Published July 6, 2004
by Taylor & Francis .
Written in English
|The Physical Object|
|Number of Pages||410|
SUMOylation is an essential post-translational protein modification in various cellular functions. To clarify the role of SUMOylation, numerous screening approaches have been reported for the discovery of novel SUMOylated proteins. SUMOylation and ubiquitination: current and emerging concepts. [Van Gene Wilson;] -- Most proteins undergo post-translational modifications altering physical and chemical properties, folding, conformation distribution, stability, activity and function. This comprehensive and up-to-date book is the definitive reference volume on all aspects. Van G. Wilson presents a new book on SUMOylation and Ubiquitination: Current and Emerging Concepts Written by highly respected leaders in their fields under the expert guidance of the editor, this volume covers the principles of ubiquitination and SUMOylation, presents detailed reviews of current and emerging concepts and highlights new advances in all areas of SUMOylation and ubiquitination. SUMOylation and Ubiquitination review Excerpt from a book review of SUMOylation and Ubiquitination: Current and Emerging Concepts "This is a comprehensive and in-depth overview of recent advances in our understanding of the physiological roles and mechanisms of action of these important regulatory covalent modifications.
Ubiquitin (Ub) is a 76 amino acid protein with seven lysine residues that can form polyubiquitin chains of eight different linkages (K6, K11, K27, K33, K48, K63, and Met1) as well as mixed and branched chains .The generation of different protein Ub chains provides structural diversity allowing proteins with specific Ub-binding domains (UBDs) to discriminate between these different structures. M.A van Es, A.R. La Spada, in Encyclopedia of the Neurological Sciences (Second Edition), Sumoylation. Sumoylation is a reversible posttranslational modification in which a small ubiquitin-like modifier (SUMO) is covalently conjugated to a lysine residue in a target protein. This provides an efficient way to modulate the subcellular localization, activity, and stability of a wide variety. Posttranslational modification with small ubiquitin-related modifier (SUMO) proteins is now established as one of the key regulatory protein modifications in eukaryotic cells. Hundreds of proteins involved in processes such as chromatin organization, transcription, DNA repair, macromolecular assembly, protein homeostasis, trafficking, and signal transduction are subject to reversible. Whimsical line drawings make The Big Book of Sumo the most user-friendly sumo guide available. Super sumo fan Mina Hall covers all aspects of the sport, including its history, traditions, training methods, stable life, rankings, fighting holds, and s:
Small Ubiquitin‐like modifier (SUMO) is a conserved protein that is ubiquitously expressed in eukaryotes and is essential for viability. It serves as a reversible posttranslational modifier by forming an isopeptide bond with lysine residues in many target proteins, in a catalytic process termed SUMOylation. SUMOylation of proteins results in altered inter‐ or intramolecular interactions of. Sumoylation. Sumoylation is an essential transient posttranslational modification that is predominantly detected in the nucleus and has key functions in many cellular pathways, including transcription, chromatin regulation, DNA replication, DNA damage responses, RNA splicing, cell cycle regulation, protein degradation, and intracellular trafficking (Droescher, Chaugule, & Pichler, ;. Systematic study of protein sumoylation: Development of a site-specific predictor of SUMOsp Jian Ren, Xinjiao Gao, Changjiang Jin, Mei Zhu, Xiwei Wang, Andrew Shaw, Longping Wen, Xuebiao Yao and Yu Xue. Proteomics. ; This volume, edited and written by leading international experts, is the first book to be devoted to sumoylation. It presents information on the history, evolution and mechanisms of sumoylation, discusses SUMO proteases, ligases and conjugation pathways, and reviews the impact on modification and nucleocytoplasmic transport, PML nuclear bodies, and transcriptional regulation.