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Polyubiquitin

Known as: Polyubiquitin [Chemical/Ingredient], Ubiquitin, poly- 
An oligomer formed from the repetitive linking of the C-terminal glycine of one UBIQUITIN molecule via an isopeptide bond to a lysine residue on a… Expand
National Institutes of Health

Papers overview

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Highly Cited
2016
Highly Cited
2016
The post-translational modification of proteins with polyubiquitin regulates virtually all aspects of cell biology. Eight… Expand
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Highly Cited
2013
Highly Cited
2013
Ubiquitylation is an essential posttranslational protein modification that is implicated in a diverse array of cellular functions… Expand
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Highly Cited
2012
Highly Cited
2012
Mechanisms of protein recognition have been extensively studied for single-domain proteins, but are less well characterized for… Expand
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Highly Cited
2012
Highly Cited
2012
The NAD-dependent histone deacetylase Sirt1 antagonizes p53 transcriptional activity to regulate cell-cycle progression and… Expand
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Highly Cited
2011
Highly Cited
2011
Polymeric chains made of a small protein ubiquitin act as molecular signals regulating a variety of cellular processes… Expand
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Highly Cited
2010
Highly Cited
2010
Polyubiquitin chains mediate a variety of biological processes, ranging from proteasomal targeting to inflammatory signaling and… Expand
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Highly Cited
2006
Highly Cited
2006
Ubiquitin (Ub)‐protein ligases (E3s) frequently modify their substrates with multiple Ub molecules in the form of a polyubiquitin… Expand
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Highly Cited
2005
Highly Cited
2005
Individual ubiquitin (Ub)–protein ligases (E3s) cooperate with specific Ub‐conjugating enzymes (E2s) to modify cognate substrates… Expand
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Highly Cited
2004
Highly Cited
2004
Ubiquitination, a modification in which single or multiple ubiquitin molecules are attached to a protein, serves as a signalling… Expand
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Highly Cited
1982
Highly Cited
1982
Abstract The energies of two and three-chain antiparallel and parallel β-sheets have been minimized. The chains were considered… Expand
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