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Cellular and biomolecular recognition [[electronic resource] ] : synthetic and non-biological molecules / / edited by Raz Jelinek
| Cellular and biomolecular recognition [[electronic resource] ] : synthetic and non-biological molecules / / edited by Raz Jelinek |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
| Descrizione fisica | 1 online resource (371 p.) |
| Disciplina |
579
620.192 |
| Altri autori (Persone) | JelinekRaz |
| Soggetto topico |
Biomolecules
Cellular recognition Biomimetics Biomolecules - Structure |
| ISBN |
1-282-68353-5
9786612683534 3-527-62701-4 3-527-62702-2 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Cellular and Biomolecular Recognition; Contents; Preface; List of Contributors; 1: Development of Functional Materials from Rod-Like Viruses; 1.1 Introduction; 1.2 Overview; 1.2.1 TMV; 1.2.2 M13 Bacteriophage; 1.3 Programmable Protein Shells; 1.3.1 Chemical Modifications; 1.3.2 Genetic Modifications; 1.3.2.1 Genetic Modification of TMV; 1.3.2.2 M13 Genetic Modification; 1.3.3 Chemical Modification in Combination with Genetic Mutation; 1.4 Templated Syntheses of Composite Materials; 1.4.1 Synthesis of Inorganic Materials Using TMV as the Template; 1.4.2 Bacteriophage M13 as the Template
1.5 Self-Assembly of Rod-Like Viruses1.5.1 Controlled 1D Assembly; 1.5.1.1 TMV Head-to-Tail Assembly; 1.5.1.2 Conductive 1D TMV Composite Fibers; 1.5.1.3 Weaving M13 Bacteriophage into Robust Fibers; 1.5.1.4 Nanoring Structure; 1.5.2 Fabrication of Thin Films by 2D Self-Assembly; 1.5.3 Controlling the 3D Assembly of TMV and M13; 1.6 Virus-Based Device and Applications; 1.7 Outlook; References; 2: Biomimetic Nanoparticles Providing Molecularly Defined Binding Sites - Protein-Featuring Structures versus Molecularly Imprinted Polymers; 2.1 Introduction; 2.2 Core Materials and Functionalities 2.2.1 Inorganic Core Materials2.2.1.1 Inorganic Crystalline Nanoparticles; 2.2.1.2 Particles with Silica Cores; 2.2.1.3 Metals and Metal Oxides; 2.2.2 Organic Core Materials; 2.2.2.1 Polymers, Lipids and Fullerenes; 2.3 Functional Shells; 2.3.1 Organic Shells; 2.3.2 MIPs; 2.3.2.1 Tools for MIP Development; 2.3.2.2 Bulk MIP and Proteins; 2.3.2.3 Nanospheric MIPs in General; 2.3.2.4 Nanospheric MIPs and Proteins; 2.4 Applications; 2.4.1 Biopurification; 2.4.1.1 Magnetic Nanoparticles; 2.4.1.2 MIPs with Magnetizable Cores; 2.4.2 Drug Delivery and Drug Targeting 2.4.2.1 Nanoparticle Systems for Drug Delivery2.4.2.2 Ligands on Nanoparticle Surfaces; 2.4.2.3 Targeting of Specific Cells; 2.5 Products; 2.5.1 MIPs-Applications and Products; 2.5.2 Luminex Assay; 2.6 Conclusions; References; 3: Interaction Between Silica Particles and Human Epithelial Cells: Atomic Force Microscopy and Fluorescence Study; 3.1 Interaction of Silica with Biological Cells: Background; 3.2 Interaction of a Silica Particle with the Cell Surface: How It Is Seen with AFM; 3.2.1 AFM; 3.2.2 AFM on Cells; 3.2.2.1 Cell Culture; 3.2.2.2 AFM; 3.2.3 AFM Probe Preparations 3.2.4 Models to Analyze the Cell Surface: Need for a Two-Layer Model3.2.5 Experimental Data; 3.2.5.1 Surface Brush on Cancer and Normal Cells; 3.2.5.2 Measurement of Adhesion: Silica Particle-Cell Interaction; 3.2.5.3 Can the Difference in Adhesion Be Used to Detect Cancer Cells?; 3.3 Ultra-Bright Fluorescent Silica Particles to Be Used to Study Interaction with Cells; 3.4 Ultra-Bright Fluorescent Silica Particles to Distinguish Between Cancer and Normal Cells; 3.4.1 Methods and Materials; 3.4.1.1 Spectrofluorometric and Optical Measurements of the Particles Attached to Cells 3.4.1.2 Detection of Affinity of Fluorescent Silica Particles to Cells |
| Record Nr. | UNINA-9910139750703321 |
| Weinheim, : Wiley-VCH | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Cellular and biomolecular recognition [[electronic resource] ] : synthetic and non-biological molecules / / edited by Raz Jelinek
| Cellular and biomolecular recognition [[electronic resource] ] : synthetic and non-biological molecules / / edited by Raz Jelinek |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
| Descrizione fisica | 1 online resource (371 p.) |
| Disciplina |
579
620.192 |
| Altri autori (Persone) | JelinekRaz |
| Soggetto topico |
Biomolecules
Cellular recognition Biomimetics Biomolecules - Structure |
| ISBN |
1-282-68353-5
9786612683534 3-527-62701-4 3-527-62702-2 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Cellular and Biomolecular Recognition; Contents; Preface; List of Contributors; 1: Development of Functional Materials from Rod-Like Viruses; 1.1 Introduction; 1.2 Overview; 1.2.1 TMV; 1.2.2 M13 Bacteriophage; 1.3 Programmable Protein Shells; 1.3.1 Chemical Modifications; 1.3.2 Genetic Modifications; 1.3.2.1 Genetic Modification of TMV; 1.3.2.2 M13 Genetic Modification; 1.3.3 Chemical Modification in Combination with Genetic Mutation; 1.4 Templated Syntheses of Composite Materials; 1.4.1 Synthesis of Inorganic Materials Using TMV as the Template; 1.4.2 Bacteriophage M13 as the Template
1.5 Self-Assembly of Rod-Like Viruses1.5.1 Controlled 1D Assembly; 1.5.1.1 TMV Head-to-Tail Assembly; 1.5.1.2 Conductive 1D TMV Composite Fibers; 1.5.1.3 Weaving M13 Bacteriophage into Robust Fibers; 1.5.1.4 Nanoring Structure; 1.5.2 Fabrication of Thin Films by 2D Self-Assembly; 1.5.3 Controlling the 3D Assembly of TMV and M13; 1.6 Virus-Based Device and Applications; 1.7 Outlook; References; 2: Biomimetic Nanoparticles Providing Molecularly Defined Binding Sites - Protein-Featuring Structures versus Molecularly Imprinted Polymers; 2.1 Introduction; 2.2 Core Materials and Functionalities 2.2.1 Inorganic Core Materials2.2.1.1 Inorganic Crystalline Nanoparticles; 2.2.1.2 Particles with Silica Cores; 2.2.1.3 Metals and Metal Oxides; 2.2.2 Organic Core Materials; 2.2.2.1 Polymers, Lipids and Fullerenes; 2.3 Functional Shells; 2.3.1 Organic Shells; 2.3.2 MIPs; 2.3.2.1 Tools for MIP Development; 2.3.2.2 Bulk MIP and Proteins; 2.3.2.3 Nanospheric MIPs in General; 2.3.2.4 Nanospheric MIPs and Proteins; 2.4 Applications; 2.4.1 Biopurification; 2.4.1.1 Magnetic Nanoparticles; 2.4.1.2 MIPs with Magnetizable Cores; 2.4.2 Drug Delivery and Drug Targeting 2.4.2.1 Nanoparticle Systems for Drug Delivery2.4.2.2 Ligands on Nanoparticle Surfaces; 2.4.2.3 Targeting of Specific Cells; 2.5 Products; 2.5.1 MIPs-Applications and Products; 2.5.2 Luminex Assay; 2.6 Conclusions; References; 3: Interaction Between Silica Particles and Human Epithelial Cells: Atomic Force Microscopy and Fluorescence Study; 3.1 Interaction of Silica with Biological Cells: Background; 3.2 Interaction of a Silica Particle with the Cell Surface: How It Is Seen with AFM; 3.2.1 AFM; 3.2.2 AFM on Cells; 3.2.2.1 Cell Culture; 3.2.2.2 AFM; 3.2.3 AFM Probe Preparations 3.2.4 Models to Analyze the Cell Surface: Need for a Two-Layer Model3.2.5 Experimental Data; 3.2.5.1 Surface Brush on Cancer and Normal Cells; 3.2.5.2 Measurement of Adhesion: Silica Particle-Cell Interaction; 3.2.5.3 Can the Difference in Adhesion Be Used to Detect Cancer Cells?; 3.3 Ultra-Bright Fluorescent Silica Particles to Be Used to Study Interaction with Cells; 3.4 Ultra-Bright Fluorescent Silica Particles to Distinguish Between Cancer and Normal Cells; 3.4.1 Methods and Materials; 3.4.1.1 Spectrofluorometric and Optical Measurements of the Particles Attached to Cells 3.4.1.2 Detection of Affinity of Fluorescent Silica Particles to Cells |
| Record Nr. | UNINA-9910829907103321 |
| Weinheim, : Wiley-VCH | ||
| 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 | ||
| ||