Download or read book Amyloid Prions and Other Protein Aggregates written by and published by Elsevier. This book was released on 1999-09-22 with total page 861 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book Amyloid Prions and Other Protein Aggregates Part C written by and published by Elsevier. This book was released on 2006-10-06 with total page 412 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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
Download or read book Amyloid Prions and Other Protein Aggregates written by and published by Academic Press. This book was released on 1999-09-28 with total page 820 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book Amyloid Prions and Other Protein Aggregates Part C written by and published by . This book was released on 2006 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Amyloid Prions and Other Protein Aggregates Part B written by Indu Kheterpal and published by . This book was released on 2006 with total page 403 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Fibrous Proteins Amyloids Prions and Beta Proteins written by John M. Squire and published by Elsevier. This book was released on 2006-12-12 with total page 329 pages. Available in PDF, EPUB and Kindle. Book excerpt: Amyloids, Prions and Beta Proteins is the last volume of the three-part thematic series on Fibrous Proteins in the Advances in Protein Chemistry serial. Fibrous proteins act as molecular scaffolds in cells providing the supporting structures of our skeletons, bones, tendons, cartilage, and skin. They define the mechanical properties of our internal hollow organs such as the intestines, heart, and blood vessels. This volume covers such topics as Beta-Structures in Fibrous Proteins; B-Silks: Enhancing and Controlling Aggregation; Beta-Rolls, Beta-Helices and Other Beta-Solenoid Proteins; Natural Triple B-Stranded Fibrous Folds; Structure, Function and Amyloidogenesis of Fungal Prions: Filament Polymorphism and Prion Variants; X-Ray Fiber and powder Diffraction of PRP Prion Peptides; From the Polymorphism of Amyloid Fibrils to Their Assembly Mechanism and Cytotoxicity; Structural Models of Amyloid-like Fibrils.
Download or read book Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease written by J. Robin Harris and published by Springer Science & Business Media. This book was released on 2012-12-09 with total page 654 pages. Available in PDF, EPUB and Kindle. Book excerpt: This volume of the Subcellular Biochemistry series is the result of the long-standing research interest of the editor in the molecular mechanism underlying Alzheimer’s disease and other amyloid diseases, indicated also by the earlier book in the series (Volume 38), devoted to Alzheimer’s disease. The broad coverage within the present amyloidogenesis book represents an attempt to collate current knowledge relating to the proteins and peptides involved in most of the known amyloid diseases, together with some amyloid/fibril-forming proteins and peptides that are not involved in diseases. Thus, the range of topics included is comprehensive and furthermore it was thought appropriate to include both basic science and clinical presentation of the subjects under discussion.
Download or read book Early Stage Protein Misfolding and Amyloid Aggregation written by and published by Academic Press. This book was released on 2017-02-01 with total page 320 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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
Download or read book Molecular Chaperones in Health and Disease written by Matthias Gaestel and published by Springer Science & Business Media. This book was released on 2005-09-27 with total page 464 pages. Available in PDF, EPUB and Kindle. Book excerpt: Molecular chaperones are involved in a wide variety of essential cellular processes in living cells. A subset of molecular chaperones have been initially described as heat shock proteins protecting cells from stress damage by keeping cellular proteins in a folding competent state and preventing them from irreversible aggregation. Later it became obvious that molecular chaperones are also expressed constitutively in the cell and are involved in complex processes such as protein synthesis, intracellular protein transport, post-translational modification and secretion of proteins as well as receptor signalling. Hence, it is not surprising that molecular chaperones are implicated in the pathogenesis of many relevant diseases and could be regarded as potential pharmacological targets. Starting with the analysis of the mode of action of chaperones at the molecular, cellular and organismic level, this book will then describe specific aspects where modulation of chaperone action could be of pharmacological and therapeutic interest.
Download or read book The Hidden World of Protein Aggregation written by and published by Elsevier. This book was released on 2024-05-30 with total page 530 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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
Download or read book Amyloid Fibrils and Prefibrillar Aggregates written by Daniel Erik Otzen and published by John Wiley & Sons. This book was released on 2013-06-04 with total page 496 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book Biophysics And Biochemistry Of Protein Aggregation Experimental And Theoretical Studies On Folding Misfolding And Self assembly Of Amyloidogenic Peptides written by Yuan Jian-min and published by World Scientific. This book was released on 2017-06-02 with total page 328 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book reviews current research on the important processes involved in neurodegenerative diseases (e.g. Alzheimer's disease) and the peptides and proteins involved in the amyloidogenic processes. It covers the design and developments of anti-amyloid inhibitors, and gives readers a fundamental understanding of the underlying oligomerization and aggregation processes of these diseases from both computational and experimental points of view.
Download or read book Protein Misfolding Aggregation and Conformational Diseases written by Vladimir N. Uversky and published by Springer Science & Business Media. This book was released on 2007-11-24 with total page 450 pages. Available in PDF, EPUB and Kindle. Book excerpt: Research indicates that most neurodegenerative diseases, systemic amyloidoses and many others, arise from the misfolding and aggregation of an underlying protein. This is the first book to discuss significant achievements in protein structure-function relationships in biochemistry, molecular biology and molecular medicine. The authors summarize recent progress in the understanding of the relationships between protein misfolding, aggregation and development of protein deposition disorders.
Download or read book The Prion Protein written by Jorg Tatzelt and published by . This book was released on 2010 with total page 80 pages. Available in PDF, EPUB and Kindle. Book excerpt: A conformational transition of the cellular prion protein (PrPC) into an aberrantly folded isoform designated scrapie prion protein (PrPSc) is the hallmark of a variety of neurodegenerative disorders collectively called prion diseases. They include Creutzfeldt-Jakob disease and Gerstmann-Stäussler-Scheinker syndrome in humans, scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle and chronic wasting disease (CWD) in free-ranging deer. In contrast to the deadly properties of misfolded PrP, PrPC seems to possess a neuroprotective activity. More-over, animal models indicated that the stress-protective activity of PrPC and the neurotoxic effects of PrPSc are somehow interconnected. In this timely book, leading scientists in the field have come together to highlight the apparently incongruous activities of different PrP conformers. The articles outline current research on celluar pathways implicated in the formation and signaling of neurotoxic and physiological PrP isoforms and delineate future research direction. Topics covered include the physiologcial activity of PrPC and its possible role as a neurotrophic factor, the finding that aberrant PrP conformers can cause neurodegeneration in the absence of infectious prion propagation, the requirement of the GPI anchor of PrPC for the neurotoxic effects of scrapie prions, the pathways implicated in the formation and neurotoxic properties of cytosolically localized PrP, the impact of metal ions on the processing of PrP, and the role of autophagy in the propagation and clearance of PrPSc. The book is fully illustrated and chapters include comprehensive reference sections. Essential reading for scientists involved in prion research.
Download or read book Protein Misfolding Aggregation and Conformational Diseases written by Vladimir N. Uversky and published by Springer Science & Business Media. This book was released on 2007-05-26 with total page 538 pages. Available in PDF, EPUB and Kindle. Book excerpt: The second volume continues to fill the gap in protein review and protocol literature. It does this while summarizing recent achievements in the understanding of the relationships between protein misfoldings, aggregation, and development of protein deposition disorders. The focus of Part B is the molecular basis of differential disorders.
Download or read book Polymorphic protein aggregation in tauopathies written by Alexander Sandberg and published by Linköping University Electronic Press. This book was released on 2019-11-08 with total page 51 pages. Available in PDF, EPUB and Kindle. Book excerpt: Alzheimer’s disease(s) comprises one of the most common and costly neurodegenerative diseases. With a larger population and an increasing life expectancy, amyloid diseases (with age as one of the most prominent risk factors) will generate an even larger burden on healthcare. We know that protein misfolding is involved in the disease process but lack a complete understanding of the mechanism behind these diseases, both the sporadic and hereditary variants. It is not always known whether it is a gain-of-toxic function or loss?of?function that causes the neurodegeneration. To determine the correct diagnosis is a major challenge. If diagnosed, only a few amyloid diseases can be treated today. Amyloids are highly ordered filamentous protein aggregates with a ??sheet structure. From identical or similar amino acid sequences, a large variety of structures can be formed by different secondary and tertiary structures and by different packing of the individual filaments. This is known as fibril polymorphism. This work focuses on characterization on two proteins involved in Alzheimer’s disease and other neurodegenerative diseases, namely Amyloid?? (A?) and microtubule associated protein tau (tau). In order to investigate the properties of these proteins in vitro it is important to have protocols for production of recombinant protein that enables characterization of these aggregation prone proteins. We present protocols for recombinant expression, purification and non?denaturing fibrillation assays used in our lab to produce and analyze A?, tau and the prion protein. Development of new ligands for characterization of fibrils is an important way of investigating different fibrillary structures and characterizing and distinguishing between the different polymorphs of aggregates. We showed that the central benzene ring of the amyloid ligand X?34 can be exchanged for other heterocyclic motifs and still retain targeting of the “Congo red” binding site. The compounds do not compete with the Pittsburgh compound B (PiB) binding site on recombinant A? fibrils. We also characterized tau fibrils formed from seeding with tau aggregates from patients diagnosed with different neurodegenerative tauopathies. We use aggregation kinetics to test the seeding activity on two different sequence isoforms of tau, 0N3R and 0N4R. Fibrillation kinetics, an array of recently developed ligands (including the X?34 analogs) and electron microscopy were used to characterize different polymorphs of the tau aggregates formed by seeded templating from patient derived seeds. Our data showed that brains contain seeds with different morphologies even with in patients diagnosed with the same disease. Investigations of the rare tau mutant G273R found in a patient with a presumed tauopathy also highlights the problem with proper diagnostics. Our results reveal that in vitro this mutation change the binding properties of 0N4R tau to the cytoskeletal proteins microtubule and F?actin. Furthermore, we could show that when seeded, the fibril formation seeding activity followed a sequence similarity dependent manner. In fibrils formed during heparin-induced aggregation we can be distinguished between wild type and mutant tau as they form fibrils with different thickness. Our in vitro biophysical data support that the G237R mutant is causing a 4R tauopathy. The work in this thesis increase our knowledge in the field of tau aggregation and tau fibril polymorphism. En av de vanligaste och mest kostsamma sjukdomarna är den nervdödande Alzheimers sjukdom. Med en större population och ökad förväntad livslängd kommer amyloida sjukdomar, som har ålder som den viktigaste riskfaktorn, att generera en ökad börda för sjukvården. Vi saknar en fullständig förståelse för mekanismerna bakom dessa sjukdomar både för de sporadiska och ärftliga varianterna. Man vet att felveckade proteiner är inblandade i dessa sjukdomar. Det är inte alltid känt hur den felveckade formen av ett protein alstrar en toxisk funktion eller om det är en förlust av dennas funktion som orsakar nervdöden. Att kunna fastställa en korrekt diagnos är en stor utmaning för forskarvärlden idag. Även när en korrekt diagnos kan ställas är det endast ett fåtal amyloida sjukdomar som kan behandlas idag. Amyloider är mycket välordnade filamentösa proteinaggregat med ?-flakstruktur. Från identiska eller liknande aminosyrasekvenser kan ett stort antal strukturer bildas med olika sekundär- och tertiär struktur och olika packning av individuella filament. Vi kallar detta för strukturell polymorfism. Det här arbetet fokuserar på karakterisering av två proteiner involverade i Alzheimers sjukdom och andra neurodegenerativa sjukdomar nämligen Amyloid ? (A?) och mikrotubuli associerade protein tau (tau). För att kunna undersöka egenskaperna hos dessa proteiner är det viktigt att ha protokoll för produktion av rekombinant protein för att kunna karakterisera dessa aggregeringsbenägna proteiner. Vi utvecklade protokoll för rekombinant utryck, rening och icke-denaturerande fibrilleringsanalyser som används i vårt labb för att producera och analysera A?, tau och prionproteinet. Utveckling av nya ligander för karakterisering av fibriller är en viktig väg för att undersöka olika fibrillstrukturer och för karakterisering och för att kunna särskilja mellan olika polymorfer av aggregat. I det här arbetet visas att den centrala bensenringen hos amyloidliganden X-34 kan bytas ut mot andra heterocykliska motiv och fortfarande behålla sin specificitet mot ”Congo röd” bindnings-sätet utan att konkurrera med Pittsburgh compound B (PiB) bindnings-säte på rekombinanta A? fibriller. Vi karaktäriserade också tau fibriller bildade via ympning, så kallad seeding, med tau aggregat isolerade från patienter diagnosticerade med olika nervdödande taupatier. Vi använder aggregerings kinetik för att testa seedningsförmåga på två olika sekvens isoformer av tau. Nyligen utvecklade ligander (inkluderat X-34 analoger) och elektronmikroskopi användes för att karakterisera de olika polymorferna av tau aggregaten. Våra data påvisar att olika patienter bär på olika seeds, det vill säga olika polymorpher. Även mellan patienter med samma diagnos finns skillnader. Undersökningar av den ovanliga tau mutationen G273R understryker också problemet med fastställandet av korrekt diagnos. Våra resultat från provrörsexperiment avslöjar att den här mutationen ändrar bindningsegenskaperna av 0N4R tau till cytoskelettproteinerna mikrotubulin och F-aktin. Vi kunde ytterligare visa att när fibrilleringsreaktionen seedades så följde det en sekvenslikhetsberoende mekanism. Fibrerna som bildas under heparininducering kan skiljas åt mellan normalt och muterat tau genom att de har olika tjocklek. Våra biofysikaliska data stödjer att G273R tau mutationen kan orsaka en 4R tauopati. Arbetet i denna avhandling ökar vår kunskap inom området tau-aggregering och tau fibrilpolymorfism.
Download or read book Bio nanoimaging written by Vladimir N Uversky and published by Academic Press. This book was released on 2013-11-05 with total page 556 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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
