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Titlebook: Conjugation and Deconjugation of Ubiquitin Family Modifiers; Marcus Groettrup Book 2010 Landes Bioscience and Springer Science+Business Me

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51#
發(fā)表于 2025-3-30 09:32:27 | 只看該作者
52#
發(fā)表于 2025-3-30 15:56:43 | 只看該作者
Assembly of K11-Linked Ubiquitin Chains by the Anaphase-Promoting Complex,ttached to a substrate. K48-linked ubiquitin chains target proteins for degradation by the 26S proteasome, while those chains connected through K63 regulate intracellular signaling cascades independently of protein degradation. Although all other linkages are detected in cells, their function is not
53#
發(fā)表于 2025-3-30 16:37:22 | 只看該作者
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發(fā)表于 2025-3-30 23:57:28 | 只看該作者
55#
發(fā)表于 2025-3-31 01:49:16 | 只看該作者
Pupylation,et them for destruction by a bacterial proteasome in a manner akin to ubiquitin in eukaryotes. Despite using a proteasome as the end point for proteolysis, Pup and ubiquitin differ in sequence, structure and method of activation and conjugation to protein substrates. Pup is so far the only known pos
56#
發(fā)表于 2025-3-31 06:38:42 | 只看該作者
57#
發(fā)表于 2025-3-31 12:15:56 | 只看該作者
The In Vivo Functions of Desumoylating Enzymes,mily. All members of this cysteine protease family express isopeptidase activity to deSUMOylate conjugated cellular protein targets. Here, we discuss how SUMO proteases discriminate amongst the SUMOylated targets based on subcellular localization and conjugated SUMO isoform. Several signal transduct
58#
發(fā)表于 2025-3-31 16:11:34 | 只看該作者
Regulatory Functions of Ubiquitin and SUMO in DNA Repair Pathways,raditionally known as a signal for proteasomal degradation, its nondegradative actions are equally important in the control of cellular key processes. Similarly, the SUMO system primarily acts in a nondegradative manner. Accumulating evidence indicates that these nonproteolytic functions of ubiquiti
59#
發(fā)表于 2025-3-31 18:55:37 | 只看該作者
60#
發(fā)表于 2025-3-31 22:58:43 | 只看該作者
In Vivo Functions of Isgylation, on physiological aspects and the biological relevance of ISG15 conjugation and deconjugation. ISG15 contains two domains with structural similarity to ubiquitin and was the first ubiquitin like modifier (UBL) described. It can be conjugated to protein substrates in a process similar to ubiquitin mo
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