Lipids and cellular membranes in amyloid diseases [[electronic resource] /] / edited by Raz Jelinek |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH, 2011 |
Descrizione fisica | 1 online resource (298 p.) |
Disciplina | 616.3995 |
Altri autori (Persone) | JelinekRaz |
Soggetto topico |
Amyloid
Amyloidosis Proteins - Metabolism - Disorders |
Soggetto genere / forma | Electronic books. |
ISBN |
3-527-63433-9
1-283-14073-X 9786613140739 3-527-63434-7 3-527-63432-0 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Lipids and Cellular Membranes in Amyloid Diseases; Contents; Preface; List of Contributors; 1 Interactions of a-Synuclein with Lipids and Artificial Membranes Monitored by ESIPT Probes; 1.1 Introduction to Parkinson's Disease and a-Synuclein; 1.2 Structural Biology of a-Synuclein; 1.3 Methods for Studying AS-Lipid Interactions; 1.4 AS-Lipid Interactions; 1.5 Interactions of Monomeric AS with Artificial Membranes Monitored with ESIPT Probes; 1.5.1 Influence of Membrane Charge; 1.5.2 Influence of Membrane Curvature; 1.5.3 Influence of Membrane Phase; 1.5.4 Influence of Acyl Chains
1.5.5 Influence of Cholesterol1.5.6 Binding Kinetics; 1.6 Aggregation of AS and the Effects of Fatty Acids Monitored with ESIPT Probes; 1.7 Concluding Remarks; References; 2 Structural and Functional Insights into a-Synuclein-Lipid Interactions; 2.1 Introduction; 2.2 Interaction of a-Synuclein with Model Membrane Systems; 2.2.1 Binding of a-Synuclein Species to Giant Unilamellar Vesicles; 2.2.2 Model Membrane Permeabilization by a-Synuclein Oligomers; 2.2.3 Structural Features of a-Synuclein Oligomers; 2.3 Biological Significance; 2.3.1 Interaction Sites; 2.3.2 Membrane Penetration References3 Surfactants and Alcohols as Inducers of Protein Amyloid: Aggregation Chaperones or Membrane Simulators?; 3.1 Introduction; 3.2 Aggregation in the Presence of Surfactants; 3.2.1 General Aspects of Protein-Surfactant Interactions; 3.2.2 Effect of Surfactants on Protein Structure; 3.2.3 Stoichiometry of SDS Binding; 3.2.4 Aggregation of Proteins by SDS; 3.2.4.1 Aß; 3.2.4.2 ß2-Microglobulin and ß2-Glycoprotein I; 3.2.4.3 Tau Protein; 3.2.4.4 Prion Protein; 3.2.4.5 Acyl CoA Binding Protein (ACBP); 3.2.4.6 a-Synuclein (aSN) 3.3 Palimpsests of Future Functions: Cytotoxic Protein-Lipid Complexes3.4 Aggregation in Fluorinated Organic Solvents; 3.4.1 Protein Examples; 3.4.1.1 Acyl Phosphatase; 3.4.1.2 ß2-Microglobulin; 3.4.1.3 a-Chymotrypsin; 3.4.1.4 Alteration of Fibril Structure by TFE; 3.4.1.5 Other Proteins; 3.5 From Mimetics to the Real Thing: Aggregation on Lipids; 3.5.1 Binding Surfaces and High Local Concentrations; 3.5.2 Conformational Changes Associated with Binding; 3.5.3 Chemical Variability of the Lipid Environment; 3.6 Summary; References 4 Interaction of hIAPP and Its Precursors with Model and Biological Membranes4.1 Introduction; 4.2 Results; 4.2.1 The Conformations of Native proIAPP and hIAPP in Bulk Solution; 4.2.2 Fibrillation Kinetics and Conformational Changes of hIAPP and proIAPP in the Presence of Anionic Lipid Bilayers; 4.2.3 Effect of the Membrane-Mimicking Anionic Surfactant SDS on the Amyloidogenic Propensity of hIAPP and proIAPP; 4.2.4 hIAPP and proIAPP Aggregation and Fibrillation at Neutral Lipid Bilayers and Heterogeneous Model Raft Mixtures; 4.2.5 Comparison with Insulin-Membrane Interaction Studies 4.2.6 Cytotoxicity of hIAPP |
Record Nr. | UNINA-9910131028903321 |
Weinheim, : Wiley-VCH, 2011 | ||
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Lo trovi qui: Univ. Federico II | ||
|
Lipids and cellular membranes in amyloid diseases [[electronic resource] /] / edited by Raz Jelinek |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH, 2011 |
Descrizione fisica | 1 online resource (298 p.) |
Disciplina | 616.3995 |
Altri autori (Persone) | JelinekRaz |
Soggetto topico |
Amyloid
Amyloidosis Proteins - Metabolism - Disorders |
ISBN |
3-527-63433-9
1-283-14073-X 9786613140739 3-527-63434-7 3-527-63432-0 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Lipids and Cellular Membranes in Amyloid Diseases; Contents; Preface; List of Contributors; 1 Interactions of a-Synuclein with Lipids and Artificial Membranes Monitored by ESIPT Probes; 1.1 Introduction to Parkinson's Disease and a-Synuclein; 1.2 Structural Biology of a-Synuclein; 1.3 Methods for Studying AS-Lipid Interactions; 1.4 AS-Lipid Interactions; 1.5 Interactions of Monomeric AS with Artificial Membranes Monitored with ESIPT Probes; 1.5.1 Influence of Membrane Charge; 1.5.2 Influence of Membrane Curvature; 1.5.3 Influence of Membrane Phase; 1.5.4 Influence of Acyl Chains
1.5.5 Influence of Cholesterol1.5.6 Binding Kinetics; 1.6 Aggregation of AS and the Effects of Fatty Acids Monitored with ESIPT Probes; 1.7 Concluding Remarks; References; 2 Structural and Functional Insights into a-Synuclein-Lipid Interactions; 2.1 Introduction; 2.2 Interaction of a-Synuclein with Model Membrane Systems; 2.2.1 Binding of a-Synuclein Species to Giant Unilamellar Vesicles; 2.2.2 Model Membrane Permeabilization by a-Synuclein Oligomers; 2.2.3 Structural Features of a-Synuclein Oligomers; 2.3 Biological Significance; 2.3.1 Interaction Sites; 2.3.2 Membrane Penetration References3 Surfactants and Alcohols as Inducers of Protein Amyloid: Aggregation Chaperones or Membrane Simulators?; 3.1 Introduction; 3.2 Aggregation in the Presence of Surfactants; 3.2.1 General Aspects of Protein-Surfactant Interactions; 3.2.2 Effect of Surfactants on Protein Structure; 3.2.3 Stoichiometry of SDS Binding; 3.2.4 Aggregation of Proteins by SDS; 3.2.4.1 Aß; 3.2.4.2 ß2-Microglobulin and ß2-Glycoprotein I; 3.2.4.3 Tau Protein; 3.2.4.4 Prion Protein; 3.2.4.5 Acyl CoA Binding Protein (ACBP); 3.2.4.6 a-Synuclein (aSN) 3.3 Palimpsests of Future Functions: Cytotoxic Protein-Lipid Complexes3.4 Aggregation in Fluorinated Organic Solvents; 3.4.1 Protein Examples; 3.4.1.1 Acyl Phosphatase; 3.4.1.2 ß2-Microglobulin; 3.4.1.3 a-Chymotrypsin; 3.4.1.4 Alteration of Fibril Structure by TFE; 3.4.1.5 Other Proteins; 3.5 From Mimetics to the Real Thing: Aggregation on Lipids; 3.5.1 Binding Surfaces and High Local Concentrations; 3.5.2 Conformational Changes Associated with Binding; 3.5.3 Chemical Variability of the Lipid Environment; 3.6 Summary; References 4 Interaction of hIAPP and Its Precursors with Model and Biological Membranes4.1 Introduction; 4.2 Results; 4.2.1 The Conformations of Native proIAPP and hIAPP in Bulk Solution; 4.2.2 Fibrillation Kinetics and Conformational Changes of hIAPP and proIAPP in the Presence of Anionic Lipid Bilayers; 4.2.3 Effect of the Membrane-Mimicking Anionic Surfactant SDS on the Amyloidogenic Propensity of hIAPP and proIAPP; 4.2.4 hIAPP and proIAPP Aggregation and Fibrillation at Neutral Lipid Bilayers and Heterogeneous Model Raft Mixtures; 4.2.5 Comparison with Insulin-Membrane Interaction Studies 4.2.6 Cytotoxicity of hIAPP |
Record Nr. | UNINA-9910830148503321 |
Weinheim, : Wiley-VCH, 2011 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Lipids and cellular membranes in amyloid diseases [[electronic resource] /] / edited by Raz Jelinek |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH, 2011 |
Descrizione fisica | 1 online resource (298 p.) |
Disciplina | 616.3995 |
Altri autori (Persone) | JelinekRaz |
Soggetto topico |
Amyloid
Amyloidosis Proteins - Metabolism - Disorders |
ISBN |
3-527-63433-9
1-283-14073-X 9786613140739 3-527-63434-7 3-527-63432-0 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Lipids and Cellular Membranes in Amyloid Diseases; Contents; Preface; List of Contributors; 1 Interactions of a-Synuclein with Lipids and Artificial Membranes Monitored by ESIPT Probes; 1.1 Introduction to Parkinson's Disease and a-Synuclein; 1.2 Structural Biology of a-Synuclein; 1.3 Methods for Studying AS-Lipid Interactions; 1.4 AS-Lipid Interactions; 1.5 Interactions of Monomeric AS with Artificial Membranes Monitored with ESIPT Probes; 1.5.1 Influence of Membrane Charge; 1.5.2 Influence of Membrane Curvature; 1.5.3 Influence of Membrane Phase; 1.5.4 Influence of Acyl Chains
1.5.5 Influence of Cholesterol1.5.6 Binding Kinetics; 1.6 Aggregation of AS and the Effects of Fatty Acids Monitored with ESIPT Probes; 1.7 Concluding Remarks; References; 2 Structural and Functional Insights into a-Synuclein-Lipid Interactions; 2.1 Introduction; 2.2 Interaction of a-Synuclein with Model Membrane Systems; 2.2.1 Binding of a-Synuclein Species to Giant Unilamellar Vesicles; 2.2.2 Model Membrane Permeabilization by a-Synuclein Oligomers; 2.2.3 Structural Features of a-Synuclein Oligomers; 2.3 Biological Significance; 2.3.1 Interaction Sites; 2.3.2 Membrane Penetration References3 Surfactants and Alcohols as Inducers of Protein Amyloid: Aggregation Chaperones or Membrane Simulators?; 3.1 Introduction; 3.2 Aggregation in the Presence of Surfactants; 3.2.1 General Aspects of Protein-Surfactant Interactions; 3.2.2 Effect of Surfactants on Protein Structure; 3.2.3 Stoichiometry of SDS Binding; 3.2.4 Aggregation of Proteins by SDS; 3.2.4.1 Aß; 3.2.4.2 ß2-Microglobulin and ß2-Glycoprotein I; 3.2.4.3 Tau Protein; 3.2.4.4 Prion Protein; 3.2.4.5 Acyl CoA Binding Protein (ACBP); 3.2.4.6 a-Synuclein (aSN) 3.3 Palimpsests of Future Functions: Cytotoxic Protein-Lipid Complexes3.4 Aggregation in Fluorinated Organic Solvents; 3.4.1 Protein Examples; 3.4.1.1 Acyl Phosphatase; 3.4.1.2 ß2-Microglobulin; 3.4.1.3 a-Chymotrypsin; 3.4.1.4 Alteration of Fibril Structure by TFE; 3.4.1.5 Other Proteins; 3.5 From Mimetics to the Real Thing: Aggregation on Lipids; 3.5.1 Binding Surfaces and High Local Concentrations; 3.5.2 Conformational Changes Associated with Binding; 3.5.3 Chemical Variability of the Lipid Environment; 3.6 Summary; References 4 Interaction of hIAPP and Its Precursors with Model and Biological Membranes4.1 Introduction; 4.2 Results; 4.2.1 The Conformations of Native proIAPP and hIAPP in Bulk Solution; 4.2.2 Fibrillation Kinetics and Conformational Changes of hIAPP and proIAPP in the Presence of Anionic Lipid Bilayers; 4.2.3 Effect of the Membrane-Mimicking Anionic Surfactant SDS on the Amyloidogenic Propensity of hIAPP and proIAPP; 4.2.4 hIAPP and proIAPP Aggregation and Fibrillation at Neutral Lipid Bilayers and Heterogeneous Model Raft Mixtures; 4.2.5 Comparison with Insulin-Membrane Interaction Studies 4.2.6 Cytotoxicity of hIAPP |
Record Nr. | UNINA-9910841897903321 |
Weinheim, : Wiley-VCH, 2011 | ||
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Lo trovi qui: Univ. Federico II | ||
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Protein misfolding diseases [[electronic resource] ] : current and emerging principles and therapies / / edited by Marina Ramirez-Alvarado, Jeffery W. Kelly, Christopher M. Dobson |
Pubbl/distr/stampa | Hoboken, N.J., : Wiley, c2010 |
Descrizione fisica | 1 online resource (1102 p.) |
Disciplina |
616.3/995
616.3995 |
Altri autori (Persone) |
Ramirez-AlvaradoMarina
KellyJeffery W DobsonC. M (Christopher M.) |
Collana | Wiley series on protein and peptide science |
Soggetto topico |
Proteins - Metabolism - Disorders
Protein folding Amyloidosis |
ISBN |
1-118-03181-4
1-282-65355-5 9786612653551 0-470-57270-1 0-470-57269-8 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | PROTEIN MISFOLDING DISEASES; CONTENTS; CONTRIBUTORS; FOREWORD; PREFACE; ACKNOWLEDGMENTS; INTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE; PART I PRINCIPLES OF PROTEIN MISFOLDING; PART II PROTEIN MISFOLDING DISEASE: GAIN-OF-FUNCTION AND LOSS-OF-FUNCTION DISEASES; PART III ROLE OF ACCESSORY MOLECULES AND RISK FACTORS; PART IV MEDICAL ASPECTS OF DISEASE: DIAGNOSIS AND CURRENT THERAPIES; PART V APPROACHES FOR NEW AND EMERGING THERAPIES; INDEX |
Record Nr. | UNINA-9910140567603321 |
Hoboken, N.J., : Wiley, c2010 | ||
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Lo trovi qui: Univ. Federico II | ||
|
Protein misfolding diseases [[electronic resource] ] : current and emerging principles and therapies / / edited by Marina Ramirez-Alvarado, Jeffery W. Kelly, Christopher M. Dobson |
Pubbl/distr/stampa | Hoboken, N.J., : Wiley, c2010 |
Descrizione fisica | 1 online resource (1102 p.) |
Disciplina |
616.3/995
616.3995 |
Altri autori (Persone) |
Ramirez-AlvaradoMarina
KellyJeffery W DobsonC. M (Christopher M.) |
Collana | Wiley series on protein and peptide science |
Soggetto topico |
Proteins - Metabolism - Disorders
Protein folding Amyloidosis |
ISBN |
1-118-03181-4
1-282-65355-5 9786612653551 0-470-57270-1 0-470-57269-8 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | PROTEIN MISFOLDING DISEASES; CONTENTS; CONTRIBUTORS; FOREWORD; PREFACE; ACKNOWLEDGMENTS; INTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE; PART I PRINCIPLES OF PROTEIN MISFOLDING; PART II PROTEIN MISFOLDING DISEASE: GAIN-OF-FUNCTION AND LOSS-OF-FUNCTION DISEASES; PART III ROLE OF ACCESSORY MOLECULES AND RISK FACTORS; PART IV MEDICAL ASPECTS OF DISEASE: DIAGNOSIS AND CURRENT THERAPIES; PART V APPROACHES FOR NEW AND EMERGING THERAPIES; INDEX |
Record Nr. | UNINA-9910831067103321 |
Hoboken, N.J., : Wiley, c2010 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Protein misfolding diseases [[electronic resource] ] : current and emerging principles and therapies / / edited by Marina Ramirez-Alvarado, Jeffery W. Kelly, Christopher M. Dobson |
Pubbl/distr/stampa | Hoboken, N.J., : Wiley, c2010 |
Descrizione fisica | 1 online resource (1102 p.) |
Disciplina |
616.3/995
616.3995 |
Altri autori (Persone) |
Ramirez-AlvaradoMarina
KellyJeffery W DobsonC. M (Christopher M.) |
Collana | Wiley series on protein and peptide science |
Soggetto topico |
Proteins - Metabolism - Disorders
Protein folding Amyloidosis |
ISBN |
1-118-03181-4
1-282-65355-5 9786612653551 0-470-57270-1 0-470-57269-8 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | PROTEIN MISFOLDING DISEASES; CONTENTS; CONTRIBUTORS; FOREWORD; PREFACE; ACKNOWLEDGMENTS; INTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE; PART I PRINCIPLES OF PROTEIN MISFOLDING; PART II PROTEIN MISFOLDING DISEASE: GAIN-OF-FUNCTION AND LOSS-OF-FUNCTION DISEASES; PART III ROLE OF ACCESSORY MOLECULES AND RISK FACTORS; PART IV MEDICAL ASPECTS OF DISEASE: DIAGNOSIS AND CURRENT THERAPIES; PART V APPROACHES FOR NEW AND EMERGING THERAPIES; INDEX |
Record Nr. | UNINA-9910841338403321 |
Hoboken, N.J., : Wiley, c2010 | ||
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Lo trovi qui: Univ. Federico II | ||
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