Download Free Protein Deimination In Human Health And Disease Book in PDF and EPUB Free Download. You can read online Protein Deimination In Human Health And Disease and write the review.

Published in 2014, Protein Deimination in Human Health and Disease was the first book on this novel post-translational modification, in which selected positively-charged arginine amino acids are converted to neutral citrulline amino acids by the peptidyl-arginine deiminase (PAD) family of enzymes. This area of research continues to expand rapidly, necessitating the need for this second edition. Chronicling the latest inflammatory, epigenetic, neurodegenerative, and carcinogenic processes, Protein Deimination in Human Health and Disease, Second Edition, updates the latest advances in deimination research, including new information on PAD enzyme structure and activity, and how PAD knock-out animals are being used to study known and newly-discovered links to various human diseases. The first edition outlined what was known about citrullinated proteins in normal tissues such as skin and hair, as well as in maladies such as rheumatoid arthritis (RA), multiple sclerosis (MS), Alzheimer’s disease (AD), glaucoma, peripheral nerve injury, neonatal hypoxic brain damage, and breast cancer. This second edition addresses numerous additional disorders such as diabetes, asthma, traumatic brain injury, inflammatory bowel disease, lupus, bone disease, heart failure, fronto-temporal dementia, and prostate and colon cancer. It also provides updates on the deimination research covering the three seminal diseases first linked to this process (RA, MS and AD), and details how auto-antibodies against citrullinated proteins contribute to disease. In addition, new hypotheses on the possible pathologic mechanisms of citrullinated myelin basic protein and glial fibrillary acidic protein are also proposed. This second edition also outlines the latest developments in therapeutic strategies, including the use of new PAD antagonists and innovative techniques such as micro-vescicles and stem cells as possible mechanisms to treat these conditions.
The Mosaic of Autoimmunity: The Novel Factors of Autoimmune Diseases describes the multifactorial origin and diversity of expression of autoimmune diseases in humans. The term implies that different combinations of factors in autoimmunity produce varying and unique clinical pictures in a wide spectrum of autoimmune diseases. Most of the factors involved in autoimmunity can be categorized into four groups: genetic, immune defects, hormonal and environmental factors. In this book, the environmental factors are reviewed, including infectious agents, vaccines as triggers of autoimmunity, smoking and its relationship with rheumatoid arthritis, systemic lupus erythematosus, thyroid disease, multiple sclerosis and inflammatory bowel diseases. An entirely new syndrome, the autoimmune/inflammatory syndrome induced by adjuvants (ASIA), is also included, along with other diseases that are now recognized as having an autoimmune etiopathogenesis.
This volume provides a collection of contemporary perspectives on using activity-based protein profiling (ABPP) for biological discoveries in protein science, microbiology, and immunology. A common theme throughout is the special utility of ABPP to interrogate protein function and small-molecule interactions on a global scale in native biological systems. Each chapter showcases distinct advantages of ABPP applied to diverse protein classes and biological systems. As such, the book offers readers valuable insights into the basic principles of ABPP technology and how to apply this approach to biological questions ranging from the study of post-translational modifications to targeting bacterial effectors in host-pathogen interactions.
Lasso peptides form a growing family of fascinating ribosomally-synthesized and post-translationally modified peptides produced by bacteria. They contain 15 to 24 residues and share a unique interlocked topology that involves an N-terminal 7 to 9-residue macrolactam ring where the C-terminal tail is threaded and irreversibly trapped. The ring results from the condensation of the N-terminal amino group with a side-chain carboxylate of a glutamate at position 8 or 9, or an aspartate at position 7, 8 or 9. The trapping of the tail involves bulky amino acids located in the tail below and above the ring and/or disulfide bridges connecting the ring and the tail. Lasso peptides are subdivided into three subtypes depending on the absence (class II) or presence of one (class III) or two (class I) disulfide bridges. The lasso topology results in highly compact structures that give to lasso peptides an extraordinary stability towards both protease degradation and denaturing conditions. Lasso peptides are generally receptor antagonists, enzyme inhibitors and/or antibacterial or antiviral (anti-HIV) agents. The lasso scaffold and the associated biological activities shown by lasso peptides on different key targets make them promising molecules with high therapeutic potential. Their application in drug design has been exemplified by the development of an integrin antagonist based on a lasso peptide scaffold. The biosynthesis machinery of lasso peptides is therefore of high biotechnological interest, especially since such highly compact and stable structures have to date revealed inaccessible by peptide synthesis. Lasso peptides are produced from a linear precursor LasA, which undergoes a maturation process involving several steps, in particular cleavage of the leader peptide and cyclization. The post-translational modifications are ensured by a dedicated enzymatic machinery, which is composed of an ATP-dependent cysteine protease (LasB) and a lactam synthetase (LasC) that form an enzymatic complex called lasso synthetase. Microcin J25, produced by Escherichia coli AY25, is the archetype of lasso peptides and the most extensively studied. To date only around forty lasso peptides have been isolated, but genome mining approaches have revealed that they are widely distributed among Proteobacteria and Actinobacteria, particularly in Streptomyces, making available a rich resource of novel lasso peptides and enzyme machineries towards lasso topologies.
The compact myelin sheath formed around nerve axons speeds up nerve conduction and also nurtures the axon. Destruction of this sheath in demyelinating diseases such as multiple sclerosis (MS) results in nerve conduction failure and neurodegeneration. Myelin basic protein (MBP) is the second most abundant protein of central nervous system (CNS) myelin (after the proteolipid protein), representing about 30 % of the total myelin protein and about 10 % of myelin by weight. It is also present in peripheral nervous system (PNS) myelin but as a lower percentage of the total protein. This book addresses the issue of Myelin and the way it binds to negatively-charged lipids on the cytosolic surfaces of the processes and is responsible for adhesion of these surfaces of myelin in the CNS, thus forming the major dense line observed by electron microscopy.
This Edited Volume Periodontology - Fundamentals and Clinical Features is a collection of reviewed and relevant research chapters, offering a comprehensive overview of recent developments in the field. The book comprises single chapters authored by various researchers and edited by an expert active in the dental medicine research area. All chapters are complete in themselves but united under a common research study topic. This publication aims at providing a thorough overview of the latest research efforts by international authors in periodontology, and opening new possible research paths for further novel developments.
With the most comprehensive and up-to-date overview of structure-based drug discovery covering both experimental and computational approaches, Structural Biology in Drug Discovery: Methods, Techniques, and Practices describes principles, methods, applications, and emerging paradigms of structural biology as a tool for more efficient drug development. Coverage includes successful examples, academic and industry insights, novel concepts, and advances in a rapidly evolving field. The combined chapters, by authors writing from the frontlines of structural biology and drug discovery, give readers a valuable reference and resource that: Presents the benefits, limitations, and potentiality of major techniques in the field such as X-ray crystallography, NMR, neutron crystallography, cryo-EM, mass spectrometry and other biophysical techniques, and computational structural biology Includes detailed chapters on druggability, allostery, complementary use of thermodynamic and kinetic information, and powerful approaches such as structural chemogenomics and fragment-based drug design Emphasizes the need for the in-depth biophysical characterization of protein targets as well as of therapeutic proteins, and for a thorough quality assessment of experimental structures Illustrates advances in the field of established therapeutic targets like kinases, serine proteinases, GPCRs, and epigenetic proteins, and of more challenging ones like protein-protein interactions and intrinsically disordered proteins
In this brief, Vladimir Uversky discusses the paradigm-shifting phenomenon of intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered domains and functional IDP regions (IDPRs). Beginning with an introduction to the concept of protein intrinsic disorder, Uversky then goes on to describe the peculiar amino acid sequences of IDPs, their structural heterogeneity, typical functions and disorder-based binding modes. In the final sections, Uversky discusses IDPs in human diseases and as potential drug targets. This volume provides a snapshot to researchers entering the field as well as providing a current overview for more experienced scientists in related areas.
Most textbooks on neurodegenerative disorders have used a classification scheme based upon either clinical syndromes or anatomical distribution of the pathology. In contrast, this book looks to the future and uses a classification based upon molecular mechanisms, rather than clinical or anatomical boundaries. Major advances in molecular genetics and the application of biochemical and immunocytochemical techniques to neurodegenerative disorders have generated this new approach. Throughout most of the current volume, diseases are clustered according to the proteins that accumulate within cells (e.g. tau, α-synuclein and TDP-43) and in the extracellular compartments (e.g. β-amyloid and prion proteins) or according to a shared pathogenetic mechanism, such as trinucleotide repeats, that are a feature of specific genetic disorders. Chapters throughout the book conform to a standard lay-out for ease of access by the reader and are written by a panel of International Experts Since the first edition of this book, major advances have been made in the discovery of common molecular mechanisms between many neurodegenerative diseases most notably in the frontotemporal lobar degenerations (FTLD) and motor neuron disease or amyotrophic lateral sclerosis. This book will be essential reading for clinicians, neuropathologists and basic neuroscientists who require the firm up-to-date knowledge of mechanisms, diagnostic pathology and genetics of Neurodegenerative diseases that is required for progress in therapy and management.