Download Full eBooks in PDF
Prpsc Prions State Of The Art Book in PDF, ePub and Kindle version is available to download in english. Read online anytime anywhere directly from your device. Click on the download button below to get a free pdf file of Prpsc Prions State Of The Art book. This book definitely worth reading, it is an incredibly well-written.
Author : Joaquín Castilla,Jesús R. Requena
Publisher : MDPI
Page : 211 pages
File Size : 55,7 Mb
Release : 2018-11-07
Category : Electronic books
ISBN : 9783038973089
This book is a printed edition of the Special Issue "PrPSc prions: state of the art" that was published in Pathogens
Author : Jesús Requena,Joaquín Castilla
Publisher : Unknown
Page : 128 pages
File Size : 49,9 Mb
Release : 2018
Category : Electronic
ISBN : 3038973092
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of fatal and transmissible neurodegenerative disorders characterized by long incubation periods, misfolded prion protein (PrP) deposition, and usually spongiform vacuolation. These devastating diseases affect many mammals, with the best known examples being Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), or Kuru in humans; and scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle, and chronic wasting disease (CWD) in cervids. Despite major achievements in research of TSEs, there are still many unresolved key issues that hamper the development of effective therapies. However, the last decade has been particularly prolific in advances in the prion field. Among others, prion propagation in vitro has been achieved, leading to new diagnostic methods; the basic architecture of infectious prions has been deciphered; new prion disease types have been described in humans and other animals; and prion disorders have emerged in places that had not previously reported the disorders, as is the case for CWD in Europe.This Special Issue will focus on the state of the art of our knowledge of PrPSc: on what we know about its structure and propagation, the basis of strains and transmission barriers, the mechanisms of PrPSc toxicity, the possible function of PrPSc's properly folded precursor, PrPC and its evolutionary history, and recent technical breakthroughs in diagnostics and therapy development among other key aspects of PrPSc prion biology.
Author : Jorg Tatzelt
Publisher : Unknown
Page : 80 pages
File Size : 46,8 Mb
Release : 2010
Category : Prions
ISBN : 0954333527
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.
Author : Uday Kishore,Nicole M. Thielens,Christine Gaboriaud
Publisher : Frontiers Media SA
Page : 102 pages
File Size : 47,7 Mb
Release : 2016-11-22
Category : Electronic book
ISBN : 9782889450589
C1q is the target recognition protein of the classical complement pathway and a major connecting link between innate and acquired immunity. As a charge pattern recognition molecule of innate immunity, C1q can engage a broad range of ligands derived from self, non-self and altered self via its heterotrimeric globular (gC1q) domain and thus trigger the classical complement pathway. The trimeric gC1q signature domain has been identified in a variety of non-complement proteins that can be grouped together as a C1q family. C1q circulates in serum as part of the C1 complex, in association with a catalytic tetrameric assembly of two homologous yet distinct serine proteases, C1r and C1s. Binding of C1q to appropriate targets leads to sequential activation of C1r and C1s, the latter being able to cleave complement components C4 and C2 thereby triggering the complement cascade. Activation of the classical pathway plays an important role in innate immune protection against pathogens and damaged elements from self. However, its involvement has been shown in various pathologies including ischemia-reperfusion injury and hereditary angioedema. Unexpected roles for the classical pathway have also been discovered recently, linked to both physiological and pathological aspects of development, including brain and cancer cells. These new perspectives should arouse renewed interest in a search for specific inhibitors of the classical pathway. In addition, C1q has recently been shown to have a number of functions that are independent of the activation of the classical pathway. This research topic is aimed at providing a state-of-the-art overview of the classical pathway, including, but not restricted to emerging functions of C1q and of the C1 complex, as well as pathological consequences of C1 activation or of the presence of anti-C1q autoantibodies . Contributions are included in the areas such as structural basis of C1q ligand recognition, C1q family proteins, inhibitors of the classical pathway identified in pathogens and improved derived inhibitors, structural determinants of the substrate specificities of C1r and C1s, elucidation of the architecture of C1, structural and functional homology of C1 with the initiating complexes of the lectin complement pathway, and novel involvement of C1q in processes such as ageing, cancer, synaptic pruning, and pregnancy.
Author : Harry F. Baker
Publisher : Springer Science & Business Media
Page : 292 pages
File Size : 46,8 Mb
Release : 2008-02-02
Category : Medical
ISBN : 9781592591343
Internationally recognized investigators review the latest developments in, and novel approaches to, understanding the prion protein and prion diseases at the molecular level. Utilizing a variety of cutting-edge techniques, these distinguished scientists seek to define the normal function of a prion protein, to detect and measure the early immune response to prion disease, and to discover possible therapeutic targets. They also use transgenic mice and new electrophysiological investigations to elucidate the pathogenetic mechanisms involved in prion diseases. State-of-the-art and richly insightful, Molecular Pathology of the Prions captures for basic and clinical neuropathologists the latest developments and approaches to understanding the pathogenesis of prion diseases, and by analogy suggests possible research techniques for the more common proteinopthies, such as Alzheimer's and Parkinson's diseases.
Author : Harry F. Baker,Rosalind M. Ridley
Publisher : Humana
Page : 319 pages
File Size : 54,6 Mb
Release : 2013-08-11
Category : Science
ISBN : 1489940405
Harry Baker and Rosalind Ridley have done an admirable job in assem bling this collection of articles that describe the methodology frequently used to study a group of CNS illnesses often referred to as the "prion diseases." Research on prions and the disorders that they cause has progressed relatively rapidly over the last decade since the discovery of the prion protein (PrP) that allowed the application of modem molecular biological and genetic tools. The power of these techniques is awesome and their use in deciphering the once mysterious prion diseases has brought a wealth of new information. Although prions are unprecedented pathogens, appearing to consist only of PrPSc molecules, the diseases that they cause are no less remarkable. The prion diseases in animals include scrapie of sheep and goats as well as "mad cow" disease or bovine spongiform encephalopathy (BSE). In the United King dom, the epidemic of BSE has heightened public awareness of this previously obscure group of diseases such that any work in the field is likely to stir up interest in the media and become a subject of public debate. It has been diffi cult for British investigators to work on prion diseases without being involved in these controversies. As such, several chapters have been included that deal with political and social issues surrounding prion diseases. The human prion diseases present an equally fascinating saga in which these CNS degenerations present as genetic, sporadic, and infectious illnesses.
Author : Claudio Soto
Publisher : CRC Press
Page : 184 pages
File Size : 43,8 Mb
Release : 2005-12-20
Category : Medical
ISBN : 9781420040128
Prion-related diseases, known as transmissible spongiform encephalopathies (TSEs), are infectious, fatal neurodegenerative disorders for which there is no cure, treatment, nor even a means for early diagnosis. The horrific advent of Mad Cow Disease -- transmitted to humans through eating meat from steers sickened by bovine spongiform encephalopathy
Author : David R. Brown
Publisher : Springer Science & Business Media
Page : 478 pages
File Size : 43,7 Mb
Release : 2005-07-26
Category : Medical
ISBN : 9780387239231
This is the first and only book on the subject of prions to cover the cause of cell death in the disease. It covers the full range of competing theories on the subject, from broad description and basic points up to the final details of the basic science.
Author : T. Hugh Pennington
Publisher : OUP Oxford
Page : 250 pages
File Size : 48,7 Mb
Release : 2003-09-18
Category : History
ISBN : 0191588776
The 'food scare' concept took on new meaning in 1996, which opened with variant CJD emerging as the human form of BSE, and closed with Britain's worst E.coli O157 outbreak in central Scotland. As people died, so did trust in government and science. This book tells the story of these events, what led up to them, and what has happened since. It breaks new ground by dissecting these tragedies alongside catastrophes like Aberfan, Piper Alpha, Chernobyl, and the worst ever railway accidents in Ireland and Britain (Armagh and Quintinshill), as well as classical outbreaks of botulism, typhoid, E.coli O157 and Salmonella food poisoning. Britain's ability to win Nobel prizes marches with a propensity to have disasters. The book explains why, demonstrating failures in policy making, failures in the application of science, and failing inspectorates. A unique feature of this book is its breadth since it covers history, politics and law as well as science. It also makes some fascinating connections, like those between 1930's nuclear physics, E.coli, and molecular biology, and the links between manslaughter in 19th century mental hospitals, syphilis, the Nobel Prize, and the prospects for successfully treating variant CJD. Royal murderers, vaccine research in Auschwitz and Buchenwald, and the race to develop the atom bomb appear as well. For the general reader its non-technical but authoritative account of the science behind these tragedies, its critical appraisal of how the government responded to them, its coverage of public inquiries and its analysis of risk will be informative and stimulating. Scientists will find its approach to the prion theory and the origins of BSE challenging and controversial. Policy makers will find not only diagnoses of what went wrong in the past, but remedies ror the future.
Author : Tetsuyuki Kitamoto
Publisher : Springer Science & Business Media
Page : 262 pages
File Size : 40,6 Mb
Release : 2006-06-09
Category : Medical
ISBN : 9784431294023
Prion diseases recently have attracted interest not only scientifically but also socially because of the bovine spongiform encephalopathy (BSE) epidemic and the outbreak of variant Creutzfeldt-Jakob disease (vCJD) in the United Kingdom. In 2004, the International Symposium of Prion Diseases for Food and Drug Safety was held October 31–November 2 in Sendai, Japan, where, 20 years earlier, arguments were first heard on whether the etiologic agent of transmissible spongiform encephalopathy was prions or scrapie-associated fibrils. This volume is a collection of current work on prion research that was presented at the 2004 symposium. Topics included range from basic research to clinical aspects of prion diseases, making the book a valuable resource for researchers and clinicians, and encouraging further developments by the next generation of researchers.
Author : Joseph Bertolini,Neil Goss,John Curling
Publisher : John Wiley & Sons
Page : 518 pages
File Size : 45,5 Mb
Release : 2012-12-06
Category : Medical
ISBN : 9781118356791
Sets forth the state of the science and technology in plasma protein production With contributions from an international team of eighty leading experts and pioneers in the field, Production of Plasma Proteins for Therapeutic Use presents a comprehensive overview of the current state of knowledge about the function, use, and production of blood plasma proteins. In addition to details of the operational requirements for the production of plasma derivatives, the book describes the biology, development, research, manufacture, and clinical indications of essentially all plasma proteins with established clinical use or therapeutic potential. Production of Plasma Proteins for Therapeutic Use covers the key aspects of the plasma fractionation industry in five sections: Section 1: Introduction to Plasma Fractionation initially describes the history of transfusion and then covers the emergence of plasma collection and fractionation from its earliest days to the present time, with the commercial and not-for-profit sectors developing into a multi-billion dollar industry. Section 2: Plasma Proteins for Therapeutic Use contains 24 chapters dedicated to specific plasma proteins, including coagulation factors, albumin, immunoglobulin, and a comprehensive range of other plasma-derived proteins with therapeutic indications. Each chapter discusses the physiology, biochemistry, mechanism of action, and manufacture of each plasma protein including viral safety issues and clinical uses. Section 3: Pathogen Safety of Plasma Products examines issues and procedures for enhancing viral safety and reducing the risk of transmissible spongiform encephalopathy transmission. Section 4: The Pharmaceutical Environment Applied to Plasma Fractionation details the requirements and activities associated with plasma collection, quality assurance, compliance with regulatory requirements, provision of medical affairs support, and the manufacture of plasma products. Section 5: The Market for Plasma Products and the Economics of Fractionation reviews the commercial environment and economics of the plasma fractionation industry including future trends, highlighting regions such as Asia, which have the potential to exert a major influence on the plasma fractionation industry in the twenty-first century.
Author : Anonim
Publisher : Unknown
Page : 564 pages
File Size : 50,9 Mb
Release : 2000
Category : Chemistry, Technical
ISBN : UCSD:31822022781314
Author : Fidel Toldrá,Leo M. L. Nollet
Publisher : Springer Science & Business Media
Page : 589 pages
File Size : 44,7 Mb
Release : 2012-12-16
Category : Technology & Engineering
ISBN : 9781461456261
Food proteomics is one of the most dynamic and fast-developing areas in food science. The goal of this book is to be a reference guide on the principles and the current and future potential applications of proteomics in food science and technology. More specifically, the book will discuss recent developments and the expected trends of the near future in food proteomics. The book will be divided into two parts. The first part (7 chapters) will focus on the basic principles for proteomics, e.g., sample preparation, such as extraction and separation techniques, analytical instrumentation currently in use, and available databases for peptide and protein identification. The second part of the book (26 chapters) will focus on applications in foods. It will deal with quality issues related to post-mortem processes in animal foods and quality traits for all foods in general, as well as the identification of bioactive peptides and proteins, which are very important from the nutritional point of view. Furthermore, consumers are now extremely susceptible to food safety issues, and proteomics can provide reassurance with different safety aspects, such as food authenticity, detection of animal species in the food, and identification of food allergens. All of these issues will be covered in this book. It is also worth noting that both editors are internationally recognized experts in the field of food science, and both have edited numerous food science books and handbooks.
Author : J. Robin Harris
Publisher : Springer Science & Business Media
Page : 654 pages
File Size : 49,5 Mb
Release : 2012-12-09
Category : Medical
ISBN : 9789400754164
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.
Author : Mathias Jucker,Yves Christen
Publisher : Springer Science & Business Media
Page : 156 pages
File Size : 55,9 Mb
Release : 2013-03-27
Category : Medical
ISBN : 9783642354915
The misfolding and aggregation of specific proteins is an early and obligatory event in many of the age-related neurodegenerative diseases of humans. The initial cause of this pathogenic cascade and the means whereby disease spreads through the nervous system, remain uncertain. A recent surge of research, first instigated by pathologic similarities between prion disease and Alzheimer’s disease, increasingly implicates the conversion of disease-specific proteins into an aggregate-prone b-sheet-rich state as the prime mover of the neurodegenerative process. This prion-like corruptive protein templating or seeding now characterizes such clinically and etiologically diverse neurological disorders as Alzheimer ́s disease, Parkinson’s disease, Huntington’s disease, amyotrophic lateral sclerosis, and frontotemporal lobar degeneration. Understanding the misfolding, aggregation, trafficking and pathogenicity of the affected proteins could therefore reveal universal pathomechanistic principles for some of the most devastating and intractable human brain disorders. It is time to accept that the prion concept is no longer confined to prionoses but is a promising concept for the understanding and treatment of a remarkable variety of diseases that afflict primarily our aging society.