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SUMO: a history of modification.
  • R. Hay
  • Biology, Medicine
  • Molecular cell
  • 1 April 2005
The small ubiquitin-like modifier (SUMO) is covalently linked to a variety of proteins and is deconjugated by SUMO-specific proteases. A characteristic of SUMO modification is that the biologicalExpand
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SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation.
Activation of NF-kappaB is achieved by ubiquitination and proteasome-mediated degradation of IkappaBalpha. We have detected modified IkappaBalpha, conjugated to the small ubiquitin-like proteinExpand
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System-Wide Changes to SUMO Modifications in Response to Heat Shock
The small ubiquitin-like modifier protein SUMO is redistributed among many targets to mediate both short- and long-term signaling events. SUMO Status Revealed Posttranslational modification ofExpand
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Polymeric Chains of SUMO-2 and SUMO-3 Are Conjugated to Protein Substrates by SAE1/SAE2 and Ubc9*
Conjugation of the small ubiquitin-like modifier SUMO-1/SMT3C/Sentrin-1 to proteins in vitro is dependent on a heterodimeric E1 (SAE1/SAE2) and an E2 (Ubc9). Although SUMO-2/SMT3A/Sentrin-3 andExpand
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Mdm2-Mediated NEDD8 Conjugation of p53 Inhibits Its Transcriptional Activity
The only reported role for the conjugation of the NEDD8 ubiquitin-like molecule is control of the activity of SCF ubiquitin ligase complexes. Here, we show that the Mdm2 RING finger E3 ubiquitinExpand
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Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind both substrate and a ubiquitin E2Expand
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SUMO-1 Conjugation in Vivo Requires Both a Consensus Modification Motif and Nuclear Targeting*
SUMO-1 is a small ubiquitin-related modifier that is covalently linked to many cellular protein targets. Proteins modified by SUMO-1 and the SUMO-1-activating and -conjugating enzymes are locatedExpand
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Ubch9 conjugates SUMO but not ubiquitin
Ubiquitin conjugating enzymes participate in the thioester cascade that leads to protein ubiquitination. Although Ubc9 is homologous to E2 ubiquitin conjugating enzymes we have shown that it isExpand
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Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62.
A role for redox regulation in activation of the NF-kappa B transcription factor was suggested by the observation that DNA binding activity of free protein, but not preformed DNA-protein complex, isExpand
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Distinct and Overlapping Sets of SUMO-1 and SUMO-2 Target Proteins Revealed by Quantitative Proteomics*S
The small ubiquitin-like modifier (SUMO) family in vertebrates includes three different family members that are conjugated as post-translational modifications to target proteins. SUMO-2 and -3 areExpand
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