Deubiquitinating Enzymes

Known as: Deubiquitinating Enzymes [Chemical/Ingredient], Deubiquitinases, Deubiquitinating Enzyme 
Deubiquitinating Enzymes are hydrolases that catalyze cleavage of ubiquitinated substrates with addition of H2O at the point of cleavage. Protein… (More)
National Institutes of Health

Papers overview

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Highly Cited
2011
Highly Cited
2011
Ubiquitin-tagged substrates are degraded by the 26S proteasome, which is a multisubunit complex comprising a proteolytic 20S core… (More)
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Highly Cited
2010
Highly Cited
2010
Ubiquitination is a reversible posttranslational modification that is essential for cell cycle control, and it is becoming… (More)
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Highly Cited
2009
Highly Cited
2009
Deubiquitinating enzymes (Dubs) function to remove covalently attached ubiquitin from proteins, thereby controlling substrate… (More)
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Review
2009
Review
2009
Ubiquitylation is a reversible protein modification that is implicated in many cellular functions. Recently, much progress has… (More)
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Review
2009
Review
2009
The proteasome is an intricate molecular machine, which serves to degrade proteins following their conjugation to ubiquitin… (More)
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Highly Cited
2008
Highly Cited
2008
Ubiquitin chain complexity in cells is likely regulated by a diverse set of deubiquitinating enzymes (DUBs) with distinct… (More)
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Highly Cited
2006
Highly Cited
2006
Uch37 is one of the three principal deubiquitinating enzymes (DUBs), and the only ubiquitin carboxy-terminal hydrolase (UCH… (More)
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Highly Cited
2002
Highly Cited
2002
The ubiquitin (Ub)-proteasome system includes a large family of deubiquitinating enzymes (DUBs). Many members are assigned to… (More)
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Highly Cited
2002
Highly Cited
2002
Eukaryotic genomes encode large families of deubiquitinating enzymes (DUBs). Genetic data suggest that Fat facets (Faf), a… (More)
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Highly Cited
2000
Highly Cited
2000
Attachment of proteins to ubiquitin is reversed by specialized proteases called deubiquitinating enzymes (Dubs), which are also… (More)
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