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Author: Daniel Erik Otzen
Publisher: John Wiley & Sons
ISBN: 3527654208
Category : Science
Languages : en
Pages : 496
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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.
Author: Daniel Erik Otzen
Publisher: John Wiley & Sons
ISBN: 3527654208
Category : Science
Languages : en
Pages : 496
Get Book Here
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.
Author:
Publisher: Elsevier
ISBN: 0080468977
Category : Science
Languages : en
Pages : 412
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Book Description
The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a major new frontier in protein research. This new volume of Methods in Enzymology along with Part B (volume 412) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume (309) in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this important class of protein assemblies. Presents detailed protocols Includes troubleshooting tips Provides coverage on structural biology, computational methods, and biology
Author: Paul M. Gorman
Publisher:
ISBN: 9780494219225
Category :
Languages : en
Pages : 348
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Book Description
Alzheimer's Disease (AD) is a neuropathological disorder characterized by the progressive deposition of insoluble amyloid plaques and vascular deposits consisting primarily of 4.5 kDa amyloid beta peptides (Abeta). There is increasing evidence that the deposition of Abeta fibrils in the brain, an invariable feature of AD, and/or prefibrillar aggregates likely cause neurodegeneration in AD. While Abeta fibrils were a previous research focus, recent experiments implicate prefibrillar aggregates as the toxic species. The identification and characterization of prefibrillar aggregates is of great importance to understanding AD and the development of therapeutic strategies. Biophysical and spectroscopic techniques were used to examine the effects of electrostatic interactions on Abeta oligomerization. Experimental work demonstrated that, while salt bridges likely provide stability to preformed Abeta aggregates, these interactions are not essential for the early stages of aggregation. Abeta oligomerization is driven by the formation of pH-independent interactions and is impeded by electrostatic repulsion at pH values away from the isoelectric point. Diffuse plaques, containing only the 42-residue form of Abeta, are unstructured and non-toxic; they appear before toxic senile plaques containing both 40 and 42-residue forms. Through incubation, Abeta40 and Abeta42 were shown to co-incorporate into unstructured aggregates early during fibrillogenesis later leading to tightly packed aggregates with secondary structure. Previously, the stage at which the Abeta variants co-incorporated during the fibrillogenic process was unknown. After observing that the amyloid precursor protein transmembrane (APP-TM) domain contains two known dimerization motifs (GXXXG/A), oligomerization of the APP-TM domain was examined. A model system was developed to investigate the effects of familial AD mutations on the dimerization propensity of APP-TM domains. This work culminated in the first experimentally supported mechanism to explain how genetic mutations within the APP gene lead to the observed phenotype and predisposition to AD. Further experimentation led to the discovery of non-denaturing detergents that stabilize suspected on-pathway spherical Abeta aggregates. These detergent-stabilized Abeta oligomers share many of the structural features and biological activities of both membrane bound Abeta and spherical oligomers of Abeta formed in solution. Thus, these stabilizing detergents may prove useful in high-resolution structural analysis of spherical oligomers.
Author: Gregory R. Bock
Publisher: John Wiley & Sons
ISBN: 0470514930
Category : Medical
Languages : en
Pages : 266
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Book Description
Amyloid fibrils are associated with a range of pathological disorders including Alzheimer's Disease, Down's syndrome, diabetes, cardiomyopathies, and transmissible spongiform encephalopathies. This volume is a comprehensive account of recent developments in the understanding of the process of amyloid fibrils. Contains up-to-date data on all of the clinical problems which, despite their pathological significance, are still largely unsolved.
Author: Vladimir N Uversky
Publisher: Academic Press
ISBN: 0123978211
Category : Science
Languages : en
Pages : 556
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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
Author: Pier Luigi San Biagio
Publisher:
ISBN: 9788178953540
Category : Amyloidosis
Languages : en
Pages : 267
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Book Description
This book collects papers by biology, chemistry and physics researchers all actively working in the field of protein aggregation as related to amyloid diseases. Protein precipitates having a highly ordered, fibril-like structure accompany several fatal diseases, such as Alzheimer's, Parkinson's, Creutzfeldt-Jacob and Huntington diseases. Amyloid fibrils associated to different diseases share a common cross beta repeat structure, despite the lack of sequence homologies and structure similarities in the relative proteins. About 20 proteins are known to form amyloid fibrils under physiological conditions. In any of them a conformational change into an unfolding intermediate seems to be responsible for amyloid fibrils formation. A growing body of evidence indicates that in vitro any protein or polypeptide can assembly into fibrillar structures under mildly denaturing conditions, where metastable unfolding intermediates become stabilized. These findings have added further interest to the outstanding problem of protein folding/unfolding and aggregation, whose high interdisciplinary character touches upon biology, chemistry and physics. Indeed, only by joining different expertise we may hope to achieve a unifying view of protein aggregation mechanism in terms of a few general principles. A central issue in the problem of amyloid formation is the understanding of the thermodynamic transitions governing this type of self-organization process in which the symmetry of the interacting molecules should play a relevant role. The first paper of this volume by Manno deals with the modeling of amyloid formation in the frame of physics of colloidal coagulation, and highlights those theoretical aspects that can be investigated by experiments in vitro. The relevance of crowding and confinement, or a combination of them, on the aggregation of proteins in living system is discussed in the paper of Temussi, where results obtained from studies in vitro and in vivo are revised and compared. The paper by Higuchi et al. addresses the theme of disease transmission in living organisms. The authors present the case of systemic amyloidosis in mice showing that pre-formed amyloid fibrils injected in, or ingested by, mice susceptible to infection are capable to accelerate amyloid deposition. A new emerging hypothesis on the onset of amyloid diseases points out the role played by small oligomeric species representing early pre-fibrillar intermediates. Such small aggregates have been observed in the case of beta-peptide responsible for Alzheimer disease. The paper by Di Carlo et al. describes the toxic properties of beta-peptide aggregates with different size, and indicates the possible degeneration pathways leading to the disease. If pre-fibrillar small oligomers are amyloid intermediates, inhibiting their formation should be an important target for therapeutic strategies. The paper by Sgarbossa et al. illustrates the potential use of small polycyclic aromatic molecules that can act as fibrillogenesis inhibitors by imposing unfavorable conformational constraints to the aggregating molecules. The paper by Pastore discusses the aggregation properties of proteins having homo-polymeric stretches, whose tract length determines the onset of the pathologies. The most famous of them is the Huntington disease associated to expansion of polyglutamine repeat. Bisaglia et al. revised the case of alpha-synuclein involved in Parkinson disease. The paper describes the capacity of this protein of adopting different conformations as a response to the environments, with relation to its physiological function or possible pathological role. Finally, two papers concern the role of metal ions on protein aggregation. The paper by Morante gives a review of the possible harmful or useful effects of some metal ions on two pathological proteins, examined through the synergic use of computational and experimental techniques. The paper by Militello et al. describes metal effects on the conformational change and structural properties of aggregates of beta-lactoglobulin and bovine serum albumin, taken as convenient model systems for studying protein aggregation. We thank the contributing authors for having provide altogether a wide perspective, multi-faceted survey of the conceptual and experimental tools that can be applied for unraveling the mechanism of protein aggregation.
Author:
Publisher: Academic Press
ISBN: 0128122528
Category : Science
Languages : en
Pages : 322
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Book Description
Early Stage Protein Misfolding and Amyloid Aggregation, Volume 329, the latest in the International Review of Cell and Molecular Biology series presents comprehensive reviews and current advances in cell and molecular biology, including articles that address the structure and control of gene expression, nucleocytoplasmic interactions, control of cell development and differentiation, and cell transformation and growth. The series has a worldwide readership and maintains a high standard by publishing invited articles on important and timely topics as authored by prominent cell and molecular biologists. Provides comprehensive reviews and current advances Presents a wide range of perspectives on specific subjects Includes valuable reference material for advanced undergraduates, graduate students, and professional scientists
Author:
Publisher: Elsevier
ISBN: 0443293414
Category : Science
Languages : en
Pages : 530
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Book Description
The Hidden World of Protein Aggregation, Volume 206 provides a comprehensive exploration of protein aggregation, uncovering the factors behind the formation of amorphous aggregates and ordered structures called amyloid fibrils. It delves into the advantages and disadvantages of protein aggregates, addressing topics such as cytotoxicity and disorders linked to misfolding. Specific chapters in this release include Protein Aggregation: An Overview, Pathways of Amyloid Fibril Formation and Aggregation, Factors Influencing Amyloid Fibril Formation, Morphological Features and Types of Aggregated Structures, Each big journey starts with a first step: Importance of Oligomerization, Liquid-Liquid Phase Separation as Triggering Factor of Fibril Formation, and more. Additional sections cover Experimental Techniques for Detecting and Evaluating the Amyloid Fibrils, Prediction of Protein Aggregation, Amyloid Fibril Cytotoxicity and Associated Disorders, Inhibitors of Amyloid Fibril Formation, Therapeutic Approaches in Proteinopathies, Functional Amyloids, Biotechnological Applications of Amyloid Fibrils, and The Hidden World of Protein Aggregation. Provides an introduction to the folding of protein and associated conditions leading to aggregation and linked pathology Discusses structural biology and computational methodologies for analysis of protein (mis)folding and aggregation Describes functional amyloids and their biotechnological applications
Author: David Eliezer
Publisher: Humana
ISBN: 9781493929771
Category : Science
Languages : en
Pages : 0
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Book Description
This detailed volume focuses on methods for the characterization of aggregation processes that lead to the formation of amyloid fibrils and amyloid oligomers which feature in the etiology of a variety of human disorders collectively known as amyloidoses. The scope of the collection includes techniques for visualizing early steps on the amyloid formation pathway, methods for capturing and characterizing oligomeric, potentially toxic, intermediates, strategies for preparing and characterizing mature amyloid fibrils and approaches for understanding templating and transmission of amyloid aggregates. Written in the highly successful Methods in Molecular Biology series format, the chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Protein Amyloid Aggregation: Methods and Protocols serves as an ideal guide for biochemists and biophysicists with an interest in elucidating the mechanisms of protein amyloid formation, as well as chemists, pharmacologists and clinicians with an interest in leveraging an understanding of such mechanisms for the purpose of therapeutic development.
Author:
Publisher: Elsevier
ISBN: 0080496679
Category : Science
Languages : en
Pages : 861
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Book Description
This volume includes a core of methodologies to attack the unique experimental problems presented by protein misassembly. Emphasis is on human biology applications, the area in which there is the most interest, in which most of the work has already been done, and in which there is the best evidence for the structural sophisitication of the protein aggregates.The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.
