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Amyloid
| Amyloid |
| Pubbl/distr/stampa | Stony Brook, N.Y., : Parthenon Pub., 1994- |
| Disciplina | 616.3995 |
| Soggetto topico |
Amyloid
Amyloidosis |
| Soggetto genere / forma |
Periodical
Fulltext Internet Resources. Periodicals. |
| ISSN | 1744-2818 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Periodico |
| Lingua di pubblicazione | eng |
| Record Nr. | UNISA-996335541503316 |
| Stony Brook, N.Y., : Parthenon Pub., 1994- | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. di Salerno | ||
| ||
Amyloid
| Amyloid |
| Pubbl/distr/stampa | Stony Brook, N.Y., : Parthenon Pub., 1994- |
| Disciplina | 616.3995 |
| Soggetto topico |
Amyloid
Amyloidosis Amiloïdosi |
| Soggetto genere / forma |
Periodical
Fulltext Internet Resources. Periodicals. Revistes electròniques. |
| ISSN | 1744-2818 |
| Formato | Materiale a stampa |
| Livello bibliografico | Periodico |
| Lingua di pubblicazione | eng |
| Record Nr. | UNINA-9910154541903321 |
| Stony Brook, N.Y., : Parthenon Pub., 1994- | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
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Amyloid fibrils and prefibrillar aggregates : molecular and biological properties / / edited by Daniel Erik Otzen
| Amyloid fibrils and prefibrillar aggregates : molecular and biological properties / / edited by Daniel Erik Otzen |
| Edizione | [1st ed.] |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2013 |
| Descrizione fisica | 1 online resource (440 p.) |
| Disciplina | 572.68 |
| Altri autori (Persone) | OtzenDaniel Erik <1969-> |
| Soggetto topico |
Amyloid
Glycoproteins |
| ISBN |
3-527-65420-8
3-527-65418-6 3-527-65421-6 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Amyloid Fibrils and Prefibrillar Aggregates; Contents; Preface; List of Contributors; 1 The Amyloid Phenomenon and Its Significance; 1.1 Introduction; 1.2 The Nature of the Amyloid State of Proteins; 1.3 The Structure and Properties of Amyloid Species; 1.4 The Kinetics and Mechanism of Amyloid Formation; 1.5 The Link between Amyloid Formation and Disease; 1.6 Strategies for Therapeutic Intervention; 1.7 Looking to the Future; 1.8 Summary; Acknowledgments; References; 2 Amyloid Structures at the Atomic Level: Insights from Crystallography
2.1 Atomic Structures of Segments of Amyloid-Forming Proteins2.1.1 Protein Segments That Form Amyloid-Related Crystals; 2.1.2 Atomic Structures of Fiber-Like Microcrystals; 2.2 Stability of Amyloid Fibers; 2.3 Which Proteins Enter the Amyloid State?; 2.4 Molecular Basis of Amyloid Polymorphism and Prion Strains; 2.5 Atomic Structures of Steric Zippers Suggest Models for Amyloid Fibers of Parent Proteins; 2.6 Atomic Structures of Steric Zippers Offer Approaches for Chemical Interventions against Amyloid Formation; 2.7 Summary; Acknowledgments; References 3 What Does Solid-State NMR Tell Us about Amyloid Structures?3.1 Introduction; 3.2 Principles of Solid-State NMR Spectroscopy and Experiments for Structural Constraints; 3.2.1 Isotope Labeling, Magic Angle Spinning, Dipolar Coupling, and Resonance Assignment; 3.2.2 De.ning the Amyloid Core by Magnetization Transfer from Water; 3.2.3 Determining the Fibril Registry; 3.2.4 Seeded versus Unseeded Fibrils; 3.3 Amyloid Fibrils Investigated by Solid-State NMR Spectroscopy; 3.3.1 Aβ peptides of Different Length; 3.3.2 Islet Amyloid Polypeptide (IAPP/Amylin): Parallel and Antiparallel Steric Zippers 3.3.3 α-Synuclein: Polymorphism with Flexible Terminal Regions3.3.4 PrP: Rearrangements to Maintain a Fibrillar Core Region; 3.3.5 Yeast Prions with Glutamine/Asparagine-Rich Prion Domains: Sup35p, Ure2p, and Rnq1p; 3.3.6 Functional Amyloid: the Yeast Prion HET-s; 3.4 Summary; References; 4 From Molecular to Supramolecular Amyloid Structures: Contributions from Fiber Diffraction and Electron Microscopy; 4.1 Introduction; 4.2 History; 4.2.1 The Historical Use of X-ray Fiber Diffraction; 4.2.2 The Historical Use of Transmission Electron Microscopy; 4.3 Methodology; 4.3.1 X-Ray Fiber Diffraction 4.3.2 Transmission Electron Microscopy4.4 Recent Advances in Amyloid Structure Determination; 4.4.1 X-ray Fiber Diffraction; 4.4.2 Transmission Electron Microscopy; 4.5 Summary; Acknowledgments; References; 5 Structures of Aggregating Species by Small-Angle X-Ray Scattering; 5.1 Introduction; 5.2 Theoretical and Experimental Aspects; 5.3 Data Analysis and Modeling Methods; 5.4 Studying Protein Aggregation and Fibrillation Using SAXS; 5.4.1 Some General Considerations; 5.4.2SAXS Studies of Insulin, Glucagon, and α-Synuclein; 5.4.3SDS-Induced Aggregation of α-Synuclein 5.4.4 Multi-Component Fitting and Analysis of SAXS Data |
| Record Nr. | UNINA-9910133857203321 |
| Weinheim, : Wiley-VCH, c2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
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Amyloid fibrils as functional nanomaterials / / Juliet Gerrard
| Amyloid fibrils as functional nanomaterials / / Juliet Gerrard |
| Autore | Gerrard Juliet, A |
| Pubbl/distr/stampa | London, : Henry Stewart Talks, 2017 |
| Descrizione fisica | 1 online resource (1 streaming video file (39 min.) : color, sound) |
| Collana | Protein folding, aggregation and design : concepts, experiments, theories and mechanisms |
| Soggetto topico |
Amyloid
Biotechnology Molecular machinery Nanotechnology Protein folding Amyloid - chemistry Amyloidogenic Proteins Biosensing Techniques Nanofibers Nanostructures Nanotechnology - methods Nanowires Protein Folding |
| Formato | Videoregistrazioni  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Contents: Generating useful materials from proteins -- Amyloid fibrils from waste materials in a commercially scalable process -- Nanoscaffolds for enzyme immobilisation -- Templates for nanowires and biosensors. |
| Record Nr. | UNINA-9910887856103321 |
Gerrard Juliet, A
|
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| London, : Henry Stewart Talks, 2017 | ||
| Videoregistrazioni | ||
| Lo trovi qui: Univ. Federico II | ||
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Amyloid proteins : the beta sheet conformation and disease
| Amyloid proteins : the beta sheet conformation and disease |
| Pubbl/distr/stampa | [Place of publication not identified], : Wiley VCH, 2005 |
| Soggetto topico |
Amyloidosis
Amyloid Protein Structure, Secondary Proteins Protein Conformation Multiprotein Complexes Proteostasis Deficiencies Molecular Conformation Macromolecular Substances Amino Acids, Peptides, and Proteins Metabolic Diseases Nutritional and Metabolic Diseases Chemicals and Drugs Molecular Structure Biochemical Phenomena Diseases Chemical Phenomena Phenomena and Processes Animal Biochemistry Human Anatomy & Physiology Health & Biological Sciences |
| ISBN | 3-527-61934-8 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNINA-9910144007403321 |
| [Place of publication not identified], : Wiley VCH, 2005 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Amyloid proteins : the beta sheet conformation and disease
| Amyloid proteins : the beta sheet conformation and disease |
| Pubbl/distr/stampa | [Place of publication not identified], : Wiley VCH, 2005 |
| Soggetto topico |
Amyloidosis
Amyloid Protein Structure, Secondary Proteins Protein Conformation Multiprotein Complexes Proteostasis Deficiencies Molecular Conformation Macromolecular Substances Amino Acids, Peptides, and Proteins Metabolic Diseases Nutritional and Metabolic Diseases Chemicals and Drugs Molecular Structure Biochemical Phenomena Diseases Chemical Phenomena Phenomena and Processes Animal Biochemistry Human Anatomy & Physiology Health & Biological Sciences |
| ISBN | 3-527-61934-8 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNINA-9910830100503321 |
| [Place of publication not identified], : Wiley VCH, 2005 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Amyloid proteins : the beta sheet conformation and disease
| Amyloid proteins : the beta sheet conformation and disease |
| Pubbl/distr/stampa | [Place of publication not identified], : Wiley VCH, 2005 |
| Soggetto topico |
Amyloidosis
Amyloid Protein Structure, Secondary Proteins Protein Conformation Multiprotein Complexes Proteostasis Deficiencies Molecular Conformation Macromolecular Substances Amino Acids, Peptides, and Proteins Metabolic Diseases Nutritional and Metabolic Diseases Chemicals and Drugs Molecular Structure Biochemical Phenomena Diseases Chemical Phenomena Phenomena and Processes Animal Biochemistry Human Anatomy & Physiology Health & Biological Sciences |
| ISBN | 3-527-61934-8 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Record Nr. | UNINA-9910876689903321 |
| [Place of publication not identified], : Wiley VCH, 2005 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Lipids and cellular membranes in amyloid diseases [[electronic resource] /] / edited by Raz Jelinek
| 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 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Lipids and cellular membranes in amyloid diseases [[electronic resource] /] / edited by Raz Jelinek
| 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 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Lipids and cellular membranes in amyloid diseases / / edited by Raz Jelinek
| Lipids and cellular membranes in amyloid diseases / / 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-9910876851103321 |
| Weinheim, : Wiley-VCH, 2011 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
