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Record Nr. |
UNINA9910143964803321 |
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Titolo |
Handbook of ATPases [[electronic resource] ] : biochemistry, cell biology, pathophysiology / / edited by Masamitsu Futai, Yoh Wada, and Jack H. Kaplan |
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Pubbl/distr/stampa |
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Weinheim, : Wiley-VCH, c2004 |
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ISBN |
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1-280-52094-9 |
9786610520947 |
3-527-60612-2 |
3-527-60628-9 |
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Descrizione fisica |
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1 online resource (495 p.) |
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Altri autori (Persone) |
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Disciplina |
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Soggetti |
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Adenosine triphosphatase |
Adenosine triphosphatase - Pathophysiology |
Electronic books. |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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Note generali |
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Description based upon print version of record. |
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Nota di bibliografia |
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Includes bibliographical references and index. |
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Nota di contenuto |
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Handbook of ATPases; Contents; Preface; List of Contributors; Part I P-type ATPases; 1 Yeast Plasma-membrane H(+)-ATPase: Model System for Studies of Structure, Function, Biogenesis, and Regulation; 1.1 Introduction; 1.2 Structure; 1.2.1 Ca(2+)-ATPase as a Model; 1.2.2 Applicability of the Ca(2+)-ATPase Structure to Other P(2)-ATPases, Including the Pma1 H(+)-ATPase; 1.2.3 H(+)-ATPase Oligomers; 1.2.4 Associated Proteolipids; 1.3 Reaction Mechanism; 1.3.1 Overview of the Reaction Cycle; 1.3.2 ATP Binding and Phosphorylation; 1.3.3 E1-E2 Conformational Change; 1.3.4 H(+) Pumping |
1.4 Biogenesis1.4.1 Pma1 Mutants with Defects in Folding and Biogenesis; 1.4.2 Use of Pma1 Mutants to Screen for Other Genes that Play a Role in Biogenesis and Quality Control; 1.4.3 Role of Lipid Rafts; 1.5 Regulation; 1.6 Emerging Knowledge of Other Yeast P-type ATPases; Acknowledgments; References; 2 Regulation of the Sarco |
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(endo)plasmic Reticulum Ca(2+)-ATPase by Phospholamban and Sarcolipin; 2.1 Introduction; 2.1.1 Background to Ca(2+) Signaling; 2.1.2 β-Adrenergic Signaling in the Heart; 2.2 Phospholamban-SERCA Interactions; 2.2.1 SERCA Structure and Function |
2.2.2 PLN Structure and Function2.2.3 Approaches to the Study of PLN-SERCA Interactions; 2.2.4 SERCA Residues Essential for Cytoplasmic Interaction with PLN; 2.2.5 PLN Residues Essential for Cytoplasmic Interaction with SERCA; 2.2.6 PLN Residues Essential for Transmembrane Interactions with SERCA; 2.2.7 SERCA Residues Essential for Transmembrane Interactions with PLN; 2.2.8 Structural Modeling of the PLN-SERCA Inhibitory Interaction; 2.3 Physiological Role of PLN in Basal Cardiac Function; 2.3.1 Alterations in PLN Levels and Function by Transcription and Phosphorylation |
2.3.2 Targeting of PLN2.3.3 Role of PLN in Smooth and Skeletal Muscles; 2.3.4 Overexpression of PLN; 2.3.5 Physiological Role of PLN in β-Adrenergic Stimulation; 2.3.6 Superinhibitory PLN Mutants; 2.4 Phospholamban in Heart Failure; 2.4.1 Introduction; 2.4.2 Potential Therapies; 2.5 Human PLN Mutations as a Cause of Cardiomyopathy; 2.5.1 PLN R9C Mutant; 2.5.2 PLN L39stop Mutant; 2.6 Sarcolipin; 2.6.1 Introduction; 2.7 Physiological Role of SLN; 2.7.1 SLN Expression; 2.7.2 Overexpression of SLN; 2.7.2.1 Response of the SLN Gene to Chronic Stimulation |
2.7.3 Inhibition of SERCA Function by SLN Plus PLN2.7.4 Modeling of the SLN-SERCA and SLN-PLN-SERCA Interactions; Acknowledgments; References; 3 Catalytic and Transport Mechanism of the Sarco-(Endo)Plasmic Reticulum Ca(2+)-ATPase (SERCA); Summary; 3.1 Introduction; 3.2 Experimental Systems; 3.3 Functional Characterization; 3.4 Structural Characterization; 3.4.1 Extramembranous Region and the Catalytic Domains of E1·2Ca(2+); 3.4.2 Transmembrane region of E1·2Ca(2+); 3.4.3 Enzyme Structure in the Absence of Ca(2+) (E2·TG); 3.4.4 Thapsigargin-binding Domain; 3.4.5 Interaction with Phospholamban |
3.5 Binding of Ligands, Catalytic Events and Conformational Changes |
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Sommario/riassunto |
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As the first comprehensive overview of this important class of enzymes, this two-volume handbook summarizes recent knowledge about the molecular mechanism of ATPases, relating this information to the physiology and pathopyhsiology of ion transport, mitochondrial function, vesicle transport and lysosomal acidification. All important P-type, F-type and V-type ATPases are treated systematically, complemented by a special section on the cell biology and physiology of acidic compartments, and backed by an extensive bibliography and index. This premier reference source for physiologists, molecular |
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2. |
Record Nr. |
UNINA9910647393303321 |
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Titolo |
Aquaporins / / edited by Baoxue Yang |
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Pubbl/distr/stampa |
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Singapore : , : Springer Nature Singapore : , : Imprint : Springer, , 2023 |
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ISBN |
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9789811974151 |
9789811974144 |
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Edizione |
[2nd ed. 2023.] |
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Descrizione fisica |
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1 online resource (362 pages) |
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Collana |
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Advances in Experimental Medicine and Biology, , 2214-8019 ; ; 1398 |
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Disciplina |
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Soggetti |
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Pharmacology |
Proteins |
Human physiology |
Biological transport |
Cell membranes |
Protein Biochemistry |
Human Physiology |
Membrane Trafficking |
Proteïnes de membrana |
Fisiologia humana |
Llibres electrònics |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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Nota di bibliografia |
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Includes bibliographical references and index. |
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Nota di contenuto |
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1. Classification and Gene Structure of Aquaporins -- 2. Protein Structure and Modification of Aquaporins -- 3. Expression Regulation and Trafficking of Aquaporins -- 4. Transport Characteristics of Aquaporins -- 5. Non-transport Functions of Aquaporins -- 6. The Evolutionary Aspects of Aquaporin Superfamily -- 7. Aquaporins in Nervous System -- 8. Aquaporins in Cardiovascular System -- 9. Aquaporins in Respiratory System -- 10. Aquaporins in Digestive System -- 11. Aquaporins in Urinary System -- 12. Aquaporins in Reproductive System -- 13. Aquaporins in Immune System.-14. Aquaporins in Eye -- 15. Aquaporins in Skin -- 16. Aquaporins in Glandular Secretion -- 17. Aquaporins in Fetal Development -- 18. Aquaporins in Diabetes Insipidus -- 19. Aquaporins in Edema -- 20. |
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Aquaporins in Obesity.-21. Aquaporins in Tumor -- 22. Aquaporin Inhibitors -- 23. Non-aquaporin Water Channels.-24. Methods to Measure Water Permeability. |
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Sommario/riassunto |
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This book provides a state-of-the-art report on our current understanding of aquaporins and the future direction of the field. Aquaporins (AQPs) are a group of water-channel proteins that are specifically permeable to water and other small molecules, such as glycerol and urea. To date thirteen water-channel proteins (AQP0 – AQP12) have been cloned and the mechanisms and physiological functions of water transport across biological membranes have long been the subject of interest. Recent advances in the molecular biology and physiology of water transport have yielded new insights into how and why water moves across cell membranes, and studies on aquaporin knockout mouse models suggest that aquaporins are involved in the development of some diseases and they may be useful targets of research into selective-inhibitor drugs. By focusing on the advances made over the last 30 years in the biophysics, genetics, protein structure, molecular biology, physiology, pathophysiology and pharmacology of aquaporins in mammalian cell membranes, this book provides novel insights into further mechanisms and the physiological significance of water and some small molecule transport in mammals in order to stimulate further research in new directions. In the second version, fourteen chapters will be updated base on the most recent research articles. Ten new chapters will be added. |
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