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Extraproteasomal Rpn10 Restricts Access of the Polyubiquitin-Binding Protein Dsk2 to Proteasome

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TLDR
By restricting Dsk2 access to the proteasome, extraproteasomal Rpn10 was essential for alleviating the cellular stress associated with DSk2, highlighting the importance of polyubiquitin shuttles such as RPN10 and Dsk1 in controlling the ubiquitin landscape.
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This article is published in Molecular Cell.The article was published on 2008-11-07 and is currently open access. It has received 95 citations till now. The article focuses on the topics: Ubiquitin-conjugating enzyme & Polyubiquitin binding.

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Citations
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Journal ArticleDOI

Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome

TL;DR: The proteasome contains deubiquitinating enzymes (DUBs) that can remove ubiquitin before substrate degradation initiates, thus allowing some substrates to dissociate from the proteasomes and escape degradation.
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Ubiquitin-binding domains — from structures to functions

TL;DR: New structure-based insights provide strategies for controlling cellular processes by targeting ubiquitin–UBD interfaces with implications for drug design and cell reprograming.
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Regulation of proteasome activity in health and disease.

TL;DR: The contributions of the proteasome to human pathology, mechanisms that regulate the proteolytic capacity of the Proteasome are described, and strategies to modulate proteasomes function as a therapeutic approach to ameliorate diseases associated with altered UPS function are discussed.
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The Ubiquitin–Proteasome System of Saccharomyces cerevisiae

TL;DR: The diverse effects of ubiquitylation reflect the assembly of structurally distinct ubiquitin chains on target proteins.
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Gene Overexpression: Uses, Mechanisms, and Interpretation

TL;DR: The history of overexpression, the mechanisms that are responsible for overexploration phenotypes, tests that begin to distinguish between those mechanisms, the varied ways in which overexposure is used, the methods and reagents available in several organisms, and the relevance of overexpression to human disease are described.
References
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Journal ArticleDOI

The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction

TL;DR: It is clear now that degradation of cellular proteins is a highly complex, temporally controlled, and tightly regulated process that plays major roles in a variety of basic pathways during cell life and death as well as in health and disease.
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Recognition of the polyubiquitin proteolytic signal.

TL;DR: The properties of the substrates studied here implicate substrate unfolding as a kinetically dominant step in the proteolysis of properly folded proteins, and suggest that extraproteasomal chaperones are required for efficient degradation of certain proteasome substrates.
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A proteomics approach to understanding protein ubiquitination

TL;DR: A proteomics approach to enrich, recover, and identify ubiquitin conjugates from Saccharomyces cerevisiae lysate provides a general tool for the large-scale analysis and characterization of protein ubiquitination.
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