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NeuroMolecular Medicine, 2013
Hibernating squirrels slow blood flow to a crawl, but sustain no damage to brain or other tissues. This phenomenon provides an excellent model of natural tolerance to ischemia. Small ubiquitin-like modifier (SUMO) is a 100-residue peptide that modifies other proteins by being attached to the epsilon amino group of specific lysine residues.
John M. Hallenbeck, Yang-ja Lee
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Hibernating squirrels slow blood flow to a crawl, but sustain no damage to brain or other tissues. This phenomenon provides an excellent model of natural tolerance to ischemia. Small ubiquitin-like modifier (SUMO) is a 100-residue peptide that modifies other proteins by being attached to the epsilon amino group of specific lysine residues.
John M. Hallenbeck, Yang-ja Lee
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SUMO and transcriptional regulation
Seminars in Cell & Developmental Biology, 2004The small ubiquitin-like modifier (SUMO) is covalently attached to lysine residues in target proteins and in doing so changes the properties of the modified protein. Here we examine the role of SUMO modification in transcriptional regulation. SUMO addition to components of the transcriptional apparatus does not have a common consequence as it can both ...
Michael H. Tatham +2 more
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Annual Review of Cell and Developmental Biology, 2000
▪ Abstract SUMO (small ubiquitin-related modifier) is the best-characterized member of a growing family of ubiquitin-related proteins. It resembles ubiquitin in its structure, its ability to be ligated to other proteins, as well as in the mechanism of ligation.
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▪ Abstract SUMO (small ubiquitin-related modifier) is the best-characterized member of a growing family of ubiquitin-related proteins. It resembles ubiquitin in its structure, its ability to be ligated to other proteins, as well as in the mechanism of ligation.
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Biochemical Society Transactions, 2013
SUMO (small ubiquitin-like modifier) emerged from the shadow of the well-established ubiquitin some 15 years ago when it was shown that a distinct conjugation pathway was responsible for SUMO modification. Since then it has been established that SUMO modifies over a thousand substrates and plays diverse roles in many important biological processes ...
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SUMO (small ubiquitin-like modifier) emerged from the shadow of the well-established ubiquitin some 15 years ago when it was shown that a distinct conjugation pathway was responsible for SUMO modification. Since then it has been established that SUMO modifies over a thousand substrates and plays diverse roles in many important biological processes ...
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2009
Post-translational modification by SUMO is now recognized as an important regulatory method employed by the cell to reversibly modulate the activity, stability, or localization of intracellular proteins. A dedicated enzymatic machinery is involved in the processing, attachment, and removal of the modifier with high selectivity.
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Post-translational modification by SUMO is now recognized as an important regulatory method employed by the cell to reversibly modulate the activity, stability, or localization of intracellular proteins. A dedicated enzymatic machinery is involved in the processing, attachment, and removal of the modifier with high selectivity.
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Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation
Nature Structural &Molecular Biology, 2017I. Hendriks +5 more
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Function and regulation of SUMO proteases
Nature Reviews Molecular Cell Biology, 2012Christopher M Hickey, Mark Hochstrasser
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Sumo, ubiquitin's mysterious cousin
Nature Reviews Molecular Cell Biology, 2001Stefan Müller +2 more
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