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Ubiquitin C-terminal hydrolases

Larsen, C. N., Krantz, B. A., and Wilkinson, K. D. Substrate specificity of deubiquitinating enzymes ubiquitin C-terminal hydrolases. Biochemistry, 1998, 37, 3358-68. [Pg.212]

Structural basis for the specificity of ubiquitin C-terminal hydrolases, Embo J, 1999, 18, 3877-87. [Pg.213]

Eytan, E., Armon, T., Heller, H., Beck, S., and Hershko, A. Ubiquitin C-terminal hydrolase activity associated with the 26 S protease complex, J Biol Chem, 1993, 268, 4668-74. [Pg.216]

Ubiquitinated H2A and H2B disappear at metaphase and reappear in anaphase [251-253]. Histone ubiquitination may also be involved in cell cycle progression through S phase [254]. In dividing and non-dividing cells, the ubiquitin moiety of the ubiquitinated histones is in rapid equilibrium with a pool of free ubiquitin [238,239]. The turnover of the ubiquitinated histones is presumably catalyzed by ubiquitin-C-terminal hydrolases. Uni- and multi-cellular eukaryotes contain... [Pg.227]

Zhao, R., Misek, D. E., Kuick, R., Brenner, D. E., Hanash, S. M. (2003). Molecular profiling of the immune response in colon cancer using protein microarrays occurrence of autoanti-bodies to ubiquitin C-terminal hydrolase L3. Proteomics 3, 2108-2115. [Pg.156]

Sequence motifs [33330 ANK (ANKyrin-like) repeats AAA (ATPases associated with a variety of cellular activities) domain or CAD (conserved ATPase domain) with Walker A and B motifs KEKE (motif rich in alternating lysine (K) and glutamate (E) residues) cys box of UBPs (ubiquitin-processing enzymes) nun- LRR (leucine-rich repeat)-like motif [ZD MPN (found in Mprland Padl in the N terminus) motif ISSSSSSS PCI (for proteasome, COP9andinitiation factor 3) motif H UCH (ubiquitin C-terminal hydrolases) block. [Pg.210]

The action of 26S proteasome generates several types of products including free peptides, and peptides linked to ubiquitin chains, which are converted to free and reusable Ub by the action of ubiquitin-C-terminal hydrolases or isopeptidases. Cytosolic peptidases further degrade short peptides to free amino acids. [Pg.433]

Denton JA, Kelly JM (2011) Disruption of Trichoderma reesei crel, encoding an ubiquitin C-terminal hydrolase, results in increased cellulase activity. BMC Biotechnol 11 103 Divne C, Stihlberg J, Reinikainen T, Ruohonen L, Pettersson G, Knowles JK, Teeri TT, Jones TA (1994) The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Science 265 524-528... [Pg.387]


See other pages where Ubiquitin C-terminal hydrolases is mentioned: [Pg.104]    [Pg.6]    [Pg.17]    [Pg.132]    [Pg.194]    [Pg.352]    [Pg.716]    [Pg.742]    [Pg.269]    [Pg.228]    [Pg.2]    [Pg.234]    [Pg.331]    [Pg.525]    [Pg.292]    [Pg.643]    [Pg.732]    [Pg.368]    [Pg.643]    [Pg.732]    [Pg.525]    [Pg.402]    [Pg.403]    [Pg.276]    [Pg.476]    [Pg.735]   
See also in sourсe #XX -- [ Pg.194 ]




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C-terminal

Ubiquitin C-terminal Hydrolases (UCH)

Ubiquitin C-terminal hydrolase

Ubiquitin C-terminal hydrolase

Ubiquitin, ubiquitination

Ubiquitination

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