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Bone morphogenic protein / / series editor Gerald Litwack, PhD, Toluca Lake, North Hollywood, California
| Bone morphogenic protein / / series editor Gerald Litwack, PhD, Toluca Lake, North Hollywood, California |
| Edizione | [First edition.] |
| Pubbl/distr/stampa | Waltham, MA : , : Elsevier, , 2015 |
| Descrizione fisica | 1 online resource (367 p.) |
| Disciplina | 612.75 |
| Collana | Vitamins and Hormones |
| Soggetto topico | Bone morphogenetic proteins |
| Soggetto genere / forma | Electronic books. |
| ISBN | 0-12-802592-1 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover; Bone Morphogenic Protein; Copyright; Former Editors; Contents; Contributors; Preface; Chapter One: Mechanisms of BMP-Receptor Interaction and Activation; 1. Evolutionary Expansion and Diversification of the Transforming Growth Factor β Superfamily; 2. Phylogenetic Analysis Reveals Four Functional Subfamilies for TGFβ Ligands; 3. Expression as Protease-Activated Proproteins and a Cystine-Knot Motif in the C-Terminal Mature Region as Key Features ...; 4. TGFβ Receptor Activation and Its Downstream Signaling Cascade; 5. Too Few Receptors for Too Many Ligands Lead to Promiscuity
6. Molecular Mechanisms to Ensure Ligand-Receptor Promiscuity and Specificity: The Concept of Multiple Hot Spots of Binding7. Molecular Mechanisms to Ensure Ligand-Receptor Promiscuity and Specificity: The Concept of Structural Adaptability; 8. Consequences of Promiscuity and Specificity in the TGFβ Superfamily: Conclusions; References; Chapter Two: The Bone Morphogenetic Proteins and Their Antagonists; 1. Bone Morphogenetic Proteins; 2. BMP Antagonist Proteins; 2.1. Chordin Family; 2.2. Follistatin and Follistatin-Like Proteins; 2.3. Noggin; 2.4. Twisted Gastrulation 3. Cerberus and Dan Family BMP Antagonists3.1. Cerberus; 3.2. Coco; 3.3. Dan; 3.4. Gremlin; 3.5. PRDC/Gremlin 2; 3.6. Sclerostin; 3.7. USAG-1/Wise; 4. BMP-Antagonists Binding to Heparin/HS; References; Chapter Three: BMP-7 Signaling and its Critical Roles in Kidney Development, the Responses to Renal Injury, and Chronic K ...; 1. Introduction; 2. The TGF-β/BMP Protein Superfamily; 3. The BMP-7 Protein; 4. TGF-β/BMP Signaling Pathways; 4.1. SMAD-Dependent Mechanisms for TGF-β/BMP Signaling; 4.1.1. Ligand Binding and Receptor Activation; 4.1.2. Activation of SMAD Transcription Factors 4.1.3. Heterodimerization and Nuclear Translocation of SMAD Transcription Factors4.1.4. SMAD-Dependent Regulation of Transcription; 4.2. SMAD-Independent Mechanisms for TGF-β/BMP Signaling; 4.3. Key Regulatory Steps in TGF-β/BMP Signaling; 4.3.1. Ligand Expression; 4.3.2. Ligand Availability; 4.3.3. Receptor Activation; 4.3.4. SMAD Activation; 4.3.5. Formation of Transcription Factor Complexes; 5. The Role of BMP-7 in Kidney Development; 5.1. Effects of BMP-7 Genetic Ablation on Development; 5.2. Functions of BMP-7 in the Metanephric Mesenchyme; 5.3. Functions of BMP-7 in the Ureteric Bud 5.4. Functions of BMP-7 in Stromal Cell Populations6. BMP-7, Congenital Renal Abnormalities, and Pediatric Kidney Disease; 7. The Role of BMP-7 in the Pathogenesis of CKD; 7.1. Therapeutic Effects of Recombinant BMP-7 in Models of CKD; 7.2. Renal Protective Mechanisms of Recombinant BMP-7; 7.2.1. Inhibition of Renal Fibrosis; 7.2.2. Other Important Renal Protective Mechanisms; 8. A Model for the Role of Endogenous BMP-7 in Regulating the Responses to Renal Injury; 9. Clinical Implications for BMP-7 in Patients with CKD; Acknowledgments; References Chapter Four: The Role of BMP Signaling and NF-κB Signaling on Osteoblastic Differentiation, Cancer Development, and Vasc... |
| Record Nr. | UNINA-9910461143403321 |
| Waltham, MA : , : Elsevier, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Bone morphogenic protein / / series editor Gerald Litwack, PhD, Toluca Lake, North Hollywood, California
| Bone morphogenic protein / / series editor Gerald Litwack, PhD, Toluca Lake, North Hollywood, California |
| Edizione | [First edition.] |
| Pubbl/distr/stampa | Waltham, MA : , : Elsevier, , 2015 |
| Descrizione fisica | 1 online resource (367 p.) |
| Disciplina | 612.75 |
| Collana | Vitamins and Hormones |
| Soggetto topico | Bone morphogenetic proteins |
| ISBN | 0-12-802592-1 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover; Bone Morphogenic Protein; Copyright; Former Editors; Contents; Contributors; Preface; Chapter One: Mechanisms of BMP-Receptor Interaction and Activation; 1. Evolutionary Expansion and Diversification of the Transforming Growth Factor β Superfamily; 2. Phylogenetic Analysis Reveals Four Functional Subfamilies for TGFβ Ligands; 3. Expression as Protease-Activated Proproteins and a Cystine-Knot Motif in the C-Terminal Mature Region as Key Features ...; 4. TGFβ Receptor Activation and Its Downstream Signaling Cascade; 5. Too Few Receptors for Too Many Ligands Lead to Promiscuity
6. Molecular Mechanisms to Ensure Ligand-Receptor Promiscuity and Specificity: The Concept of Multiple Hot Spots of Binding7. Molecular Mechanisms to Ensure Ligand-Receptor Promiscuity and Specificity: The Concept of Structural Adaptability; 8. Consequences of Promiscuity and Specificity in the TGFβ Superfamily: Conclusions; References; Chapter Two: The Bone Morphogenetic Proteins and Their Antagonists; 1. Bone Morphogenetic Proteins; 2. BMP Antagonist Proteins; 2.1. Chordin Family; 2.2. Follistatin and Follistatin-Like Proteins; 2.3. Noggin; 2.4. Twisted Gastrulation 3. Cerberus and Dan Family BMP Antagonists3.1. Cerberus; 3.2. Coco; 3.3. Dan; 3.4. Gremlin; 3.5. PRDC/Gremlin 2; 3.6. Sclerostin; 3.7. USAG-1/Wise; 4. BMP-Antagonists Binding to Heparin/HS; References; Chapter Three: BMP-7 Signaling and its Critical Roles in Kidney Development, the Responses to Renal Injury, and Chronic K ...; 1. Introduction; 2. The TGF-β/BMP Protein Superfamily; 3. The BMP-7 Protein; 4. TGF-β/BMP Signaling Pathways; 4.1. SMAD-Dependent Mechanisms for TGF-β/BMP Signaling; 4.1.1. Ligand Binding and Receptor Activation; 4.1.2. Activation of SMAD Transcription Factors 4.1.3. Heterodimerization and Nuclear Translocation of SMAD Transcription Factors4.1.4. SMAD-Dependent Regulation of Transcription; 4.2. SMAD-Independent Mechanisms for TGF-β/BMP Signaling; 4.3. Key Regulatory Steps in TGF-β/BMP Signaling; 4.3.1. Ligand Expression; 4.3.2. Ligand Availability; 4.3.3. Receptor Activation; 4.3.4. SMAD Activation; 4.3.5. Formation of Transcription Factor Complexes; 5. The Role of BMP-7 in Kidney Development; 5.1. Effects of BMP-7 Genetic Ablation on Development; 5.2. Functions of BMP-7 in the Metanephric Mesenchyme; 5.3. Functions of BMP-7 in the Ureteric Bud 5.4. Functions of BMP-7 in Stromal Cell Populations6. BMP-7, Congenital Renal Abnormalities, and Pediatric Kidney Disease; 7. The Role of BMP-7 in the Pathogenesis of CKD; 7.1. Therapeutic Effects of Recombinant BMP-7 in Models of CKD; 7.2. Renal Protective Mechanisms of Recombinant BMP-7; 7.2.1. Inhibition of Renal Fibrosis; 7.2.2. Other Important Renal Protective Mechanisms; 8. A Model for the Role of Endogenous BMP-7 in Regulating the Responses to Renal Injury; 9. Clinical Implications for BMP-7 in Patients with CKD; Acknowledgments; References Chapter Four: The Role of BMP Signaling and NF-κB Signaling on Osteoblastic Differentiation, Cancer Development, and Vasc... |
| Record Nr. | UNINA-9910797425103321 |
| Waltham, MA : , : Elsevier, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Bone morphogenic protein / / series editor Gerald Litwack, PhD, Toluca Lake, North Hollywood, California
| Bone morphogenic protein / / series editor Gerald Litwack, PhD, Toluca Lake, North Hollywood, California |
| Edizione | [First edition.] |
| Pubbl/distr/stampa | Waltham, MA : , : Elsevier, , 2015 |
| Descrizione fisica | 1 online resource (367 p.) |
| Disciplina | 612.75 |
| Collana | Vitamins and Hormones |
| Soggetto topico | Bone morphogenetic proteins |
| ISBN | 0-12-802592-1 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover; Bone Morphogenic Protein; Copyright; Former Editors; Contents; Contributors; Preface; Chapter One: Mechanisms of BMP-Receptor Interaction and Activation; 1. Evolutionary Expansion and Diversification of the Transforming Growth Factor β Superfamily; 2. Phylogenetic Analysis Reveals Four Functional Subfamilies for TGFβ Ligands; 3. Expression as Protease-Activated Proproteins and a Cystine-Knot Motif in the C-Terminal Mature Region as Key Features ...; 4. TGFβ Receptor Activation and Its Downstream Signaling Cascade; 5. Too Few Receptors for Too Many Ligands Lead to Promiscuity
6. Molecular Mechanisms to Ensure Ligand-Receptor Promiscuity and Specificity: The Concept of Multiple Hot Spots of Binding7. Molecular Mechanisms to Ensure Ligand-Receptor Promiscuity and Specificity: The Concept of Structural Adaptability; 8. Consequences of Promiscuity and Specificity in the TGFβ Superfamily: Conclusions; References; Chapter Two: The Bone Morphogenetic Proteins and Their Antagonists; 1. Bone Morphogenetic Proteins; 2. BMP Antagonist Proteins; 2.1. Chordin Family; 2.2. Follistatin and Follistatin-Like Proteins; 2.3. Noggin; 2.4. Twisted Gastrulation 3. Cerberus and Dan Family BMP Antagonists3.1. Cerberus; 3.2. Coco; 3.3. Dan; 3.4. Gremlin; 3.5. PRDC/Gremlin 2; 3.6. Sclerostin; 3.7. USAG-1/Wise; 4. BMP-Antagonists Binding to Heparin/HS; References; Chapter Three: BMP-7 Signaling and its Critical Roles in Kidney Development, the Responses to Renal Injury, and Chronic K ...; 1. Introduction; 2. The TGF-β/BMP Protein Superfamily; 3. The BMP-7 Protein; 4. TGF-β/BMP Signaling Pathways; 4.1. SMAD-Dependent Mechanisms for TGF-β/BMP Signaling; 4.1.1. Ligand Binding and Receptor Activation; 4.1.2. Activation of SMAD Transcription Factors 4.1.3. Heterodimerization and Nuclear Translocation of SMAD Transcription Factors4.1.4. SMAD-Dependent Regulation of Transcription; 4.2. SMAD-Independent Mechanisms for TGF-β/BMP Signaling; 4.3. Key Regulatory Steps in TGF-β/BMP Signaling; 4.3.1. Ligand Expression; 4.3.2. Ligand Availability; 4.3.3. Receptor Activation; 4.3.4. SMAD Activation; 4.3.5. Formation of Transcription Factor Complexes; 5. The Role of BMP-7 in Kidney Development; 5.1. Effects of BMP-7 Genetic Ablation on Development; 5.2. Functions of BMP-7 in the Metanephric Mesenchyme; 5.3. Functions of BMP-7 in the Ureteric Bud 5.4. Functions of BMP-7 in Stromal Cell Populations6. BMP-7, Congenital Renal Abnormalities, and Pediatric Kidney Disease; 7. The Role of BMP-7 in the Pathogenesis of CKD; 7.1. Therapeutic Effects of Recombinant BMP-7 in Models of CKD; 7.2. Renal Protective Mechanisms of Recombinant BMP-7; 7.2.1. Inhibition of Renal Fibrosis; 7.2.2. Other Important Renal Protective Mechanisms; 8. A Model for the Role of Endogenous BMP-7 in Regulating the Responses to Renal Injury; 9. Clinical Implications for BMP-7 in Patients with CKD; Acknowledgments; References Chapter Four: The Role of BMP Signaling and NF-κB Signaling on Osteoblastic Differentiation, Cancer Development, and Vasc... |
| Record Nr. | UNINA-9910820372003321 |
| Waltham, MA : , : Elsevier, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Hormones and transport systems / / edited by Gerald Litwack ; contributors, Yasaman Aghazadeh [and thirty-eight others]
| Hormones and transport systems / / edited by Gerald Litwack ; contributors, Yasaman Aghazadeh [and thirty-eight others] |
| Edizione | [First edition.] |
| Pubbl/distr/stampa | Amsterdam, [Netherlands] : , : Academic Press, , 2015 |
| Descrizione fisica | 1 online resource (584 p.) |
| Disciplina | 612.4 |
| Collana | Vitamins and Hormones |
| Soggetto topico | Hormones |
| Soggetto genere / forma | Electronic books. |
| ISBN |
0-12-803008-9
0-12-803028-3 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover; Hormones and Transport Systems; Copyright; Former Editors; Contents; Contributors; Preface; Chapter One: Dietary I- Absorption: Expression and Regulation of the Na+/I- Symporter in the Intestine; 1. The Importance of Iodide in Human Health; 2. The Na+/I- Symporter; 2.1. Molecular identification of NIS; 2.2. NIS-mediated transport: Substrates and stoichiometry; 2.3. The role of physiological Na+ concentrations in NIS affinity for I-; 3. NIS Expression Beyond the Thyroid; 4. Targeting of NIS to the Plasma Membrane; 5. Hormonal Regulation of NIS Expression; 6. Dietary I- Absorption
7. Regulation of Intestinal NIS Expression8. Conclusions and Future Directions; Acknowledgments; References; Chapter Two: Apical Iodide Efflux in Thyroid; 1. Introduction; 2. Iodide and Thyroid Hormone Synthesis; 2.1. Thyroid organization; 2.2. Thyroid hormone synthesis; 3. Vectorial Transport Processes in Epithelia and Thyroid I- Accumulation; 3.1. Brief overview of basic epithelial transport processes; 3.2. Basolateral iodide uptake; 3.3. Apical iodide release; 4. Chloride Transport Proteins and Luminal I- Translocation; 4.1. SLC26A4 (Pendrin); 4.1.1. SLC26A4, HCO3-, luminal pH 4.2. Cystic fibrosis transmembrane conductance regulator4.2.1. CFTR and SLC26A4 interplay; 4.3. SLC5A8, a sodium-monocarboxylate transporter (hAIT; SLC5A8; SMCT1); 4.4. TMEM16A (anoctamin 1); 5. Conclusions; Acknowledgment; References; Chapter Three: The Sodium/Multivitamin Transporter: A Multipotent System with Therapeutic Implications; 1. Introduction; 2. ""Active"" Transport; 3. Identification of the Multivitamin Transporter; 4. The hSMVT Gene; 4.1. Expression of hSMVT in various tissues; 4.2. An additional high-affinity hSMVT-like uptake system?; 5. From Gene to Protein; 6. Family Ties 7. The Predicted Structure of hSMVT8. The (Co)Substrates of hSMVT; 9. The Characterization of the Cloned hSMVT; 9.1. Electrogenicity of hSMVT-mediated transport; 9.2. Mechanistic implications; 10. Medical Implications; 11. Conclusion and Future Directions; Acknowledgments; References; Chapter Four: Regulation of αENaC Transcription; 1. Introduction; 1.1. Aldosterone is a ligand for the mineralocorticoid receptor and glucocorticoid receptor; 1.2. Epithelial sodium channel (ENaC) is a major target of aldosterone action and a key ion channel in regulating Na+ balance 2. Dot1a-Af9 Complex Mediates Repression of αENaC2.1. Histone H3 K79 methyltransferase Dot1a; 2.1.1. Dot1 proteins are a unique class of histone methyltransferases; 2.1.2. Dot1 proteins and H3 K79 methylation have diverse functions; 2.1.3. Dot1a is the first aldosterone-regulated target with a known function in epigenetics; 2.1.4. Dot1a modulates targeted H3 K79 methylation at the αENaC promoter and represses αENaC in a methyltransferase-depen...; 2.1.5. Dot1a-mediated repression apparently requires its nuclear expression as well as its methyltransferase activity and... 2.1.6. Dot1a-mediated repression of αENaC raised new questions |
| Record Nr. | UNINA-9910459886503321 |
| Amsterdam, [Netherlands] : , : Academic Press, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Hormones and transport systems / / edited by Gerald Litwack ; contributors, Yasaman Aghazadeh [and thirty-eight others]
| Hormones and transport systems / / edited by Gerald Litwack ; contributors, Yasaman Aghazadeh [and thirty-eight others] |
| Edizione | [First edition.] |
| Pubbl/distr/stampa | Amsterdam, [Netherlands] : , : Academic Press, , 2015 |
| Descrizione fisica | 1 online resource (584 p.) |
| Disciplina | 612.4 |
| Collana | Vitamins and Hormones |
| Soggetto topico | Hormones |
| ISBN |
0-12-803008-9
0-12-803028-3 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover; Hormones and Transport Systems; Copyright; Former Editors; Contents; Contributors; Preface; Chapter One: Dietary I- Absorption: Expression and Regulation of the Na+/I- Symporter in the Intestine; 1. The Importance of Iodide in Human Health; 2. The Na+/I- Symporter; 2.1. Molecular identification of NIS; 2.2. NIS-mediated transport: Substrates and stoichiometry; 2.3. The role of physiological Na+ concentrations in NIS affinity for I-; 3. NIS Expression Beyond the Thyroid; 4. Targeting of NIS to the Plasma Membrane; 5. Hormonal Regulation of NIS Expression; 6. Dietary I- Absorption
7. Regulation of Intestinal NIS Expression8. Conclusions and Future Directions; Acknowledgments; References; Chapter Two: Apical Iodide Efflux in Thyroid; 1. Introduction; 2. Iodide and Thyroid Hormone Synthesis; 2.1. Thyroid organization; 2.2. Thyroid hormone synthesis; 3. Vectorial Transport Processes in Epithelia and Thyroid I- Accumulation; 3.1. Brief overview of basic epithelial transport processes; 3.2. Basolateral iodide uptake; 3.3. Apical iodide release; 4. Chloride Transport Proteins and Luminal I- Translocation; 4.1. SLC26A4 (Pendrin); 4.1.1. SLC26A4, HCO3-, luminal pH 4.2. Cystic fibrosis transmembrane conductance regulator4.2.1. CFTR and SLC26A4 interplay; 4.3. SLC5A8, a sodium-monocarboxylate transporter (hAIT; SLC5A8; SMCT1); 4.4. TMEM16A (anoctamin 1); 5. Conclusions; Acknowledgment; References; Chapter Three: The Sodium/Multivitamin Transporter: A Multipotent System with Therapeutic Implications; 1. Introduction; 2. ""Active"" Transport; 3. Identification of the Multivitamin Transporter; 4. The hSMVT Gene; 4.1. Expression of hSMVT in various tissues; 4.2. An additional high-affinity hSMVT-like uptake system?; 5. From Gene to Protein; 6. Family Ties 7. The Predicted Structure of hSMVT8. The (Co)Substrates of hSMVT; 9. The Characterization of the Cloned hSMVT; 9.1. Electrogenicity of hSMVT-mediated transport; 9.2. Mechanistic implications; 10. Medical Implications; 11. Conclusion and Future Directions; Acknowledgments; References; Chapter Four: Regulation of αENaC Transcription; 1. Introduction; 1.1. Aldosterone is a ligand for the mineralocorticoid receptor and glucocorticoid receptor; 1.2. Epithelial sodium channel (ENaC) is a major target of aldosterone action and a key ion channel in regulating Na+ balance 2. Dot1a-Af9 Complex Mediates Repression of αENaC2.1. Histone H3 K79 methyltransferase Dot1a; 2.1.1. Dot1 proteins are a unique class of histone methyltransferases; 2.1.2. Dot1 proteins and H3 K79 methylation have diverse functions; 2.1.3. Dot1a is the first aldosterone-regulated target with a known function in epigenetics; 2.1.4. Dot1a modulates targeted H3 K79 methylation at the αENaC promoter and represses αENaC in a methyltransferase-depen...; 2.1.5. Dot1a-mediated repression apparently requires its nuclear expression as well as its methyltransferase activity and... 2.1.6. Dot1a-mediated repression of αENaC raised new questions |
| Record Nr. | UNINA-9910797044003321 |
| Amsterdam, [Netherlands] : , : Academic Press, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Hormones and transport systems / / edited by Gerald Litwack ; contributors, Yasaman Aghazadeh [and thirty-eight others]
| Hormones and transport systems / / edited by Gerald Litwack ; contributors, Yasaman Aghazadeh [and thirty-eight others] |
| Edizione | [First edition.] |
| Pubbl/distr/stampa | Amsterdam, [Netherlands] : , : Academic Press, , 2015 |
| Descrizione fisica | 1 online resource (584 p.) |
| Disciplina | 612.4 |
| Collana | Vitamins and Hormones |
| Soggetto topico | Hormones |
| ISBN |
0-12-803008-9
0-12-803028-3 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover; Hormones and Transport Systems; Copyright; Former Editors; Contents; Contributors; Preface; Chapter One: Dietary I- Absorption: Expression and Regulation of the Na+/I- Symporter in the Intestine; 1. The Importance of Iodide in Human Health; 2. The Na+/I- Symporter; 2.1. Molecular identification of NIS; 2.2. NIS-mediated transport: Substrates and stoichiometry; 2.3. The role of physiological Na+ concentrations in NIS affinity for I-; 3. NIS Expression Beyond the Thyroid; 4. Targeting of NIS to the Plasma Membrane; 5. Hormonal Regulation of NIS Expression; 6. Dietary I- Absorption
7. Regulation of Intestinal NIS Expression8. Conclusions and Future Directions; Acknowledgments; References; Chapter Two: Apical Iodide Efflux in Thyroid; 1. Introduction; 2. Iodide and Thyroid Hormone Synthesis; 2.1. Thyroid organization; 2.2. Thyroid hormone synthesis; 3. Vectorial Transport Processes in Epithelia and Thyroid I- Accumulation; 3.1. Brief overview of basic epithelial transport processes; 3.2. Basolateral iodide uptake; 3.3. Apical iodide release; 4. Chloride Transport Proteins and Luminal I- Translocation; 4.1. SLC26A4 (Pendrin); 4.1.1. SLC26A4, HCO3-, luminal pH 4.2. Cystic fibrosis transmembrane conductance regulator4.2.1. CFTR and SLC26A4 interplay; 4.3. SLC5A8, a sodium-monocarboxylate transporter (hAIT; SLC5A8; SMCT1); 4.4. TMEM16A (anoctamin 1); 5. Conclusions; Acknowledgment; References; Chapter Three: The Sodium/Multivitamin Transporter: A Multipotent System with Therapeutic Implications; 1. Introduction; 2. ""Active"" Transport; 3. Identification of the Multivitamin Transporter; 4. The hSMVT Gene; 4.1. Expression of hSMVT in various tissues; 4.2. An additional high-affinity hSMVT-like uptake system?; 5. From Gene to Protein; 6. Family Ties 7. The Predicted Structure of hSMVT8. The (Co)Substrates of hSMVT; 9. The Characterization of the Cloned hSMVT; 9.1. Electrogenicity of hSMVT-mediated transport; 9.2. Mechanistic implications; 10. Medical Implications; 11. Conclusion and Future Directions; Acknowledgments; References; Chapter Four: Regulation of αENaC Transcription; 1. Introduction; 1.1. Aldosterone is a ligand for the mineralocorticoid receptor and glucocorticoid receptor; 1.2. Epithelial sodium channel (ENaC) is a major target of aldosterone action and a key ion channel in regulating Na+ balance 2. Dot1a-Af9 Complex Mediates Repression of αENaC2.1. Histone H3 K79 methyltransferase Dot1a; 2.1.1. Dot1 proteins are a unique class of histone methyltransferases; 2.1.2. Dot1 proteins and H3 K79 methylation have diverse functions; 2.1.3. Dot1a is the first aldosterone-regulated target with a known function in epigenetics; 2.1.4. Dot1a modulates targeted H3 K79 methylation at the αENaC promoter and represses αENaC in a methyltransferase-depen...; 2.1.5. Dot1a-mediated repression apparently requires its nuclear expression as well as its methyltransferase activity and... 2.1.6. Dot1a-mediated repression of αENaC raised new questions |
| Record Nr. | UNINA-9910819578803321 |
| Amsterdam, [Netherlands] : , : Academic Press, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Vitamins and hormones . Volume ninety-seven Nociceptin opioid / / series editor, Gerald Litwack
| Vitamins and hormones . Volume ninety-seven Nociceptin opioid / / series editor, Gerald Litwack |
| Edizione | [First edition.] |
| Pubbl/distr/stampa | Waltham, Massachusetts : , : Academic Press, , 2015 |
| Descrizione fisica | 1 online resource (392 p.) |
| Disciplina | 612.015756 |
| Collana | Vitamins and Hormones |
| Soggetto topico |
Neuropeptides
Opioid peptides Nociceptive pain |
| Soggetto genere / forma | Electronic books. |
| ISBN |
0-12-802593-X
0-12-802443-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover; Nociceptin Opioid; Copyright; Contents; Contributors; Preface; Chapter 1: Helix-Constrained Nociceptin Peptides Are Potent Agonists and Antagonists of ORL-1 and Nociception; 1. Nociception in Brief; 1.1. Opioid receptor-like receptor-ORL-1; 1.2. Nociceptin; 1.3. Interrogating the activation and address domains of nociceptin(1-17); 2. Prospecting the Importance of the N-Terminal Tetrapeptide of Nociceptin(1-17); 3. Other Modifications to Nociceptin(1-17); 4. The Importance of Structure in Nociceptin Analogues; 4.1. Importance of helicity; 4.2. Other nociceptin derivatives
5. Recent Advances in ORL-1 Active Nociceptin Peptides6. The Development of New Helix-Constrained Nociceptin Analogues; 6.1. Design of helix-constrained nociceptin analogues; 6.2. Helical structure of nociceptin(1-17)-NH2 analogues in water; 6.3. Nuclear magnetic resonance spectra-derived structures; 7. Biological Properties of Helical Nociceptin Mimetics; 7.1. Cellular expression of ORL-1 and ERK phosphorylation; 7.2. Agonist and antagonist activity of nociceptin(1-17)-NH2 and analogues; 7.3. Effects of helical constraint on biological activity in Neuro-2a cells 7.4. Stability and cell toxicity of helix-constrained versus unconstrained peptides7.5. In vivo activity of helix-constrained versus unconstrained nociceptin analogues; 8. Concluding Remarks; References; Chapter 2: Bioinformatics and Evolution of Vertebrate Nociceptin and Opioid Receptors; 1. Introduction; 1.1. The origin of G protein-coupled receptors; 1.2. A brief history of opioid receptors; 1.3. Evidence for opioid receptors in nonmammalian vertebrates; 2. The Vertebrate Opioid Receptor Sequence Database; 2.1. Alignment of protein sequences 2.2. Phylogenetic analysis of vertebrate opioid receptors2.3. Divergence and convergence of opioid receptor types; 3. The Human Genome and the Evolution of Opioid Receptors; 3.1. Duplicated opioid family receptor genes in the human genome; 3.2. Variation in human opioid receptor genes; 4. The Molecular Evolution of Vertebrate Opioid Family Receptors; 5. Future Directions; 6. Conclusions; Acknowledgments; References; Chapter 3: Ancestral Vertebrate Complexity of the Opioid System; 1. Introduction; 2. Opioid Peptide Family; 3. Opioid Receptor Family 4. Discussion: Complexity, Coevolution, and Divergence5. Conclusions; Acknowledgement; References; Chapter 4: Synthesis and Biological Activity of Small Peptides as NOP and Opioid Receptors' Ligands: View on Current Devel...; 1. Introduction; 2. Endogenous Opioid Peptides and Receptors: Nociceptin and NOP Receptor Ligands; 3. Hexapeptides with NOP Receptor Affinity; 4. Solid-Phase Peptide Synthesis; 5. Conclusions; Acknowledgment; References; Chapter 5: Pain Regulation by Nocistatin-Targeting Molecules: G Protein-Coupled-Receptor and Nocistatin-Interacting Protein; 1. Introduction 2. Biological Activity by NST Through G Protein-Coupled Receptor |
| Record Nr. | UNINA-9910460751403321 |
| Waltham, Massachusetts : , : Academic Press, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Vitamins and hormones . Volume ninety-seven Nociceptin opioid / / series editor, Gerald Litwack
| Vitamins and hormones . Volume ninety-seven Nociceptin opioid / / series editor, Gerald Litwack |
| Edizione | [First edition.] |
| Pubbl/distr/stampa | Waltham, Massachusetts : , : Academic Press, , 2015 |
| Descrizione fisica | 1 online resource (392 p.) |
| Disciplina | 612.015756 |
| Collana | Vitamins and Hormones |
| Soggetto topico |
Neuropeptides
Opioid peptides Nociceptive pain |
| ISBN |
0-12-802593-X
0-12-802443-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover; Nociceptin Opioid; Copyright; Contents; Contributors; Preface; Chapter 1: Helix-Constrained Nociceptin Peptides Are Potent Agonists and Antagonists of ORL-1 and Nociception; 1. Nociception in Brief; 1.1. Opioid receptor-like receptor-ORL-1; 1.2. Nociceptin; 1.3. Interrogating the activation and address domains of nociceptin(1-17); 2. Prospecting the Importance of the N-Terminal Tetrapeptide of Nociceptin(1-17); 3. Other Modifications to Nociceptin(1-17); 4. The Importance of Structure in Nociceptin Analogues; 4.1. Importance of helicity; 4.2. Other nociceptin derivatives
5. Recent Advances in ORL-1 Active Nociceptin Peptides6. The Development of New Helix-Constrained Nociceptin Analogues; 6.1. Design of helix-constrained nociceptin analogues; 6.2. Helical structure of nociceptin(1-17)-NH2 analogues in water; 6.3. Nuclear magnetic resonance spectra-derived structures; 7. Biological Properties of Helical Nociceptin Mimetics; 7.1. Cellular expression of ORL-1 and ERK phosphorylation; 7.2. Agonist and antagonist activity of nociceptin(1-17)-NH2 and analogues; 7.3. Effects of helical constraint on biological activity in Neuro-2a cells 7.4. Stability and cell toxicity of helix-constrained versus unconstrained peptides7.5. In vivo activity of helix-constrained versus unconstrained nociceptin analogues; 8. Concluding Remarks; References; Chapter 2: Bioinformatics and Evolution of Vertebrate Nociceptin and Opioid Receptors; 1. Introduction; 1.1. The origin of G protein-coupled receptors; 1.2. A brief history of opioid receptors; 1.3. Evidence for opioid receptors in nonmammalian vertebrates; 2. The Vertebrate Opioid Receptor Sequence Database; 2.1. Alignment of protein sequences 2.2. Phylogenetic analysis of vertebrate opioid receptors2.3. Divergence and convergence of opioid receptor types; 3. The Human Genome and the Evolution of Opioid Receptors; 3.1. Duplicated opioid family receptor genes in the human genome; 3.2. Variation in human opioid receptor genes; 4. The Molecular Evolution of Vertebrate Opioid Family Receptors; 5. Future Directions; 6. Conclusions; Acknowledgments; References; Chapter 3: Ancestral Vertebrate Complexity of the Opioid System; 1. Introduction; 2. Opioid Peptide Family; 3. Opioid Receptor Family 4. Discussion: Complexity, Coevolution, and Divergence5. Conclusions; Acknowledgement; References; Chapter 4: Synthesis and Biological Activity of Small Peptides as NOP and Opioid Receptors' Ligands: View on Current Devel...; 1. Introduction; 2. Endogenous Opioid Peptides and Receptors: Nociceptin and NOP Receptor Ligands; 3. Hexapeptides with NOP Receptor Affinity; 4. Solid-Phase Peptide Synthesis; 5. Conclusions; Acknowledgment; References; Chapter 5: Pain Regulation by Nocistatin-Targeting Molecules: G Protein-Coupled-Receptor and Nocistatin-Interacting Protein; 1. Introduction 2. Biological Activity by NST Through G Protein-Coupled Receptor |
| Record Nr. | UNINA-9910787429703321 |
| Waltham, Massachusetts : , : Academic Press, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Vitamins and hormones . Volume ninety-seven Nociceptin opioid / / series editor, Gerald Litwack
| Vitamins and hormones . Volume ninety-seven Nociceptin opioid / / series editor, Gerald Litwack |
| Edizione | [First edition.] |
| Pubbl/distr/stampa | Waltham, Massachusetts : , : Academic Press, , 2015 |
| Descrizione fisica | 1 online resource (392 p.) |
| Disciplina | 612.015756 |
| Collana | Vitamins and Hormones |
| Soggetto topico |
Neuropeptides
Opioid peptides Nociceptive pain |
| ISBN |
0-12-802593-X
0-12-802443-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover; Nociceptin Opioid; Copyright; Contents; Contributors; Preface; Chapter 1: Helix-Constrained Nociceptin Peptides Are Potent Agonists and Antagonists of ORL-1 and Nociception; 1. Nociception in Brief; 1.1. Opioid receptor-like receptor-ORL-1; 1.2. Nociceptin; 1.3. Interrogating the activation and address domains of nociceptin(1-17); 2. Prospecting the Importance of the N-Terminal Tetrapeptide of Nociceptin(1-17); 3. Other Modifications to Nociceptin(1-17); 4. The Importance of Structure in Nociceptin Analogues; 4.1. Importance of helicity; 4.2. Other nociceptin derivatives
5. Recent Advances in ORL-1 Active Nociceptin Peptides6. The Development of New Helix-Constrained Nociceptin Analogues; 6.1. Design of helix-constrained nociceptin analogues; 6.2. Helical structure of nociceptin(1-17)-NH2 analogues in water; 6.3. Nuclear magnetic resonance spectra-derived structures; 7. Biological Properties of Helical Nociceptin Mimetics; 7.1. Cellular expression of ORL-1 and ERK phosphorylation; 7.2. Agonist and antagonist activity of nociceptin(1-17)-NH2 and analogues; 7.3. Effects of helical constraint on biological activity in Neuro-2a cells 7.4. Stability and cell toxicity of helix-constrained versus unconstrained peptides7.5. In vivo activity of helix-constrained versus unconstrained nociceptin analogues; 8. Concluding Remarks; References; Chapter 2: Bioinformatics and Evolution of Vertebrate Nociceptin and Opioid Receptors; 1. Introduction; 1.1. The origin of G protein-coupled receptors; 1.2. A brief history of opioid receptors; 1.3. Evidence for opioid receptors in nonmammalian vertebrates; 2. The Vertebrate Opioid Receptor Sequence Database; 2.1. Alignment of protein sequences 2.2. Phylogenetic analysis of vertebrate opioid receptors2.3. Divergence and convergence of opioid receptor types; 3. The Human Genome and the Evolution of Opioid Receptors; 3.1. Duplicated opioid family receptor genes in the human genome; 3.2. Variation in human opioid receptor genes; 4. The Molecular Evolution of Vertebrate Opioid Family Receptors; 5. Future Directions; 6. Conclusions; Acknowledgments; References; Chapter 3: Ancestral Vertebrate Complexity of the Opioid System; 1. Introduction; 2. Opioid Peptide Family; 3. Opioid Receptor Family 4. Discussion: Complexity, Coevolution, and Divergence5. Conclusions; Acknowledgement; References; Chapter 4: Synthesis and Biological Activity of Small Peptides as NOP and Opioid Receptors' Ligands: View on Current Devel...; 1. Introduction; 2. Endogenous Opioid Peptides and Receptors: Nociceptin and NOP Receptor Ligands; 3. Hexapeptides with NOP Receptor Affinity; 4. Solid-Phase Peptide Synthesis; 5. Conclusions; Acknowledgment; References; Chapter 5: Pain Regulation by Nocistatin-Targeting Molecules: G Protein-Coupled-Receptor and Nocistatin-Interacting Protein; 1. Introduction 2. Biological Activity by NST Through G Protein-Coupled Receptor |
| Record Nr. | UNINA-9910821059903321 |
| Waltham, Massachusetts : , : Academic Press, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||