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Protein Degradation Series, 4 Volume Set by R. John Mayer, Aaron J. Ciechanover, Martin Rechsteiner

25 February 2017 adminCell Biology

By R. John Mayer, Aaron J. Ciechanover, Martin Rechsteiner

Книга Protein Degradation sequence, four quantity Set Protein Degradation sequence, four quantity SetКниги Биология Автор: R. John Mayer, Aaron J. Ciechanover, Martin Rechsteiner Год издания: 2008 Формат: pdf Издат.:Wiley-VCH Страниц: 1203 Размер: 14,6 Mb ISBN: 352731878X Язык: Русский0 (голосов: zero) Оценка:Nobel prize content material through Nobel prize winners: the fundamental position of protein degradation as a regulatory swap in mobilephone body structure has been venerated by way of the 2004 Nobel prize in Chemistry to Aaron Ciechanover, editor of the sequence, and Avram Hershko, the writer of the hole bankruptcy of quantity 1. vast insurance: 4 volumes with greater than 50 contributions in overall conceal all points of protein degradation. each one person quantity highlights a distinct element of the sector; all 4 volumes jointly give you the so much complete reference on protein degradation to be had. unequalled services: Editors and authors contain almost the entire best scientists within the box, together with the pioneers of protein degradation learn.

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Additional info for Protein Degradation Series, 4 Volume Set

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Mdm2 promotes p21 waf 1=cip1 proteasomal turnover independently of ubiquitylation. , 2003, 22, 6365–6377. Varshavsky, A. The N-end rule: Functions, mysteries, uses. Proc. Natl. Acad. Sci. USA, 1996, 93, 12142– 12149. Johnson, E. , Ma, P. , Ota, I. M. and Varshavsky, A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. , 1995, 270, 17442–17456. Polevoda, B. and Sherman, F. N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins.

Roussel, M. , and Sherr, C. J. N-terminal polyubiquitination and degradation of the Arf tumor suppressor. , 2004, 18, 1862–1874. , Schwartz, A. , and Ciechanover, A. The Tumor Suppressor Protein p16INK4a and the Human Papillomavirus oncoprotein E7-58 are Naturally Occurring LysineLess Proteins that are Degraded by the Ubiquitin System: Direct Evidence for Ubiquitination at the N-Terminal Residue. J. Biol. , 2004, 279, 41414–41421. Sheaff, R. , Singer, J. , Roberts, J. M. and Clurman, B. E. Proteasomal turnover of p21 Cip1 does not require p21 Cip1 ubiquitination.

Ecker, D. , Gonda, D. K. and Varshavsky, A. A multi ubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science, 1989, 243, 1576–1583. , Jensen, J. , Nguygen, H. B. and Weissman, A. M. Activation-dependent ubiquitination of a T cell antigen receptor subunit on multiple intracellular lysines. J. Biol. , 1994, 269, 14244–14247. , Staszewski, L. and Bohmann, D. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the d-domain. Cell, 1994, 78, 787– 798. King, R.

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