AbstractTwo papers published in 1984 by the Varshavsky laboratory revealed that the ubiquitin/proteasome pathway is the principal system for degradation of short-lived proteins in mammalian cells, setting the stage for future demonstrations of this pathway's many regulatory roles. This perspective discusses the impact of those papers and highlights some of the subsequent insights that have led to our current appreciation of the breadth of ubiquitin-mediated signaling
Emerging data reveal that besides degrading proteins tagged with ubiquitin, the proteasome plays a m...
The 2004 Nobel Prize in chemistry for the discovery of protein ubiquitination has led to the recogni...
AbstractThe ubiquitin–proteasome system (UPS) is the primary selective degradation system in the nuc...
AbstractTwo papers published in 1984 by the Varshavsky laboratory revealed that the ubiquitin/protea...
International audienceThe importance of the discovery, at the beginning of the 1980s, of a complex ...
The Nobel Prize in Chem. for 2004 is shared by Aaron Ciechanover, Avram Hershko and Irwin Rose, who ...
What follows is a story of some of the lab’s adventures mentioned above, including the inventions of...
AbstractThis year the most prestigious prize in medical sciences, the Lasker Award, has been present...
First paragraph (this article has no abstract): In a review published in 2004 [1] and that still rep...
AbstractIn the ubiquitin-proteasome system, substrates fated for destruction first acquire covalent ...
Ubiquitylation is an intracellular chemical reaction in which the small polypeptide, ubiquitin, is c...
Protein turnover plays an important role in a broad spectrum of cellular processes. Notably, approxi...
AbstractMost proteasome substrates are marked for degradation by ubiquitin conjugation, but some are...
The ubiquitin system has become synonymous with the modification of lysine residues. However, the su...
AbstractThe ubiquitin proteasome system (UPS) is essential in regulating myriad aspects of protein f...
Emerging data reveal that besides degrading proteins tagged with ubiquitin, the proteasome plays a m...
The 2004 Nobel Prize in chemistry for the discovery of protein ubiquitination has led to the recogni...
AbstractThe ubiquitin–proteasome system (UPS) is the primary selective degradation system in the nuc...
AbstractTwo papers published in 1984 by the Varshavsky laboratory revealed that the ubiquitin/protea...
International audienceThe importance of the discovery, at the beginning of the 1980s, of a complex ...
The Nobel Prize in Chem. for 2004 is shared by Aaron Ciechanover, Avram Hershko and Irwin Rose, who ...
What follows is a story of some of the lab’s adventures mentioned above, including the inventions of...
AbstractThis year the most prestigious prize in medical sciences, the Lasker Award, has been present...
First paragraph (this article has no abstract): In a review published in 2004 [1] and that still rep...
AbstractIn the ubiquitin-proteasome system, substrates fated for destruction first acquire covalent ...
Ubiquitylation is an intracellular chemical reaction in which the small polypeptide, ubiquitin, is c...
Protein turnover plays an important role in a broad spectrum of cellular processes. Notably, approxi...
AbstractMost proteasome substrates are marked for degradation by ubiquitin conjugation, but some are...
The ubiquitin system has become synonymous with the modification of lysine residues. However, the su...
AbstractThe ubiquitin proteasome system (UPS) is essential in regulating myriad aspects of protein f...
Emerging data reveal that besides degrading proteins tagged with ubiquitin, the proteasome plays a m...
The 2004 Nobel Prize in chemistry for the discovery of protein ubiquitination has led to the recogni...
AbstractThe ubiquitin–proteasome system (UPS) is the primary selective degradation system in the nuc...
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