Author: Daniel Erik Otzen
Publisher: John Wiley & Sons
ISBN: 3527654208
Category : Science
Languages : en
Pages : 496
Book Description
Summing up almost a decade of biomedical research, this topical and eagerly awaited handbook is the first reference on the topic to incorporate recent breakthroughs in amyloid research. The first part covers the structural biology of amyloid fibrils and pre-fibrillar assemblies, including a description of current models for amyloid formation. The second part looks at the diagnosis and biomedical study of amyloid in humans and in animal models, while the final section discusses pharmacological approaches to manipulating amyloid and also looks at its physiological roles in lower and higher organisms. For Biochemists, Molecular Biologists, Neurobiologists, Neurophysiologists and those working in the Pharmaceutical Industry.
Amyloid Fibrils and Prefibrillar Aggregates
Author: Daniel Erik Otzen
Publisher: John Wiley & Sons
ISBN: 3527654208
Category : Science
Languages : en
Pages : 496
Book Description
Summing up almost a decade of biomedical research, this topical and eagerly awaited handbook is the first reference on the topic to incorporate recent breakthroughs in amyloid research. The first part covers the structural biology of amyloid fibrils and pre-fibrillar assemblies, including a description of current models for amyloid formation. The second part looks at the diagnosis and biomedical study of amyloid in humans and in animal models, while the final section discusses pharmacological approaches to manipulating amyloid and also looks at its physiological roles in lower and higher organisms. For Biochemists, Molecular Biologists, Neurobiologists, Neurophysiologists and those working in the Pharmaceutical Industry.
Publisher: John Wiley & Sons
ISBN: 3527654208
Category : Science
Languages : en
Pages : 496
Book Description
Summing up almost a decade of biomedical research, this topical and eagerly awaited handbook is the first reference on the topic to incorporate recent breakthroughs in amyloid research. The first part covers the structural biology of amyloid fibrils and pre-fibrillar assemblies, including a description of current models for amyloid formation. The second part looks at the diagnosis and biomedical study of amyloid in humans and in animal models, while the final section discusses pharmacological approaches to manipulating amyloid and also looks at its physiological roles in lower and higher organisms. For Biochemists, Molecular Biologists, Neurobiologists, Neurophysiologists and those working in the Pharmaceutical Industry.
Molecular Pathology of Alzheimer's Disease
Author: Rudy Castellani
Publisher: Biota Publishing
ISBN: 1615046399
Category : Health & Fitness
Languages : en
Pages : 93
Book Description
Alzheimer’s Disease is characterized pathologically by two principal hallmark lesions: the senile plaque and the neurofibrillary tangle. Since the identification of each over 100 years ago, the major protein components have been elucidated. This has led in turn to the elaboration of metabolic cascades involving amyloid-β production in the case of the senile plaque, and phosphorylated-tau protein in the case of the neurofibrillary tangle. The pathogenesis and histogenesis of each have been the source of extensive investigation and some controversy in recent years, as both cascades have been implicated in the pathogenesis of Alzheimer’s Disease, relied upon in the diagnostic criteria for Alzheimer’s Disease at autopsy, and targeted for therapeutic intervention. With the accumulation of data and expansion of knowledge of the molecular biology of Alzheimer’s Disease, it appears that the enthusiasm for successful intervention has been premature. In this book, we detail the discovery and characterization of the major pathological lesions, their associated molecular biology, their relationship to clinical disease, and potential fundamental errors in understanding that may be leading scientific investigators in unintended directions.
Publisher: Biota Publishing
ISBN: 1615046399
Category : Health & Fitness
Languages : en
Pages : 93
Book Description
Alzheimer’s Disease is characterized pathologically by two principal hallmark lesions: the senile plaque and the neurofibrillary tangle. Since the identification of each over 100 years ago, the major protein components have been elucidated. This has led in turn to the elaboration of metabolic cascades involving amyloid-β production in the case of the senile plaque, and phosphorylated-tau protein in the case of the neurofibrillary tangle. The pathogenesis and histogenesis of each have been the source of extensive investigation and some controversy in recent years, as both cascades have been implicated in the pathogenesis of Alzheimer’s Disease, relied upon in the diagnostic criteria for Alzheimer’s Disease at autopsy, and targeted for therapeutic intervention. With the accumulation of data and expansion of knowledge of the molecular biology of Alzheimer’s Disease, it appears that the enthusiasm for successful intervention has been premature. In this book, we detail the discovery and characterization of the major pathological lesions, their associated molecular biology, their relationship to clinical disease, and potential fundamental errors in understanding that may be leading scientific investigators in unintended directions.
Lipids and Cellular Membranes in Amyloid Diseases
Author: Raz Jelinek
Publisher: John Wiley & Sons
ISBN: 3527634339
Category : Science
Languages : en
Pages : 431
Book Description
Addressing one of the biggest riddles in current molecular cell biology, this ground-breaking monograph builds the case for the crucial involvement of lipids and membranes in the formation of amyloid deposits. Tying together recent knowledge from in vitro and in vivo studes, and built on a sound biophysical and biochemical foundation, this overview brings the reader up to date with current models of the interplay between membranes and amyloid formation. Required reading for any researcher interested in amyloid formation and amyloid toxicity, and possible avenues for the prevention or treatment of neurodegenerative disorders. From the contents: * Interactions of Alpha-Synuclein with Lipids * Interaction of hIAPP and its Precursors with Membranes * Amyloid Polymorphisms: Structural Basis and Significance in Biology and Molecular Medicine * The Role of Lipid Rafts in Alzheimer's Disease * Alzheimer's Disease as a Membrane-Associated Enzymopathy of Beta-Amyloid Precursor Protein (APP) Secretases * Impaired Regulation of Glutamate Receptor Channels and Signaling Molecules by Beta-Amyloid in Alzheimer's Disease * Membrane Changes in BSE and Scrapie * Experimental Approaches and Technical Challenges for Studying Amyloid-Membrane Interactions and more
Publisher: John Wiley & Sons
ISBN: 3527634339
Category : Science
Languages : en
Pages : 431
Book Description
Addressing one of the biggest riddles in current molecular cell biology, this ground-breaking monograph builds the case for the crucial involvement of lipids and membranes in the formation of amyloid deposits. Tying together recent knowledge from in vitro and in vivo studes, and built on a sound biophysical and biochemical foundation, this overview brings the reader up to date with current models of the interplay between membranes and amyloid formation. Required reading for any researcher interested in amyloid formation and amyloid toxicity, and possible avenues for the prevention or treatment of neurodegenerative disorders. From the contents: * Interactions of Alpha-Synuclein with Lipids * Interaction of hIAPP and its Precursors with Membranes * Amyloid Polymorphisms: Structural Basis and Significance in Biology and Molecular Medicine * The Role of Lipid Rafts in Alzheimer's Disease * Alzheimer's Disease as a Membrane-Associated Enzymopathy of Beta-Amyloid Precursor Protein (APP) Secretases * Impaired Regulation of Glutamate Receptor Channels and Signaling Molecules by Beta-Amyloid in Alzheimer's Disease * Membrane Changes in BSE and Scrapie * Experimental Approaches and Technical Challenges for Studying Amyloid-Membrane Interactions and more
Tau oligomers
Author: Jesus Avila
Publisher: Frontiers E-books
ISBN: 288919261X
Category : Medicine (General)
Languages : en
Pages : 114
Book Description
Neurofibrillary tangles (NFTs) composed of intracellular aggregates of tau protein are a key neuropathological feature of Alzheimer’s Disease (AD) and other neurodegenerative diseases, collectively termed tauopathies. The abundance of NFTs has been reported to correlate positively with the severity of cognitive impairment in AD. However, accumulating evidences derived from studies of experimental models have identified that NFTs themselves may not be neurotoxic. Now, many of tau researchers are seeking a “toxic” form of tau protein. Moreover, it was suggested that a “toxic” tau was capable to seed aggregation of native tau protein and to propagate in a prion-like manner. However, the exact neurotoxic tau species remain unclear. Because mature tangles seem to be non-toxic component, “tau oligomers” as the candidate of “toxic” tau have been investigated for more than one decade. In this topic, we will discuss our consensus of “tau oligomers” because the term of “tau oligomers” [e.g. dimer (disulfide bond-dependent or independent), multimer (more than dimer), granular (definition by EM or AFM) and maybe small filamentous aggregates] has been used by each researchers definition. From a biochemical point of view, tau protein has several unique characteristics such as natively unfolded conformation, thermo-stability, acid-stability, and capability of post-translational modifications. Although tau protein research has been continued for a long time, we are still missing the mechanisms of NFT formation. It is unclear how the conversion is occurred from natively unfolded protein to abnormally mis-folded protein. It remains unknown how tau protein can be formed filaments [e.g. paired helical filament (PHF), straight filament and twisted filament] in cells albeit in vitro studies confirmed tau self-assembly by several inducing factors. Researchers are still debating whether tau oligomerization is primary event rather than tau phosphorylation in the tau pathogenesis. Inhibition of either tau phosphorylation or aggregation has been investigated for the prevention of tauopathies, however, it will make an irrelevant result if we don’t know an exact target of neurotoxicity. It is a time to have a consensus of definition, terminology and methodology for the identification of “tau oligomers”.
Publisher: Frontiers E-books
ISBN: 288919261X
Category : Medicine (General)
Languages : en
Pages : 114
Book Description
Neurofibrillary tangles (NFTs) composed of intracellular aggregates of tau protein are a key neuropathological feature of Alzheimer’s Disease (AD) and other neurodegenerative diseases, collectively termed tauopathies. The abundance of NFTs has been reported to correlate positively with the severity of cognitive impairment in AD. However, accumulating evidences derived from studies of experimental models have identified that NFTs themselves may not be neurotoxic. Now, many of tau researchers are seeking a “toxic” form of tau protein. Moreover, it was suggested that a “toxic” tau was capable to seed aggregation of native tau protein and to propagate in a prion-like manner. However, the exact neurotoxic tau species remain unclear. Because mature tangles seem to be non-toxic component, “tau oligomers” as the candidate of “toxic” tau have been investigated for more than one decade. In this topic, we will discuss our consensus of “tau oligomers” because the term of “tau oligomers” [e.g. dimer (disulfide bond-dependent or independent), multimer (more than dimer), granular (definition by EM or AFM) and maybe small filamentous aggregates] has been used by each researchers definition. From a biochemical point of view, tau protein has several unique characteristics such as natively unfolded conformation, thermo-stability, acid-stability, and capability of post-translational modifications. Although tau protein research has been continued for a long time, we are still missing the mechanisms of NFT formation. It is unclear how the conversion is occurred from natively unfolded protein to abnormally mis-folded protein. It remains unknown how tau protein can be formed filaments [e.g. paired helical filament (PHF), straight filament and twisted filament] in cells albeit in vitro studies confirmed tau self-assembly by several inducing factors. Researchers are still debating whether tau oligomerization is primary event rather than tau phosphorylation in the tau pathogenesis. Inhibition of either tau phosphorylation or aggregation has been investigated for the prevention of tauopathies, however, it will make an irrelevant result if we don’t know an exact target of neurotoxicity. It is a time to have a consensus of definition, terminology and methodology for the identification of “tau oligomers”.
Protein Folding, Misfolding and Aggregation
Author: Victor Muñoz
Publisher: Royal Society of Chemistry
ISBN: 0854042571
Category : Science
Languages : en
Pages : 290
Book Description
Protein folding and aggregation is the process by which newly synthesized proteins fold into the specific three-dimensional structures defining their biologically active states. It has always been a major focus of research in biochemistry and has often been seen as the unsolved second part of the genetic code. In the last 10 years we have witnessed a quantum leap in the research in this exciting area. Computational methods have improved to the extent of making possible to simulate the complete folding process of small proteins and the early stages of protein aggregation. Experimental methods h.
Publisher: Royal Society of Chemistry
ISBN: 0854042571
Category : Science
Languages : en
Pages : 290
Book Description
Protein folding and aggregation is the process by which newly synthesized proteins fold into the specific three-dimensional structures defining their biologically active states. It has always been a major focus of research in biochemistry and has often been seen as the unsolved second part of the genetic code. In the last 10 years we have witnessed a quantum leap in the research in this exciting area. Computational methods have improved to the extent of making possible to simulate the complete folding process of small proteins and the early stages of protein aggregation. Experimental methods h.
Amyloidosis: New Insights for the Healthcare Professional: 2012 Edition
Author:
Publisher: ScholarlyEditions
ISBN: 1464974411
Category : Medical
Languages : en
Pages : 61
Book Description
Amyloidosis: New Insights for the Healthcare Professional / 2012 Edition is a ScholarlyBrief™ that delivers timely, authoritative, comprehensive, and specialized information about Amyloidosis in a concise format. The editors have built Amyloidosis: New Insights for the Healthcare Professional / 2012 Edition on the vast information databases of ScholarlyNews.™ You can expect the information about Amyloidosis in this eBook to be deeper than what you can access anywhere else, as well as consistently reliable, authoritative, informed, and relevant. The content of Amyloidosis: New Insights for the Healthcare Professional / 2012 Edition has been produced by the world’s leading scientists, engineers, analysts, research institutions, and companies. All of the content is from peer-reviewed sources, and all of it is written, assembled, and edited by the editors at ScholarlyEditions™ and available exclusively from us. You now have a source you can cite with authority, confidence, and credibility. More information is available at http://www.ScholarlyEditions.com/.
Publisher: ScholarlyEditions
ISBN: 1464974411
Category : Medical
Languages : en
Pages : 61
Book Description
Amyloidosis: New Insights for the Healthcare Professional / 2012 Edition is a ScholarlyBrief™ that delivers timely, authoritative, comprehensive, and specialized information about Amyloidosis in a concise format. The editors have built Amyloidosis: New Insights for the Healthcare Professional / 2012 Edition on the vast information databases of ScholarlyNews.™ You can expect the information about Amyloidosis in this eBook to be deeper than what you can access anywhere else, as well as consistently reliable, authoritative, informed, and relevant. The content of Amyloidosis: New Insights for the Healthcare Professional / 2012 Edition has been produced by the world’s leading scientists, engineers, analysts, research institutions, and companies. All of the content is from peer-reviewed sources, and all of it is written, assembled, and edited by the editors at ScholarlyEditions™ and available exclusively from us. You now have a source you can cite with authority, confidence, and credibility. More information is available at http://www.ScholarlyEditions.com/.
Amyloid and Amyloidosis
Author: Gilles Grateau
Publisher: CRC Press
ISBN: 1420037498
Category : Medical
Languages : en
Pages : 577
Book Description
This authoritative volume contains 179 chapters by international experts on recent developments in our understanding of amyloid proteins, protein folding disorders, and new and proposed clinical trials in amyloidosis. Topics include detection and characterization techniques; biological functions; genetics; disorders, diagnosis, and treatments, incl
Publisher: CRC Press
ISBN: 1420037498
Category : Medical
Languages : en
Pages : 577
Book Description
This authoritative volume contains 179 chapters by international experts on recent developments in our understanding of amyloid proteins, protein folding disorders, and new and proposed clinical trials in amyloidosis. Topics include detection and characterization techniques; biological functions; genetics; disorders, diagnosis, and treatments, incl
Peptide Catalysts, including Catalytic Amyloids
Author:
Publisher: Elsevier
ISBN: 0443236682
Category : Science
Languages : en
Pages : 550
Book Description
Peptide Catalysts, including Catalytic Amyloids, Volume 697 in this esteemed series, highlights new advances in the field, with this new volume presenting interesting topics on Screening of oxidative behaviors in catalytic amyloid assemblies, Catalytic amyloids derived for natural proteins, AFM-IR studies of catalytic amyloids, MD structural studies of catalytic amyloids, Characterization of crystalline, amyloid-like amino acid assemblies, Computational modeling of supramolecular peptide assemblies, and Assembly and activity of short prion-inspired peptides. - Provides the authority and expertise of leading contributors from an international board of authors - Presents the latest release in Methods in Enzymology series - Updated release includes the latest information on Peptide Catalysts, including Catalytic Amyloids
Publisher: Elsevier
ISBN: 0443236682
Category : Science
Languages : en
Pages : 550
Book Description
Peptide Catalysts, including Catalytic Amyloids, Volume 697 in this esteemed series, highlights new advances in the field, with this new volume presenting interesting topics on Screening of oxidative behaviors in catalytic amyloid assemblies, Catalytic amyloids derived for natural proteins, AFM-IR studies of catalytic amyloids, MD structural studies of catalytic amyloids, Characterization of crystalline, amyloid-like amino acid assemblies, Computational modeling of supramolecular peptide assemblies, and Assembly and activity of short prion-inspired peptides. - Provides the authority and expertise of leading contributors from an international board of authors - Presents the latest release in Methods in Enzymology series - Updated release includes the latest information on Peptide Catalysts, including Catalytic Amyloids
Bio-nanoimaging
Author: Vladimir N Uversky
Publisher: Academic Press
ISBN: 0123978211
Category : Science
Languages : en
Pages : 556
Book Description
Bio-Nanoimaging: Protein Misfolding & Aggregation provides a unique introduction to both novel and established nanoimaging techniques for visualization and characterization of misfolded and aggregated protein species. The book is divided into three sections covering: - Nanotechnology and nanoimaging technology, including cryoelectron microscopy of beta(2)-microglobulin, studying amyloidogensis by FRET; and scanning tunneling microscopy of protein deposits - Polymorphisms of protein misfolded and aggregated species, including fibrillar polymorphism, amyloid-like protofibrils, and insulin oligomers - Polymorphisms of misfolding and aggregation processes, including multiple pathways of lysozyme aggregation, misfolded intermediate of a PDZ domain, and micelle formation by human islet amyloid polypeptide Protein misfolding and aggregation is a fast-growing frontier in molecular medicine and protein chemistry. Related disorders include cataracts, arthritis, cystic fibrosis, late-onset diabetes mellitus, and numerous neurodegenerative diseases like Alzheimer's and Parkinson's. Nanoimaging technology has proved crucial in understanding protein-misfolding pathologies and in potential drug design aimed at the inhibition or reversal of protein aggregation. Using these technologies, researchers can monitor the aggregation process, visualize protein aggregates and analyze their properties. - Provides practical examples of nanoimaging research from leading molecular biology, cell biology, protein chemistry, biotechnology, genetics, and pharmaceutical labs - Includes over 200 color images to illustrate the power of various nanoimaging technologies - Focuses on nanoimaging techniques applied to protein misfolding and aggregation in molecular medicine
Publisher: Academic Press
ISBN: 0123978211
Category : Science
Languages : en
Pages : 556
Book Description
Bio-Nanoimaging: Protein Misfolding & Aggregation provides a unique introduction to both novel and established nanoimaging techniques for visualization and characterization of misfolded and aggregated protein species. The book is divided into three sections covering: - Nanotechnology and nanoimaging technology, including cryoelectron microscopy of beta(2)-microglobulin, studying amyloidogensis by FRET; and scanning tunneling microscopy of protein deposits - Polymorphisms of protein misfolded and aggregated species, including fibrillar polymorphism, amyloid-like protofibrils, and insulin oligomers - Polymorphisms of misfolding and aggregation processes, including multiple pathways of lysozyme aggregation, misfolded intermediate of a PDZ domain, and micelle formation by human islet amyloid polypeptide Protein misfolding and aggregation is a fast-growing frontier in molecular medicine and protein chemistry. Related disorders include cataracts, arthritis, cystic fibrosis, late-onset diabetes mellitus, and numerous neurodegenerative diseases like Alzheimer's and Parkinson's. Nanoimaging technology has proved crucial in understanding protein-misfolding pathologies and in potential drug design aimed at the inhibition or reversal of protein aggregation. Using these technologies, researchers can monitor the aggregation process, visualize protein aggregates and analyze their properties. - Provides practical examples of nanoimaging research from leading molecular biology, cell biology, protein chemistry, biotechnology, genetics, and pharmaceutical labs - Includes over 200 color images to illustrate the power of various nanoimaging technologies - Focuses on nanoimaging techniques applied to protein misfolding and aggregation in molecular medicine
Conjugated Polyelectrolytes
Author: Bin Liu
Publisher: John Wiley & Sons
ISBN: 3527655727
Category : Technology & Engineering
Languages : en
Pages : 448
Book Description
This is the first monograph to specifically focus on fundamentals and applications of polyelectrolytes, a class of molecules that gained substantial interest due to their unique combination of properties. Combining both features of organic semiconductors and polyelectrolytes, they offer a broad field for fundamental research as well as applications to analytical chemistry, optical imaging, and opto-electronic devices. The initial chapters introduce readers to the synthesis, optical and electrical properties of various conjugated polyelectrolytes. This is followed by chapters on the applications of these materials in optical sensing and imaging with emphasis on biological systems, while the final section addresses the emerging applications of conjugated polyelectrolytes in optoelectronic devices, concluding with an in-depth discussion of structure-property relationship. The editors and contributors are all pioneers and experts in this expanding field. This monograph is not only for chemists, materials scientists, and physicists, but also a unique source of knowledge for readers with scientific background interested in polyelectrolytes.
Publisher: John Wiley & Sons
ISBN: 3527655727
Category : Technology & Engineering
Languages : en
Pages : 448
Book Description
This is the first monograph to specifically focus on fundamentals and applications of polyelectrolytes, a class of molecules that gained substantial interest due to their unique combination of properties. Combining both features of organic semiconductors and polyelectrolytes, they offer a broad field for fundamental research as well as applications to analytical chemistry, optical imaging, and opto-electronic devices. The initial chapters introduce readers to the synthesis, optical and electrical properties of various conjugated polyelectrolytes. This is followed by chapters on the applications of these materials in optical sensing and imaging with emphasis on biological systems, while the final section addresses the emerging applications of conjugated polyelectrolytes in optoelectronic devices, concluding with an in-depth discussion of structure-property relationship. The editors and contributors are all pioneers and experts in this expanding field. This monograph is not only for chemists, materials scientists, and physicists, but also a unique source of knowledge for readers with scientific background interested in polyelectrolytes.