{"product_id":"the-ubiquitin-code-9781071628584","title":"The Ubiquitin Code","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e\u003cp\u003eThis volume details novel and popular approaches to decipher the \u003ci\u003eUbiquitin Code\u003c\/i\u003e. Chapters guide readers through ubiquitin chain complexity, methods to generate non-hydrolysable ubiquitin-NEDD8, a fully synthetic method for the linear synthesis of fluorescently labelled rhodamine LC3A and LC3B, a HECT ligase-mediated ubiquitylation \u003ci\u003ein vitro, a \u003c\/i\u003eRNAi-based screening to identify DUBs, a Yuh1 activity assay, a pull-down to isolate K48 and K63 chains using specific nanobodies, identification of NeDDylated protein based in a NEDD8\u003csup\u003eR74K \u003c\/sup\u003emutant, \u003ci\u003ein vivo\u003c\/i\u003e identification of NEDDylated proteins from liver diseases, UbL-ID method to identify ubiquitin-like modified proteins, a LC3\/GABARAP capturing system, and methods to isolate peptides that are closely associated with proteasomes or trapped inside the core particle o\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003c\/p\u003e\u003cp\u003e\u003cb\u003ePart I: \u003c\/b\u003e\u003cb\u003eChain Diversity                                                         \u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e1            Thioester and oxyester linkages in the ubiquitin system\u003c\/p\u003e  \u003cp\u003eAlba Ferri-Blazquez, Ernst Jarosch and Thomas Sommer\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e2            Getting to the root of branched ubiquitin chains: A review of current methods and functions\u003c\/p\u003e  \u003cp\u003eAnita Waltho, Thomas Sommer\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003ePart II: Ub and UbL Chemical Tools                                                             \u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e3            Chemical synthesis of non-hydrolysable Ubiquitin(-like) hybrid chains\u003c\/p\u003e  \u003cp\u003eDavid A. Pérez Berrocal, Gerbrand J. van der Heden van Noort and Monique P. C. Mulder \u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e4            Total Linear Chemical Synthesis of LC3A and LC3B\u003c\/p\u003e  \u003cp\u003eYara Huppelschoten, Jens Buchardt, Thomas Eiland Nielsen and Gerbrand J. van der Heden van Noort\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003ePart III: Methods to study Conjugating enzymes (E3s)                                                     \u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e5            A microbead-based flow cytometry assay to assess the activity of Ubiquitin and Ubiquitin-like conjugating enzymes \u003c\/p\u003e  \u003cp\u003eClara Recasens-Zorzo, Pierre Gâtel, Frédérique Brockly and Guillaume Bossis\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e6            Monitoring HECT ubiquitination activity in vitro \u003c\/p\u003e  \u003cp\u003eVincenzo Taibi, Simona Polo and Elena Maspero1     \u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003ePart IV: Methods to study DUBs                                                                  \u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e7            RNAi-based screening for the identification of specific substrate-deubiquitinase pairs \u003c\/p\u003e  \u003cp\u003eNagore Elu, Natalia Presa and Ugo Mayor\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e8            Strategies for monitoring ‘ubiquitin C-terminal hydrolase 1’ (Yuh1) activity \u003c\/p\u003e  \u003cp\u003eShahaf Saad, Eden Berda, Yuval Klein, Suha Issa and Elah Pick\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003ePart V: Methods to identify new targets and regulators                                                 \u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e9            Isolation and Mass Spectrometry Identification of K48 and K63 Ubiquitin Proteome using Chain-Specific Nanobodies \u003c\/p\u003e  \u003cp\u003eMaria Gonzalez-Santamarta, Laurie Ceccato, Ana Sofia Carvalho, Jean-Christophe Rain, Rune Matthiesen and Manuel S. Rodriguez\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e10          A mass spectrometry-based strategy for mapping modification sites for the Ubiquitin-like modifier NEDD8\u003c\/p\u003e  \u003cp\u003eCaio A.B. Oliveira, Ekaterina Isaakova, Petra Beli and Dimitris P. Xirodimas         \u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e11          Isolation of the hepatic ubiquitome\/NEDDylome by streptavidin pull-down assay in the biotinylated ubiquitin (bioUb)\/biotinylated NEDD8 (bioNEDD8) transgenic mice \u003c\/p\u003e  \u003cp\u003eMarina Serrano-Maciá, Teresa Cardoso Delgado and María Luz Martínez-Chantar\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e12          The Lambda display technology: a useful tool for the identification of ubiquitin and ubiquitin like-binding domains \u003c\/p\u003e  \u003cp\u003eElena Santonico\u003c\/p\u003e   \u003cp\u003e\u003c\/p\u003e  \u003cp\u003e13          SUMO-ID: a strategy for the identification of SUMO-dependent proximal interactors \u003c\/p\u003e  \u003cp\u003eOrhi Barroso-Gomila, Ugo Mayor, Rosa Barrio and James D. Sutherland\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e14          Analysis of ATG8 family members using LC3-Interacting Regions (LIR)-based molecular traps \u003c\/p\u003e  \u003cp\u003eGrégoire Quinet, Pierre Génin, Naima Belgareh-Touzé, Oznur Ozturk, Robert Weil, Mickael M. Cohen, Renaud Legouis and Manuel S. Rodriguez\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e15          A computational tool for analysis of mass spectrometry data of ubiquitin enriched samples \u003c\/p\u003e  \u003cp\u003eRune Matthiesen, Manuel S. Rodriguez, and Ana Sofia Carvalho\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003ePart VI:  to measure proteasome activity                                                               \u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e16          In-plate and in-gel assays for the assessment of proteasome activity in \u003ci\u003eCaenorhabditis elegans\u003c\/i\u003e \u003c\/p\u003e  \u003cp\u003eEleni Panagiotidou, Anna Gioran and Niki Chondrogianni\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e17          Isolation of Proteasome-Trapped Peptides (PTPs) for degradome analysis \u003c\/p\u003e  \u003cp\u003eIndrajit Sahu, Manisha Priyadarsini Sahoo, Oded Kleifeld and Michael H. Glickman\u003c\/p\u003e","brand":"Springer-Verlag New York Inc.","offers":[{"title":"Default Title","offer_id":49984479986007,"sku":"9781071628584","price":143.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781071628584.jpg?v=1739451608","url":"https:\/\/bookcurl.com\/products\/the-ubiquitin-code-9781071628584","provider":"Book Curl","version":"1.0","type":"link"}