Coverart for item
The Resource Protein folding disorders of the central nervous system, edited by Jorge Ghiso, Agueda Rostagno

Protein folding disorders of the central nervous system, edited by Jorge Ghiso, Agueda Rostagno

Label
Protein folding disorders of the central nervous system
Title
Protein folding disorders of the central nervous system
Statement of responsibility
edited by Jorge Ghiso, Agueda Rostagno
Contributor
Subject
Language
eng
Summary
"This exciting new book explores the dark side of the molecular protein assembly bringing an updated view of how failures in the homeostatic mechanisms that efficiently regulate protein folding leads to the accumulation of structurally abnormal pathogenic assemblies, encompassing an emerging group of diseases collectively known as "Protein Folding Disorders." This complex and diverse group of chronic and progressive entities are bridged together by their relationship to structural transitions in the native state of specific proteinaceous components, which for reasons poorly understood, convert into polymeric aggregates that generate poorly soluble tissue deposits and which are considered today the culprit of the disease pathogenesis in their respective diseases. Despite the diversity in the amino acid sequence of the different proteins involved in these heterogeneous disorders, all the pathologic conformers can trigger cascades of events ultimately resulting in cell dysfunction and death with devastating clinical consequences in many of the most precious aspects of human existence including personality, cognition, memory, and skilled movements. This book, which is composed of a compilation of chapters authored by outstanding and well-published scientists in the respective fields currently performing active investigations at world renowned universities and research centers, focuses on the growing number of diseases associated with protein misfolding in the central nervous system. Individual chapters are dedicated to the most common neurodegenerative diseases associated with protein aggregation/fibrillization focusing on the nature of the pathogenic species and the cellular pathways involved in the molecular pathogenesis of Alzheimer's, Parkinson's, and Huntington's diseases as well as in Amyotrophic Lateral Sclerosis, and Prion disorders. A group of contributions is centered on the current knowledge of the intracellular pathways and subcellular organelles affected by the different disease conditions, while others are focused in the emerging pathogenic role of misfolded subunits assembled into neurotoxic soluble oligomers, and in the novel notion of the transmissibility of the protein misfolded species, an innovative concept until recently only accepted for Prion diseases. Lastly, a different set of chapters is dedicated to the evaluation of novel therapeutic strategies for these devastating diseases."--Publisher's website
Dewey number
616.83
Illustrations
illustrations
Index
index present
Literary form
non fiction
Nature of contents
  • dictionaries
  • bibliography
http://library.link/vocab/relatedWorkOrContributorName
  • Ghiso, Jorge,
  • Rostagno, Agueda,
http://library.link/vocab/subjectName
  • Central nervous system
  • Prion diseases
  • Protein folding
  • Proteins
Label
Protein folding disorders of the central nervous system, edited by Jorge Ghiso, Agueda Rostagno
Instantiates
Publication
Copyright
Bibliography note
Includes bibliographical references and index
Contents
  • ""Contents""; ""Preface""; ""List of Contributors""; ""List of Figures""; ""List of Tables""; ""Chapter 1 Misfolding, Aggregation, and Amyloid Formation: The Dark Side of Proteins""; ""1.1 Introduction""; ""1.2 Molecules associated with extra- and intracellular deposits of misfolded proteins""; ""1.3 Protein folding and misfolding: Gauging the nature of the pathogenic species""; ""1.4 Modulation of fibril formation: Lessons from cerebral amyloidosis""; ""1.4.1 Mutations""; ""1.4.2 Protein concentration: Effect of enhanced synthesis versus downregulated clearance""; ""1.4.3 Acidic pH""
  • ""1.4.4 Presence of metal ions""""1.4.5 Post-translational modifications""; ""1.5 Mechanisms of disease associated with protein misfolding""; ""1.5.1 Formation of ion channel-like structures""; ""1.5.2 Induction of apoptotic cell death mechanisms""; ""1.5.3 Mitochondrial dysfunction and oxidative stress""; ""1.5.4 Inflammation-mediated pathways""; ""1.6 Concluding remarks""; ""Acknowledgments""; ""References""; ""Chapter 2 Oligomers at the Synapse: Synaptic Dysfunction and Neurodegeneration""; ""2.1 Introduction""
  • ""2.2 Mechanisms of oligomer toxicity are related to protein conformation and misfolding""""2.3 Protein oligomers that interfere with synaptic function and the disorders they cause""; ""2.3.1 Alpha synuclein""; ""2.3.2 Tau""; ""2.3.3 Amyloid beta""; ""2.3.4 BRI2""; ""2.3.5 Huntingtin""; ""2.4 Other oligomeric proteins implicated in neurodegenerative disease""; ""2.5 A case study of one mechanism by which oligomers disrupt synaptic function: AÎ2O interference with zinc modulation of neurotransmission""; ""2.6 Conclusion""; ""Acknowledgment""; ""References""
  • ""Chapter 3 Prion-like Protein Seeding and the Pathobiology of Alzheimerâ#x80;#x99;s Disease""""3.1 Alzheimerâ#x80;#x99;s disease (AD) and the amyloid (AÎ2) cascade hypothesis""; ""3.1.1 AÎ2 plaque load and dementia""; ""3.1.2 Tauopathy and dementia""; ""3.1.3 Clinical trials""; ""3.1.4 Animal models and AD""; ""3.1.5 Complexity""; ""3.2 The prion paradigm""; ""3.3 The prion paradigm and AD""; ""3.3.1 Similarities between AÎ2 seeds and PrP-prions""; ""3.3.2 Evidence for the prion-like seeding of AÎ2 in humans""; ""3.3.3 Similarities between tau seeds and PrP-prions""
  • ""3.4 Wide range of prion-like mechanisms""""Acknowledgments""; ""References""; ""Chapter 4 The Tau Misfolding Pathway to Dementia""; ""4.1 Introduction to tauopathies""; ""4.2 Microtubule-associated protein (MAP) tau: Isoforms and normal physiology""; ""4.3 Post-translational modifications of tau and the implications in creating a toxic molecule""; ""4.3.1 Tau phosphorylation""; ""4.3.2 Acetylation""; ""4.3.3 Ubiquitination and protein degradation""; ""4.3.4 Proteolysis of tau""; ""4.4 Tau: Normal biological function and pathological gain of function""; ""4.4.1 Microtubules and tau in AD""
Control code
on1005539998
Extent
1 online resource (334 pages)
Form of item
online
Isbn
9789813222960
Other physical details
illustrations (some color)
Specific material designation
remote
System control number
(OCoLC)1005539998
Label
Protein folding disorders of the central nervous system, edited by Jorge Ghiso, Agueda Rostagno
Publication
Copyright
Bibliography note
Includes bibliographical references and index
Contents
  • ""Contents""; ""Preface""; ""List of Contributors""; ""List of Figures""; ""List of Tables""; ""Chapter 1 Misfolding, Aggregation, and Amyloid Formation: The Dark Side of Proteins""; ""1.1 Introduction""; ""1.2 Molecules associated with extra- and intracellular deposits of misfolded proteins""; ""1.3 Protein folding and misfolding: Gauging the nature of the pathogenic species""; ""1.4 Modulation of fibril formation: Lessons from cerebral amyloidosis""; ""1.4.1 Mutations""; ""1.4.2 Protein concentration: Effect of enhanced synthesis versus downregulated clearance""; ""1.4.3 Acidic pH""
  • ""1.4.4 Presence of metal ions""""1.4.5 Post-translational modifications""; ""1.5 Mechanisms of disease associated with protein misfolding""; ""1.5.1 Formation of ion channel-like structures""; ""1.5.2 Induction of apoptotic cell death mechanisms""; ""1.5.3 Mitochondrial dysfunction and oxidative stress""; ""1.5.4 Inflammation-mediated pathways""; ""1.6 Concluding remarks""; ""Acknowledgments""; ""References""; ""Chapter 2 Oligomers at the Synapse: Synaptic Dysfunction and Neurodegeneration""; ""2.1 Introduction""
  • ""2.2 Mechanisms of oligomer toxicity are related to protein conformation and misfolding""""2.3 Protein oligomers that interfere with synaptic function and the disorders they cause""; ""2.3.1 Alpha synuclein""; ""2.3.2 Tau""; ""2.3.3 Amyloid beta""; ""2.3.4 BRI2""; ""2.3.5 Huntingtin""; ""2.4 Other oligomeric proteins implicated in neurodegenerative disease""; ""2.5 A case study of one mechanism by which oligomers disrupt synaptic function: AÎ2O interference with zinc modulation of neurotransmission""; ""2.6 Conclusion""; ""Acknowledgment""; ""References""
  • ""Chapter 3 Prion-like Protein Seeding and the Pathobiology of Alzheimerâ#x80;#x99;s Disease""""3.1 Alzheimerâ#x80;#x99;s disease (AD) and the amyloid (AÎ2) cascade hypothesis""; ""3.1.1 AÎ2 plaque load and dementia""; ""3.1.2 Tauopathy and dementia""; ""3.1.3 Clinical trials""; ""3.1.4 Animal models and AD""; ""3.1.5 Complexity""; ""3.2 The prion paradigm""; ""3.3 The prion paradigm and AD""; ""3.3.1 Similarities between AÎ2 seeds and PrP-prions""; ""3.3.2 Evidence for the prion-like seeding of AÎ2 in humans""; ""3.3.3 Similarities between tau seeds and PrP-prions""
  • ""3.4 Wide range of prion-like mechanisms""""Acknowledgments""; ""References""; ""Chapter 4 The Tau Misfolding Pathway to Dementia""; ""4.1 Introduction to tauopathies""; ""4.2 Microtubule-associated protein (MAP) tau: Isoforms and normal physiology""; ""4.3 Post-translational modifications of tau and the implications in creating a toxic molecule""; ""4.3.1 Tau phosphorylation""; ""4.3.2 Acetylation""; ""4.3.3 Ubiquitination and protein degradation""; ""4.3.4 Proteolysis of tau""; ""4.4 Tau: Normal biological function and pathological gain of function""; ""4.4.1 Microtubules and tau in AD""
Control code
on1005539998
Extent
1 online resource (334 pages)
Form of item
online
Isbn
9789813222960
Other physical details
illustrations (some color)
Specific material designation
remote
System control number
(OCoLC)1005539998

Library Locations

    • InternetBorrow it
      Albany, Auckland, 0632, NZ
Processing Feedback ...