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"Protein degradation, especially via the ubiquitin-proteosome system, has emerged as a critical molecular component to mechanisms of cell death in a variety of prominent neurodegenerative diseases. Thus, the editors of this book should be praised for the comprehensiveness and timeliness of their effort. In this single volume, the reader will find a mixture of valuable information regarding the ubiquitin-proteosome machinery ranging from the most basic to the most clinically-relevant. The book also provides insightful comments and views on the complex question of ubiquitin-proteosome in neurodegeneration by well-respected experts, which enrich this volume with many balanced opinionsand a scientific honesty rarely found in these types of books. It is unquestionable that this publication would be an asset to any neuroscientist and clinician alike." Serge Przedborski, Columbia University Impaired function of the ubiquitin-proteosome system (UPS) has long been implicated as a contributing factor in various neurodegenerative diseases. In fact, the presence of various ubiquitin-decorated protein aggregates is pathonumonic for many such diseases. Unfortunately, this system was sorely neglected until the recent association between several genes, encoding UPS-related proteins, and Parkinson’s disease placed UPS dysfunction center stage in the neurodegeneration field. With increasing interest in this fast growing area, this book represents a timely and critical effort summarizing the most exciting development to date by many renown experts in the field. With a thoughtful and useful structure, the book takes the reader from a detailed introduction of the UPS system, through an elegant discussion of the relationship between UPS and critical cellular functions to an outstanding summary of the UPS in various neurodegenerative diseases. As such, this book serves equally well to both those who are new and those who are knowledgeable to the field. There is no doubt that this book will generate ever more interest in this fertile research area. Mark A. Smith, Case Western Reserve University This is excellent timing! The role of the ubiquitin proteasome system in neurodegeneration is a hot topic, and recent research has shown that this system plays a role in various neurodegenerative diseases, such as Alzheimer’s disease, Parkinson’s disease and Huntington’s disease. This book contains up-to-date reviews on different aspects of the ubiquitin proteasome system and its involvement in several neurodegenerative diseases. It is an indispensable source of information for scientists studying neurodegeneration. The book provides information on the basics of the ubiquitin proteasome system, but mainly describes a number of aspects of involvement of this system in neurodegeneration. All major hypotheses on the possible causes of neurodegeneration, such as oxidative stress, inflammation, and aging, are discussed in view of their effect on the ubiquitin proteasome system. The contributions and different views from leading authors in the field provide a balanced, comprehensive and up-to-date view of the possible role of the proteasome in neurodegeneration. The book is a unique reference work for all biological and medical researchers working in the field of neurodegeneration. Elly M. Hol, Cellular Quality Control Netherlands Institute for Brain Research.

Ubiquitin. --- Proteins --- Nervous system --- Metabolism. --- Degeneration. --- Degeneration, Nerve --- Nerve degeneration --- Nervous system degeneration --- Neurodegenerative disease --- Neurodegenerative diseases --- Neurodegenerative disorders --- Neuron degeneration --- Nissl degeneration --- Retrograde degeneration --- Wallerian degeneration --- Degeneration (Pathology) --- Protein metabolism --- High mobility protein 20 --- HMP-20 --- Degeneration and regeneration --- Neurosciences. --- Cytology. --- Cell Biology. --- Cell biology --- Cellular biology --- Biology --- Cells --- Cytologists --- Neural sciences --- Neurological sciences --- Neuroscience --- Medical sciences --- Cell biology.

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The targeted addition of ubiquitin to proteins is now known to regulate many cellular events, with the enzymes involved in protein ubiquitination linked to a variety of clinical problems, such as cancer, heart disease, and immune dysfunction. In Ubiquitin-Proteasome Protocols, hands-on leaders in the field, many of whom originally developed the methods they describe, detail cutting-edge techniques for studying ubiquitin-dependent protein degradation via the proteasome. The topics covered range broadly from basic biochemistry to cellular assays to discovery techniques using mass spectrometric analysis. These biochemical and cellular methods are necessary to explore the ubiquitin-proteasome system and ubiquitin-proteasome- dependent functions. The protocols follow the successful Methods in Molecular Biology™ series format, each offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls. State-of-the-art and user-friendly, Ubiquitin-Proteasome Protocols offers novice and experienced bench scientists alike a thorough compendium of readily reproducible techniques that will accelerate discovery, enhance productivity, and permit manipulation of the system for varied research purposes.

Electronic books. -- local. --- Proteolytic enzymes -- Laboratory manuals. --- Ubiquitin -- Laboratory manuals. --- Multienzyme Complexes --- Ubiquitin --- Cysteine Endopeptidases --- Multiprotein Complexes --- Enzymes --- Cysteine Proteases --- Ubiquitins --- Endopeptidases --- Peptide Hydrolases --- Macromolecular Substances --- Proteins --- Enzymes and Coenzymes --- Hydrolases --- Chemicals and Drugs --- Amino Acids, Peptides, and Proteins --- Proteolytic enzymes --- Cysteine Endopeptidases. --- Multienzyme Complexes. --- Ubiquitine --- Enzymes protéolytiques --- metabolism. --- Laboratory manuals --- Manuels de laboratoire --- EPUB-LIV-FT SPRINGER-B LIVBIOLO --- Peptide hydrolases --- Proteases --- High mobility protein 20 --- HMP-20 --- Biochemistry. --- Biochemistry, general. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Composition --- Laboratory manuals.

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† 1 a a 4 † 17 10 15 ubiquitin; and of 16 VCP 17 18 20 33 34 34 36 p domain. 41 42 42 43 P U 42 47 binding. C. elegans 16 In 21 22 50 51 52 53 13 and UFD 4 10 of Cdc48. 18 30 of Ufd2. COFACTORS 47 23 13 47 47 47 72 15 15 and of Spt23 p90. Ufd2 and Cdc48. In C. elegans 74 16 75 75 76 76 Ufd2 25 54 54 7 56 p47 7 7 80 30 30 81 82 82 but and CD3 26 DUB COFACTORS 30 UFD3 OTU1 4 Cdc48 30 4 OLE1. 15 27 87 REFERENCES 30 REGULATION OF UBIQUITIN MONOUBIQUITINATION UBIQUITINATION 1 32 7 S) d 33 12 13 14 15 18 19 15 20 21 35 15 15 27 15 31 32 31 33 36 monoubiquitination of pol pol 34 37 34 monoubiquitination. 20 35 trans 3 15 REFERENCES by monoubiquitination. Mol Cell; 2009. UBIQUITIN LIGASE ACTIVITY BY Nedd 1 2 of 41 5 6 8 fold. 9 13 14 edd 43 18 18 K M and k 18 22 23 K M 24 25 K M 26 edd 45 18 27 K M K D 18 25 . 8 10 M 21 28 MECHANISM AND REGULATION OF CRLs 34 41 34 edd 47 48 S. pombe 49 51 p27 and I by SCF and SCF 57 58 59 60 CTD CTD CTD CTD in Cul5 CTD CTD CTD 60 18.

Post-translational modification. --- Ubiquitin. --- Ubiquitin --- Post-translational modification --- Metabolic Phenomena --- Protein Processing, Post-Translational --- Proteins --- Ligases --- Protein Modification, Translational --- Enzymes --- Amino Acids, Peptides, and Proteins --- Phenomena and Processes --- Protein Biosynthesis --- Enzymes and Coenzymes --- Biochemical Processes --- Gene Expression Regulation --- Chemicals and Drugs --- Peptide Biosynthesis --- Chemical Processes --- Genetic Processes --- Biochemical Phenomena --- Genetic Phenomena --- Chemical Phenomena --- Ubiquitination --- Ubiquitin-Protein Ligase Complexes --- Metabolism --- Ubiquitins --- Biology --- Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- Biophysics --- Co-translational modification --- Cotranslational modification --- Modification, Post-translational --- Post-translation protein modification --- Post-translational protein modification --- Posttranslation protein modification --- Posttranslational modification --- Posttranslational protein modification --- High mobility protein 20 --- HMP-20 --- Life sciences. --- Human physiology. --- Molecular biology. --- Proteins. --- Life Sciences. --- Protein Science. --- Human Physiology. --- Molecular Medicine. --- Genetic translation --- Synthesis --- Biochemistry. --- Medicine. --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Medical sciences --- Pathology --- Physicians --- Physiology --- Human body --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Chemistry --- Composition --- Health Workforce --- Proteins . --- Molecular biochemistry --- Molecular biophysics --- Biochemistry --- Biomolecules --- Systems biology --- Proteids --- Polypeptides --- Proteomics --- Medicine --- Protein Biochemistry. --- Biomedical Research. --- Research. --- Biological research --- Biomedical research