an eventful history, including changes in name from 'prealbumin' to 'thyroxine-binding prealbumin' to 'transthyretin' as knowledge increased about its functions. TTR is synthesised in a wide range of tissues in humans and other eutherian mammals: the liver, choroid plexus (blood- cerebrospinal uid barrier), retinal pigment epithelium of the eye, pancreas, intestine and meninges. However, its sites of synthesis are more restricted in other vertebrates. This implies that the number of tissues synthesising TTR during vertebrate evolution has increased, and raises questions about the selection pressures governing TTR synthesis. TTR is most widely known as a distributor of thyroid hormones. In addition, TTR binds retinol-binding protein, which binds retinol. In this way, TTR is also involved with retinoid distribution. More recently, TTR has been demonstrated to bind a wide variety of endocrine disruptors including drugs, pollutants, industrial compounds, heavy metals, and some naturally occurring plant avonoids. These not only interfere with thyroid hormone delivery in the body, but also transport such endocrine disruptors into the brain, where they have the potential to accumulate.…

Buch. Zustand: Neu. Druck auf Anfrage Neuware - Printed after ordering - Since its rst description in 1942 in both serum and cerebrospinal uid, transthyretin (TTR) has had an eventful history, including changes in name from 'prealbumin' to 'thyroxine-binding prealbumin' to 'transthyretin' as knowledge increased about its functions. TTR is synthesised in a wide range of tissues in humans and other eutherian mammals: the liver, choroid plexus (blood- cerebrospinal uid barrier), retinal pigment epithelium of the eye, pancreas, intestine and meninges. However, its sites of synthesis are more restricted in other vertebrates. This implies that the number of tissues synthesising TTR during vertebrate evolution has increased, and raises questions about the selection pressures governing TTR synthesis. TTR is most widely known as a distributor of thyroid hormones. In addition, TTR binds retinol-binding protein, which binds retinol. In this way, TTR is also involved with retinoid distribution. More recently, TTR has been demonstrated to bind a wide variety of endocrine disruptors including drugs, pollutants, industrial compounds, heavy metals, and some naturally occurring plant avonoids. These not only interfere with thyroid hormone delivery in the body, but also transport such endocrine disruptors into the brain, where they have the potential to accumulate.…

Hardcover. Zustand: Brand New. 1st edition. 360 pages. 9.53x6.30x1.18 inches. In Stock.