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Proteasomes : The World of Regulatory Proteolysis (Molecular by Wolfgang Hilt, Dieter H. Wolf

By Wolfgang Hilt, Dieter H. Wolf

This e-book highlights proteasome constructions and the way they are concerning assorted elements of proteasome functionality. furthermore, the e-book reviews at the sensible roles those hugely built proteolytic machines play in the mobilephone. It used to be an excellent shock to the clinical global that proteolysis offers an important features in mobile law. The shock used to be even better while it used to be came upon that now not lysosomes, yet protease complexes with remarkably subtle architectures have been liable for the keep an eye on of crucial regulatory occasions. Excitingly, proteasomes have been came upon to be enthusiastic about frequent features of cellphone body structure, which incorporated degradation of protein waste, antigen presentation, legislation of cellphone metabolism and cellphone differentiation in addition to keep an eye on of the cellphone cycle. the invention of such a number of and crucial services made research of proteasome mediated regulatory proteolysis a hugely major topic in cellphone biology. Written via pioneers within the box the publication represents a finished updated view on proteasome constructions and features from the last word frontier of mobilephone biology learn. It ties the reader to all features of cellphone functionality. This paintings is an critical resource for scientists operating within the fields of simple and utilized telephone biology and immunology. varied points of proteasome features are linked to the advance of unsafe ailments like melanoma, neurodegeneration, cystic fibrosis or immune problems. hence, information reviewed during this ebook are vital for physicians and pharmacologists lively in study, and specialists within the pharmaceutical undefined.

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Extra resources for Proteasomes : The World of Regulatory Proteolysis (Molecular Biology Intelligence Unit)

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Homologues of 26S proteasome subunits are regulators of transcription and translation. Protein Sci 1998; 7:1250-1254. 73. Hofmann K, Bucher P. The PCI domain: A common theme in three multiprotein complexes. Trends Biochem Sci 1998; 23: 204-205. 74. Seeger M, Kraft R, Ferrell K et al. A novel protein complex involved in signal-transduction possessing similarities to 26S proteasome subunits. FASEB J 1998; 12:469-478. 75. Wei N, Tsuge T, Serino G et al. The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex.

54. Chen P, Hochstrasser M. Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell 1996; 86:961-972. 55. Pamer E, Cresswell P. Mechanisms of MHC class I-restricted antigen processing. Annu Rev Immunol 1998; 16:323-358. 56. Gaczynska M, Rock KL, Spies T et al. Peptidase activities of proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP2 and LMP7. Proc Natl Acad Sci USA 1994; 91:9213-9217.

Cell 1998; 94:615-623. 71. Lupas A, Baumeister W, Hofmann K. A repetitive sequence in subunits of the 26S proteasome and 20S cyclosome (anaphasepromoting complex). Trends Biochem Sci 1997; 22:195-196. 72. Aravind L, Ponting CP. Homologues of 26S proteasome subunits are regulators of transcription and translation. Protein Sci 1998; 7:1250-1254. 73. Hofmann K, Bucher P. The PCI domain: A common theme in three multiprotein complexes. Trends Biochem Sci 1998; 23: 204-205. 74. Seeger M, Kraft R, Ferrell K et al.

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