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Transmissible spongiform encephalopathies (TSE), known as prion diseases, have been recognized for nearly 300 years in animals and almost 100 years in humans. Modern studies, including the protein-misfolding cyclic amplification (PMCA), have greatly advanced our understanding of the pathogenesis of prion diseases and facilitated the identification of new prion diseases in animals and humans. In the second edition of Prions and Diseases, more than 60 leading researchers and clinicians worldwide provide an up-to-date discussion of these unique infectious pathogens and their associated diseases.…mehr
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Transmissible spongiform encephalopathies (TSE), known as prion diseases, have been recognized for nearly 300 years in animals and almost 100 years in humans. Modern studies, including the protein-misfolding cyclic amplification (PMCA), have greatly advanced our understanding of the pathogenesis of prion diseases and facilitated the identification of new prion diseases in animals and humans. In the second edition of Prions and Diseases, more than 60 leading researchers and clinicians worldwide provide an up-to-date discussion of these unique infectious pathogens and their associated diseases. The book provides up-to-date knowledge about the etiology, pathogenesis, classification, histopathological, and clinical aspects of the full range of animal and human prion diseases. As a result, the book contains by far the most authoritative views about the past, present, and future of prions and prion diseases. The new second edition covers such important emerging topics such as inherited human prion disease, stem-cell models in prion research, human prion disease surveillance, and gene therapy strategies.
Produktdetails
- Produktdetails
- Verlag: Springer International Publishing
- Erscheinungstermin: 1. Januar 2023
- Englisch
- ISBN-13: 9783031205651
- Artikelnr.: 67152080
- Verlag: Springer International Publishing
- Erscheinungstermin: 1. Januar 2023
- Englisch
- ISBN-13: 9783031205651
- Artikelnr.: 67152080
Wen-Quan Zou, MD, PhD is Professor of Pathology at Case Western University School of Medicine, and he is Associate Director of the National Prion Disease Pathology Surveillance Center.
Pierluigi Gambetti, MD, is Professor of Pathology and Neurology at Case Western University School of Medicine.
Pierluigi Gambetti, MD, is Professor of Pathology and Neurology at Case Western University School of Medicine.
Part I: HISTORY.- Chapter 1: Transmissible Spongiform Encephalopathy: from its beginnings to Daniel Carleton Gajdusek.- Part II: GENERAL ASPECTS OF PRIONS.- Chapter 2: The Rich Chemistry of the Copper and Zinc Sites in Cellular Prion Protein.- Chapter 3: Mammalian Prion Structures.- Chapter 4: Insoluble Cellular Prion Protein and Other Neurodegeneration-related Misfolded Protein Aggregates in the Brain of Asymptomatic Individuals.- Part III: CONVERSION AND STRAIN OF PRIONS.- Chapter 5: Prion Conversion and Deformed Templating.- Chapter 6: Prion Strain Interference.- Chapter 7: Molecular Mechanisms Encoding Strains of Prions and Prion-Like Misfolded Proteins.- Chapter 8: Cofactor Involvement in Prion Propagation.- Chapter 9: Prion Protein Conversion and Lipids.- Part IV: ENVIRONMENT AND TRANSMISSION OF PRIONS.- Chapter 10: Prions in the Environment.- Chapter 11: Environmentally Acquired Transmissible Spongiform Encephalopathy.- Chapter 12: Risk of Transmission of Creutzfeldt-Jakob Disease by Blood Transfusion.- Chapter 13: Species Barriers in Prion Disease.- Part V: MODELLING OF PRIONS.- Chapter 14: Modeling the Cell Biology of Prions.- Chapter 15: Transgenic Mice Modelling in Prion Diseases.- Chapter 16: Stem Cell Models in Prion Research.- Chapter 17: Drosophila Models of Prion Diseases.- Part VI: HUMAN PRION DISEASES AND OTHER PATHOLOGIES.- Chapter 18: Human Sporadic Prion Diseases.- Chapter 19 Genetic Creutzfeldt-Jakob and Gerstmann-Sträussler-Scheinker Diseases.- Chapter 20: Glycoform-selective Prions in Sporadic and Inherited Variably Protease-sensitive Prionopathies.- Chapter 21: The Spectrum of Tau Pathology in Human Prion Disease.- Chapter 22: Prion Protein Complex with mGluR5 Mediates Amyloid-ß Synaptic Loss in Alzheimer’s Disease.- Chapter 23: Prion and Cancers.- Chapter 24: Protective Role of Cellular Prion Protein in Tissue Ischemic/Reperfusion Injury.- Part VII: ANIMAL PRION DISEASES.- Chapter 25: Bovine Spongiform Encephalopathy.- Chapter 26: Classical and Atypical Scrapie in Sheep and Goats.- Chapter 27: Research models for studying chronic wasting disease.- Part VIII: YEAST PRIONS.- Chapter 28: Introduction to Yeast and Fungal Prions.- Chapter 29: Yeast Prions Are Folded, In-Register Parallel Amyloids Subject to Multiple Anti-prion Systems.- Part IX: DIAGNOSIS AND HUMAN PRION SURVEILLANCE.- Chapter 30: Real-time quaking-induced conversion (QuIC) assays for the detection and diagnosis of human prion diseases.- Chapter 31: Protein Misfolding Cyclic Amplification.- Chapter 32: Skin Misfolded Proteins as Biomarkers for Diagnosis of Prion and Prion-like Diseases.- Chapter 33: Diagnosis of Prion Disease: Conventional Approaches.- Chapter 34: Human Prion Disease Surveillance.- Part X: TREATMENT.- Chapter 35: Overview on Treatment of Prion Diseases and Decontamination of Prions.- Chapter 36: Gene Therapy Strategies for Prophylactic and Therapeutic Treatments of Human Prion Diseases.- Chapter 37: Immunomodulation.
Part I: HISTORY.- Chapter 1: Transmissible Spongiform Encephalopathy: from its beginnings to Daniel Carleton Gajdusek.- Part II: GENERAL ASPECTS OF PRIONS.- Chapter 2: The Rich Chemistry of the Copper and Zinc Sites in Cellular Prion Protein.- Chapter 3: Mammalian Prion Structures.- Chapter 4: Insoluble Cellular Prion Protein and Other Neurodegeneration-related Misfolded Protein Aggregates in the Brain of Asymptomatic Individuals.- Part III: CONVERSION AND STRAIN OF PRIONS.- Chapter 5: Prion Conversion and Deformed Templating.- Chapter 6: Prion Strain Interference.- Chapter 7: Molecular Mechanisms Encoding Strains of Prions and Prion-Like Misfolded Proteins.- Chapter 8: Cofactor Involvement in Prion Propagation.- Chapter 9: Prion Protein Conversion and Lipids.- Part IV: ENVIRONMENT AND TRANSMISSION OF PRIONS.- Chapter 10: Prions in the Environment.- Chapter 11: Environmentally Acquired Transmissible Spongiform Encephalopathy.- Chapter 12: Risk of Transmission of Creutzfeldt-Jakob Disease by Blood Transfusion.- Chapter 13: Species Barriers in Prion Disease.- Part V: MODELLING OF PRIONS.- Chapter 14: Modeling the Cell Biology of Prions.- Chapter 15: Transgenic Mice Modelling in Prion Diseases.- Chapter 16: Stem Cell Models in Prion Research.- Chapter 17: Drosophila Models of Prion Diseases.- Part VI: HUMAN PRION DISEASES AND OTHER PATHOLOGIES.- Chapter 18: Human Sporadic Prion Diseases.- Chapter 19 Genetic Creutzfeldt-Jakob and Gerstmann-Sträussler-Scheinker Diseases.- Chapter 20: Glycoform-selective Prions in Sporadic and Inherited Variably Protease-sensitive Prionopathies.- Chapter 21: The Spectrum of Tau Pathology in Human Prion Disease.- Chapter 22: Prion Protein Complex with mGluR5 Mediates Amyloid-ß Synaptic Loss in Alzheimer's Disease.- Chapter 23: Prion and Cancers.- Chapter 24: Protective Role of Cellular Prion Protein in Tissue Ischemic/Reperfusion Injury.- Part VII: ANIMAL PRION DISEASES.- Chapter 25: Bovine Spongiform Encephalopathy.- Chapter 26: Classical and Atypical Scrapie in Sheep and Goats.- Chapter 27: Research models for studying chronic wasting disease.- Part VIII: YEAST PRIONS.- Chapter 28: Introduction to Yeast and Fungal Prions.- Chapter 29: Yeast Prions Are Folded, In-Register Parallel Amyloids Subject to Multiple Anti-prion Systems.- Part IX: DIAGNOSIS AND HUMAN PRION SURVEILLANCE.- Chapter 30: Real-time quaking-induced conversion (QuIC) assays for the detection and diagnosis of human prion diseases.- Chapter 31: Protein Misfolding Cyclic Amplification.- Chapter 32: Skin Misfolded Proteins as Biomarkers for Diagnosis of Prion and Prion-like Diseases.- Chapter 33: Diagnosis of Prion Disease: Conventional Approaches.- Chapter 34: Human Prion Disease Surveillance.- Part X: TREATMENT.- Chapter 35: Overview on Treatment of Prion Diseases and Decontamination of Prions.- Chapter 36: Gene Therapy Strategies for Prophylactic and Therapeutic Treatments of Human Prion Diseases.- Chapter 37: Immunomodulation.
Part I: HISTORY.- Chapter 1: Transmissible Spongiform Encephalopathy: from its beginnings to Daniel Carleton Gajdusek.- Part II: GENERAL ASPECTS OF PRIONS.- Chapter 2: The Rich Chemistry of the Copper and Zinc Sites in Cellular Prion Protein.- Chapter 3: Mammalian Prion Structures.- Chapter 4: Insoluble Cellular Prion Protein and Other Neurodegeneration-related Misfolded Protein Aggregates in the Brain of Asymptomatic Individuals.- Part III: CONVERSION AND STRAIN OF PRIONS.- Chapter 5: Prion Conversion and Deformed Templating.- Chapter 6: Prion Strain Interference.- Chapter 7: Molecular Mechanisms Encoding Strains of Prions and Prion-Like Misfolded Proteins.- Chapter 8: Cofactor Involvement in Prion Propagation.- Chapter 9: Prion Protein Conversion and Lipids.- Part IV: ENVIRONMENT AND TRANSMISSION OF PRIONS.- Chapter 10: Prions in the Environment.- Chapter 11: Environmentally Acquired Transmissible Spongiform Encephalopathy.- Chapter 12: Risk of Transmission of Creutzfeldt-Jakob Disease by Blood Transfusion.- Chapter 13: Species Barriers in Prion Disease.- Part V: MODELLING OF PRIONS.- Chapter 14: Modeling the Cell Biology of Prions.- Chapter 15: Transgenic Mice Modelling in Prion Diseases.- Chapter 16: Stem Cell Models in Prion Research.- Chapter 17: Drosophila Models of Prion Diseases.- Part VI: HUMAN PRION DISEASES AND OTHER PATHOLOGIES.- Chapter 18: Human Sporadic Prion Diseases.- Chapter 19 Genetic Creutzfeldt-Jakob and Gerstmann-Sträussler-Scheinker Diseases.- Chapter 20: Glycoform-selective Prions in Sporadic and Inherited Variably Protease-sensitive Prionopathies.- Chapter 21: The Spectrum of Tau Pathology in Human Prion Disease.- Chapter 22: Prion Protein Complex with mGluR5 Mediates Amyloid-ß Synaptic Loss in Alzheimer’s Disease.- Chapter 23: Prion and Cancers.- Chapter 24: Protective Role of Cellular Prion Protein in Tissue Ischemic/Reperfusion Injury.- Part VII: ANIMAL PRION DISEASES.- Chapter 25: Bovine Spongiform Encephalopathy.- Chapter 26: Classical and Atypical Scrapie in Sheep and Goats.- Chapter 27: Research models for studying chronic wasting disease.- Part VIII: YEAST PRIONS.- Chapter 28: Introduction to Yeast and Fungal Prions.- Chapter 29: Yeast Prions Are Folded, In-Register Parallel Amyloids Subject to Multiple Anti-prion Systems.- Part IX: DIAGNOSIS AND HUMAN PRION SURVEILLANCE.- Chapter 30: Real-time quaking-induced conversion (QuIC) assays for the detection and diagnosis of human prion diseases.- Chapter 31: Protein Misfolding Cyclic Amplification.- Chapter 32: Skin Misfolded Proteins as Biomarkers for Diagnosis of Prion and Prion-like Diseases.- Chapter 33: Diagnosis of Prion Disease: Conventional Approaches.- Chapter 34: Human Prion Disease Surveillance.- Part X: TREATMENT.- Chapter 35: Overview on Treatment of Prion Diseases and Decontamination of Prions.- Chapter 36: Gene Therapy Strategies for Prophylactic and Therapeutic Treatments of Human Prion Diseases.- Chapter 37: Immunomodulation.
Part I: HISTORY.- Chapter 1: Transmissible Spongiform Encephalopathy: from its beginnings to Daniel Carleton Gajdusek.- Part II: GENERAL ASPECTS OF PRIONS.- Chapter 2: The Rich Chemistry of the Copper and Zinc Sites in Cellular Prion Protein.- Chapter 3: Mammalian Prion Structures.- Chapter 4: Insoluble Cellular Prion Protein and Other Neurodegeneration-related Misfolded Protein Aggregates in the Brain of Asymptomatic Individuals.- Part III: CONVERSION AND STRAIN OF PRIONS.- Chapter 5: Prion Conversion and Deformed Templating.- Chapter 6: Prion Strain Interference.- Chapter 7: Molecular Mechanisms Encoding Strains of Prions and Prion-Like Misfolded Proteins.- Chapter 8: Cofactor Involvement in Prion Propagation.- Chapter 9: Prion Protein Conversion and Lipids.- Part IV: ENVIRONMENT AND TRANSMISSION OF PRIONS.- Chapter 10: Prions in the Environment.- Chapter 11: Environmentally Acquired Transmissible Spongiform Encephalopathy.- Chapter 12: Risk of Transmission of Creutzfeldt-Jakob Disease by Blood Transfusion.- Chapter 13: Species Barriers in Prion Disease.- Part V: MODELLING OF PRIONS.- Chapter 14: Modeling the Cell Biology of Prions.- Chapter 15: Transgenic Mice Modelling in Prion Diseases.- Chapter 16: Stem Cell Models in Prion Research.- Chapter 17: Drosophila Models of Prion Diseases.- Part VI: HUMAN PRION DISEASES AND OTHER PATHOLOGIES.- Chapter 18: Human Sporadic Prion Diseases.- Chapter 19 Genetic Creutzfeldt-Jakob and Gerstmann-Sträussler-Scheinker Diseases.- Chapter 20: Glycoform-selective Prions in Sporadic and Inherited Variably Protease-sensitive Prionopathies.- Chapter 21: The Spectrum of Tau Pathology in Human Prion Disease.- Chapter 22: Prion Protein Complex with mGluR5 Mediates Amyloid-ß Synaptic Loss in Alzheimer's Disease.- Chapter 23: Prion and Cancers.- Chapter 24: Protective Role of Cellular Prion Protein in Tissue Ischemic/Reperfusion Injury.- Part VII: ANIMAL PRION DISEASES.- Chapter 25: Bovine Spongiform Encephalopathy.- Chapter 26: Classical and Atypical Scrapie in Sheep and Goats.- Chapter 27: Research models for studying chronic wasting disease.- Part VIII: YEAST PRIONS.- Chapter 28: Introduction to Yeast and Fungal Prions.- Chapter 29: Yeast Prions Are Folded, In-Register Parallel Amyloids Subject to Multiple Anti-prion Systems.- Part IX: DIAGNOSIS AND HUMAN PRION SURVEILLANCE.- Chapter 30: Real-time quaking-induced conversion (QuIC) assays for the detection and diagnosis of human prion diseases.- Chapter 31: Protein Misfolding Cyclic Amplification.- Chapter 32: Skin Misfolded Proteins as Biomarkers for Diagnosis of Prion and Prion-like Diseases.- Chapter 33: Diagnosis of Prion Disease: Conventional Approaches.- Chapter 34: Human Prion Disease Surveillance.- Part X: TREATMENT.- Chapter 35: Overview on Treatment of Prion Diseases and Decontamination of Prions.- Chapter 36: Gene Therapy Strategies for Prophylactic and Therapeutic Treatments of Human Prion Diseases.- Chapter 37: Immunomodulation.