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Cell membrane [[electronic resource] ] : the red blood cell as a model / / Yoshihito Yawata
| Cell membrane [[electronic resource] ] : the red blood cell as a model / / Yoshihito Yawata |
| Autore | Yawata Yoshihito <1936-> |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2003 |
| Descrizione fisica | 1 online resource (457 p.) |
| Disciplina |
612.111
616.0792 |
| Soggetto topico |
Erythrocyte membranes
Membrane proteins |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-280-52041-8
9786610520411 3-527-60532-0 3-527-60153-8 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Cell Membrane; Contents; Preface; Foreword; Acknowledgments; 1 Introduction: History of Red Cell Membrane Research; 1.1 Invention of Optical Microscopes and Their Application to Hematology; 1.2 Discovery of Hereditary Spherocytosis by Light Microscopy; 1.3 The Dawn of Red Cell Membrane Research; 1.4 Commencement of Membrane Protein Biochemistry: Introduction of Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis; 1.5 Elucidation of the Pathogenesis of Red Cell Membrane Disorders; 1.6 Genotypes of Red Cell Membrane Disorders
1.7 Reevaluation of Molecular Electron Microscopy for Phenotypes2 Composition of Normal Red Cell Membranes; 2.1 Introduction; 2.2 Membrane Lipids; 2.2.1 The Contents and Nature of Membrane Lipids; 2.2.2 Asymmetry of the Membrane Lipid Bilayer; 2.2.3 Membrane Fluidity; 2.2.4 Renewal of Membrane Lipids; 2.2.5 Interactions Between Membrane Lipids and Proteins; 2.2.6 Membrane Lipids as a Determinant of Red Cell Shape; 2.3 Membrane Proteins; 2.3.1 Separation and Identification of Membrane Proteins; 2.3.2 Membrane Proteins and Membrane Structure; 2.3.3 Membrane Proteins in the Red Cell Surface 2.3.4 Membrane Proteins and Membrane Functions2.3.4.1 Red Cell Morphology and Shape Change; 2.3.4.2 Red Cell Deformability; 2.3.4.3 Membrane Transport and Permeability; 3 Stereotactic Structure of Red Cell Membranes; 3.1 Historical Background to Membrane Models; 3.2 Ultrastructure of Red Cell Membranes; 3.2.1 Introduction; 3.2.2 Evaluation of the Cytoskeletal Network; 3.2.2.1 Electron Microscopy With the Negative Staining Method; 3.2.2.2 Electron Microscopy With the Quick-Freeze Deep-Etching (QFDE) Method; 3.2.2.3 Electron Microscopy With the Surface Replica (SR) Method 3.2.3 Integral Proteins Examined by Electron Microscopy With the Freeze Fracture Method3.2.4 Visualization of Glycophorins by Field Emission Scanning Electron Microscopy; 4 Skeletal Proteins; 4.1 α- and β-Spectrins; 4.1.1 Introduction; 4.1.2 Structure of Red Cell Spectrins; 4.1.3 Functions of Red Cell Spectrins; 4.1.4 Erythroid and Nonerythroid Spectrins; 4.2 Protein 4.1; 4.2.1 Structure of Protein 4.1; 4.2.2 Binding to Other Membrane Proteins; 4.2.3 Extensive Alternative Splicings; 4.2.4 Nonerythroid Protein 4.1 Isoforms; 4.3 Actin; 4.4 Other Minor Skeletal Proteins; 4.4.1 The p55 Protein 4.4.2 Adducin4.4.3 Dematin (Protein 4.9); 4.4.4 Tropomyosin; 4.4.5 Tropomodulin; 4.4.6 Other Membrane Proteins; 5 Integral Proteins; 5.1 Band 3; 5.1.1 Structure of Band 3; 5.1.2 Functions of Band 3; 5.1.2.1 Membrane Protein Binding by the Cytoplasmic Domain of Band 3; 5.1.2.2 Binding to Glycolytic Enzymes by the Cytoplasmic Domain of Band 3; 5.1.2.3 Binding to Hemoglobin by the Cytoplasmic Domain of Band 3; 5.1.2.4 Anion Exchange Channel by the Transmembrane Domain of Band 3; 5.1.2.5 Lateral and Rotational Mobility of Band 3; 5.1.2.6 Blood Type Antigens and Band 3 5.1.3 Band 3 in Nonerythyroid Cells |
| Record Nr. | UNINA-9910146242603321 |
Yawata Yoshihito <1936->
|
||
| Weinheim, : Wiley-VCH, c2003 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Cell membrane [[electronic resource] ] : the red blood cell as a model / / Yoshihito Yawata
| Cell membrane [[electronic resource] ] : the red blood cell as a model / / Yoshihito Yawata |
| Autore | Yawata Yoshihito <1936-> |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2003 |
| Descrizione fisica | 1 online resource (457 p.) |
| Disciplina |
612.111
616.0792 |
| Soggetto topico |
Erythrocyte membranes
Membrane proteins |
| ISBN |
1-280-52041-8
9786610520411 3-527-60532-0 3-527-60153-8 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Cell Membrane; Contents; Preface; Foreword; Acknowledgments; 1 Introduction: History of Red Cell Membrane Research; 1.1 Invention of Optical Microscopes and Their Application to Hematology; 1.2 Discovery of Hereditary Spherocytosis by Light Microscopy; 1.3 The Dawn of Red Cell Membrane Research; 1.4 Commencement of Membrane Protein Biochemistry: Introduction of Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis; 1.5 Elucidation of the Pathogenesis of Red Cell Membrane Disorders; 1.6 Genotypes of Red Cell Membrane Disorders
1.7 Reevaluation of Molecular Electron Microscopy for Phenotypes2 Composition of Normal Red Cell Membranes; 2.1 Introduction; 2.2 Membrane Lipids; 2.2.1 The Contents and Nature of Membrane Lipids; 2.2.2 Asymmetry of the Membrane Lipid Bilayer; 2.2.3 Membrane Fluidity; 2.2.4 Renewal of Membrane Lipids; 2.2.5 Interactions Between Membrane Lipids and Proteins; 2.2.6 Membrane Lipids as a Determinant of Red Cell Shape; 2.3 Membrane Proteins; 2.3.1 Separation and Identification of Membrane Proteins; 2.3.2 Membrane Proteins and Membrane Structure; 2.3.3 Membrane Proteins in the Red Cell Surface 2.3.4 Membrane Proteins and Membrane Functions2.3.4.1 Red Cell Morphology and Shape Change; 2.3.4.2 Red Cell Deformability; 2.3.4.3 Membrane Transport and Permeability; 3 Stereotactic Structure of Red Cell Membranes; 3.1 Historical Background to Membrane Models; 3.2 Ultrastructure of Red Cell Membranes; 3.2.1 Introduction; 3.2.2 Evaluation of the Cytoskeletal Network; 3.2.2.1 Electron Microscopy With the Negative Staining Method; 3.2.2.2 Electron Microscopy With the Quick-Freeze Deep-Etching (QFDE) Method; 3.2.2.3 Electron Microscopy With the Surface Replica (SR) Method 3.2.3 Integral Proteins Examined by Electron Microscopy With the Freeze Fracture Method3.2.4 Visualization of Glycophorins by Field Emission Scanning Electron Microscopy; 4 Skeletal Proteins; 4.1 α- and β-Spectrins; 4.1.1 Introduction; 4.1.2 Structure of Red Cell Spectrins; 4.1.3 Functions of Red Cell Spectrins; 4.1.4 Erythroid and Nonerythroid Spectrins; 4.2 Protein 4.1; 4.2.1 Structure of Protein 4.1; 4.2.2 Binding to Other Membrane Proteins; 4.2.3 Extensive Alternative Splicings; 4.2.4 Nonerythroid Protein 4.1 Isoforms; 4.3 Actin; 4.4 Other Minor Skeletal Proteins; 4.4.1 The p55 Protein 4.4.2 Adducin4.4.3 Dematin (Protein 4.9); 4.4.4 Tropomyosin; 4.4.5 Tropomodulin; 4.4.6 Other Membrane Proteins; 5 Integral Proteins; 5.1 Band 3; 5.1.1 Structure of Band 3; 5.1.2 Functions of Band 3; 5.1.2.1 Membrane Protein Binding by the Cytoplasmic Domain of Band 3; 5.1.2.2 Binding to Glycolytic Enzymes by the Cytoplasmic Domain of Band 3; 5.1.2.3 Binding to Hemoglobin by the Cytoplasmic Domain of Band 3; 5.1.2.4 Anion Exchange Channel by the Transmembrane Domain of Band 3; 5.1.2.5 Lateral and Rotational Mobility of Band 3; 5.1.2.6 Blood Type Antigens and Band 3 5.1.3 Band 3 in Nonerythyroid Cells |
| Record Nr. | UNINA-9910830882603321 |
|
Yawata Yoshihito <1936->
|
||
| Weinheim, : Wiley-VCH, c2003 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Cell membrane : the red blood cell as a model / / Yoshihito Yawata
| Cell membrane : the red blood cell as a model / / Yoshihito Yawata |
| Autore | Yawata Yoshihito <1936-> |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2003 |
| Descrizione fisica | 1 online resource (457 p.) |
| Disciplina | 612.1/11 |
| Soggetto topico |
Erythrocyte membranes
Membrane proteins |
| ISBN |
1-280-52041-8
9786610520411 3-527-60532-0 3-527-60153-8 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Cell Membrane; Contents; Preface; Foreword; Acknowledgments; 1 Introduction: History of Red Cell Membrane Research; 1.1 Invention of Optical Microscopes and Their Application to Hematology; 1.2 Discovery of Hereditary Spherocytosis by Light Microscopy; 1.3 The Dawn of Red Cell Membrane Research; 1.4 Commencement of Membrane Protein Biochemistry: Introduction of Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis; 1.5 Elucidation of the Pathogenesis of Red Cell Membrane Disorders; 1.6 Genotypes of Red Cell Membrane Disorders
1.7 Reevaluation of Molecular Electron Microscopy for Phenotypes2 Composition of Normal Red Cell Membranes; 2.1 Introduction; 2.2 Membrane Lipids; 2.2.1 The Contents and Nature of Membrane Lipids; 2.2.2 Asymmetry of the Membrane Lipid Bilayer; 2.2.3 Membrane Fluidity; 2.2.4 Renewal of Membrane Lipids; 2.2.5 Interactions Between Membrane Lipids and Proteins; 2.2.6 Membrane Lipids as a Determinant of Red Cell Shape; 2.3 Membrane Proteins; 2.3.1 Separation and Identification of Membrane Proteins; 2.3.2 Membrane Proteins and Membrane Structure; 2.3.3 Membrane Proteins in the Red Cell Surface 2.3.4 Membrane Proteins and Membrane Functions2.3.4.1 Red Cell Morphology and Shape Change; 2.3.4.2 Red Cell Deformability; 2.3.4.3 Membrane Transport and Permeability; 3 Stereotactic Structure of Red Cell Membranes; 3.1 Historical Background to Membrane Models; 3.2 Ultrastructure of Red Cell Membranes; 3.2.1 Introduction; 3.2.2 Evaluation of the Cytoskeletal Network; 3.2.2.1 Electron Microscopy With the Negative Staining Method; 3.2.2.2 Electron Microscopy With the Quick-Freeze Deep-Etching (QFDE) Method; 3.2.2.3 Electron Microscopy With the Surface Replica (SR) Method 3.2.3 Integral Proteins Examined by Electron Microscopy With the Freeze Fracture Method3.2.4 Visualization of Glycophorins by Field Emission Scanning Electron Microscopy; 4 Skeletal Proteins; 4.1 α- and β-Spectrins; 4.1.1 Introduction; 4.1.2 Structure of Red Cell Spectrins; 4.1.3 Functions of Red Cell Spectrins; 4.1.4 Erythroid and Nonerythroid Spectrins; 4.2 Protein 4.1; 4.2.1 Structure of Protein 4.1; 4.2.2 Binding to Other Membrane Proteins; 4.2.3 Extensive Alternative Splicings; 4.2.4 Nonerythroid Protein 4.1 Isoforms; 4.3 Actin; 4.4 Other Minor Skeletal Proteins; 4.4.1 The p55 Protein 4.4.2 Adducin4.4.3 Dematin (Protein 4.9); 4.4.4 Tropomyosin; 4.4.5 Tropomodulin; 4.4.6 Other Membrane Proteins; 5 Integral Proteins; 5.1 Band 3; 5.1.1 Structure of Band 3; 5.1.2 Functions of Band 3; 5.1.2.1 Membrane Protein Binding by the Cytoplasmic Domain of Band 3; 5.1.2.2 Binding to Glycolytic Enzymes by the Cytoplasmic Domain of Band 3; 5.1.2.3 Binding to Hemoglobin by the Cytoplasmic Domain of Band 3; 5.1.2.4 Anion Exchange Channel by the Transmembrane Domain of Band 3; 5.1.2.5 Lateral and Rotational Mobility of Band 3; 5.1.2.6 Blood Type Antigens and Band 3 5.1.3 Band 3 in Nonerythyroid Cells |
| Record Nr. | UNINA-9910877609103321 |
|
Yawata Yoshihito <1936->
|
||
| Weinheim, : Wiley-VCH, c2003 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Transport and trafficking in the malaria-infected erthrocyte [[electronic resource] /] / [editors, Gregory R. Bock and Gail Cardew]
| Transport and trafficking in the malaria-infected erthrocyte [[electronic resource] /] / [editors, Gregory R. Bock and Gail Cardew] |
| Pubbl/distr/stampa | Chichester ; ; New York, : John Wiley, 1999 |
| Descrizione fisica | 1 online resource (306 p.) |
| Disciplina |
616.9
616.936207 |
| Altri autori (Persone) |
BockGregory
CardewGail |
| Collana | Novartis Foundation symposium |
| Soggetto topico |
Malaria - Pathophysiology
Erythrocyte membranes Biological transport Plasmodium falciparum |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-282-34817-5
9786612348174 0-470-51573-2 0-470-51574-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
TRANSPORT AND TRAFFICKING IN THE ERYTHROCYTE MALARIA-INFECTED; Contents; Participants; Introduction: host-parasite interrelations in the genomic age; Erythrocyte membrane transport; Chemical and physical in vitro alterations of the erythrocyte membrane: a model for its pathophysiological states?; The effects of transport perturbations on the homeostasis of erythrocytes; Transport properties of the host cell membrane; Transport of phospholipid synthesis precursors and lipid trafficking into malaria-infected erythrocytes; A nutrient-permeable channel on the intraerythrocytic malaria parasite
The permeability properties of the parasite cell membraneMacromolecular transport in malaria-infected erythrocytes; Expression of parasite transporters in Xenopus oocytes; Reconstitution of protein transport across the vacuolar membrane in P Zusmodium fu Zc@urum-infected permeabilized erythrocytes; Export of parasite proteins to the erythrocyte cytoplasm: secretory machinery and traffic signals; Transport and trafficking: Toxoplasma as a model for PZasmodium; An alternative secretory pathway in Pkusmodium: more questions than answers The transport of the histidine-rich protein I from Plasmodium falczarum is insensitive to brefeldin AProtein transport in the host cell cytoplasm and ATP-binding cassette proteins in Plasmodium fukiparum- infected erythrocytes; General discussion I; Chloroquine uptake and activity is determined by binding to ferriprotoporphyrin IX in Plasmodium f a lciparum; Chloroquine uptake, altered partitioning and the basis of drug resistance: evidence for chloride- dependent ionic regulation; Surnrnarv; Index of contributors; Subject index |
| Record Nr. | UNINA-9910144741803321 |
| Chichester ; ; New York, : John Wiley, 1999 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Transport and trafficking in the malaria-infected erthrocyte [[electronic resource] /] / [editors, Gregory R. Bock and Gail Cardew]
| Transport and trafficking in the malaria-infected erthrocyte [[electronic resource] /] / [editors, Gregory R. Bock and Gail Cardew] |
| Pubbl/distr/stampa | Chichester ; ; New York, : John Wiley, 1999 |
| Descrizione fisica | 1 online resource (306 p.) |
| Disciplina |
616.9
616.936207 |
| Altri autori (Persone) |
BockGregory
CardewGail |
| Collana | Novartis Foundation symposium |
| Soggetto topico |
Malaria - Pathophysiology
Erythrocyte membranes Biological transport Plasmodium falciparum |
| ISBN |
1-282-34817-5
9786612348174 0-470-51573-2 0-470-51574-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
TRANSPORT AND TRAFFICKING IN THE ERYTHROCYTE MALARIA-INFECTED; Contents; Participants; Introduction: host-parasite interrelations in the genomic age; Erythrocyte membrane transport; Chemical and physical in vitro alterations of the erythrocyte membrane: a model for its pathophysiological states?; The effects of transport perturbations on the homeostasis of erythrocytes; Transport properties of the host cell membrane; Transport of phospholipid synthesis precursors and lipid trafficking into malaria-infected erythrocytes; A nutrient-permeable channel on the intraerythrocytic malaria parasite
The permeability properties of the parasite cell membraneMacromolecular transport in malaria-infected erythrocytes; Expression of parasite transporters in Xenopus oocytes; Reconstitution of protein transport across the vacuolar membrane in P Zusmodium fu Zc@urum-infected permeabilized erythrocytes; Export of parasite proteins to the erythrocyte cytoplasm: secretory machinery and traffic signals; Transport and trafficking: Toxoplasma as a model for PZasmodium; An alternative secretory pathway in Pkusmodium: more questions than answers The transport of the histidine-rich protein I from Plasmodium falczarum is insensitive to brefeldin AProtein transport in the host cell cytoplasm and ATP-binding cassette proteins in Plasmodium fukiparum- infected erythrocytes; General discussion I; Chloroquine uptake and activity is determined by binding to ferriprotoporphyrin IX in Plasmodium f a lciparum; Chloroquine uptake, altered partitioning and the basis of drug resistance: evidence for chloride- dependent ionic regulation; Surnrnarv; Index of contributors; Subject index |
| Record Nr. | UNINA-9910830576303321 |
| Chichester ; ; New York, : John Wiley, 1999 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Transport and trafficking in the malaria-infected erthrocyte / / [editors, Gregory R. Bock and Gail Cardew]
| Transport and trafficking in the malaria-infected erthrocyte / / [editors, Gregory R. Bock and Gail Cardew] |
| Pubbl/distr/stampa | Chichester ; ; New York, : John Wiley, 1999 |
| Descrizione fisica | 1 online resource (306 p.) |
| Disciplina |
616.9
616.936207 |
| Altri autori (Persone) |
BockGregory
CardewGail |
| Collana | Novartis Foundation symposium |
| Soggetto topico |
Malaria - Pathophysiology
Erythrocyte membranes Biological transport Plasmodium falciparum |
| ISBN |
1-282-34817-5
9786612348174 0-470-51573-2 0-470-51574-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
TRANSPORT AND TRAFFICKING IN THE ERYTHROCYTE MALARIA-INFECTED; Contents; Participants; Introduction: host-parasite interrelations in the genomic age; Erythrocyte membrane transport; Chemical and physical in vitro alterations of the erythrocyte membrane: a model for its pathophysiological states?; The effects of transport perturbations on the homeostasis of erythrocytes; Transport properties of the host cell membrane; Transport of phospholipid synthesis precursors and lipid trafficking into malaria-infected erythrocytes; A nutrient-permeable channel on the intraerythrocytic malaria parasite
The permeability properties of the parasite cell membraneMacromolecular transport in malaria-infected erythrocytes; Expression of parasite transporters in Xenopus oocytes; Reconstitution of protein transport across the vacuolar membrane in P Zusmodium fu Zc@urum-infected permeabilized erythrocytes; Export of parasite proteins to the erythrocyte cytoplasm: secretory machinery and traffic signals; Transport and trafficking: Toxoplasma as a model for PZasmodium; An alternative secretory pathway in Pkusmodium: more questions than answers The transport of the histidine-rich protein I from Plasmodium falczarum is insensitive to brefeldin AProtein transport in the host cell cytoplasm and ATP-binding cassette proteins in Plasmodium fukiparum- infected erythrocytes; General discussion I; Chloroquine uptake and activity is determined by binding to ferriprotoporphyrin IX in Plasmodium f a lciparum; Chloroquine uptake, altered partitioning and the basis of drug resistance: evidence for chloride- dependent ionic regulation; Surnrnarv; Index of contributors; Subject index |
| Record Nr. | UNINA-9910877296603321 |
| Chichester ; ; New York, : John Wiley, 1999 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
