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Polyubiquitin chains: polymeric protein signals.
The 76-residue protein ubiquitin exists within eukaryotic cells both as a monomer and in the form of isopeptide-linked polymers called polyubiquitin chains. In two well-described cases, structurallyExpand
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Solution Structure of the Proapoptotic Molecule BID A Structural Basis for Apoptotic Agonists and Antagonists
Members of the BCL2 family of proteins are key regulators of programmed cell death, acting either as apoptotic agonists or antagonists. Here we describe the solution structure of BID, presenting theExpand
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Diverse polyubiquitin interaction properties of ubiquitin-associated domains
The ubiquitin-associated (UBA) domain occurs frequently in proteins involved in ubiquitin-dependent signaling pathways. Although polyubiquitin chain binding is considered to be a defining feature ofExpand
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Structural determinants for selective recognition of a Lys48-linked polyubiquitin chain by a UBA domain.
Although functional diversity in polyubiquitin chain signaling has been ascribed to the ability of differently linked chains to bind in a distinctive manner to effector proteins, structural models ofExpand
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Solution Conformation of Lys63-linked Di-ubiquitin Chain Provides Clues to Functional Diversity of Polyubiquitin Signaling*
Diverse cellular events are regulated by post-translational modification of substrate proteins via covalent attachment of one or a chain of ubiquitin molecules. The outcome of (poly)ubiquitinationExpand
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Structure of the s5a:k48-linked diubiquitin complex and its interactions with rpn13.
Degradation by the proteasome typically requires substrate ubiquitination. Two ubiquitin receptors exist in the proteasome, S5a/Rpn10 and Rpn13. Whereas Rpn13 has only one ubiquitin-binding surface,Expand
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Rpn1 and Rpn2 Coordinate Ubiquitin Processing Factors at Proteasome*
Background: Proteasome substrates are recognized by (poly)ubiquitin receptors or mediated by ubiquitin-like domain-containing shuttles. Results: Multiple ubiquitin-like domain-containing proteinsExpand
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Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH.
Ubiquitin modification of proteins is used as a signal in many cellular processes. Lysine side-chains can be modified by a single ubiquitin or by a polyubiquitin chain, which is defined by anExpand
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Analyses of the effects of all ubiquitin point mutants on yeast growth rate.
The amino acid sequence of a protein governs its function. We used bulk competition and focused deep sequencing to investigate the effects of all ubiquitin point mutants on yeast growth rate. ManyExpand
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Evidence for bidentate substrate binding as the basis for the K48 linkage specificity of otubain 1.
Otubain 1 belongs to the ovarian tumor (OTU) domain class of cysteine protease deubiquitinating enzymes. We show here that human otubain 1 (hOtu1) is highly linkage-specific, cleaving Lys48Expand
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