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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1994 1
1997 1
2001 2
2002 1
2003 2
2004 144
2005 406
2006 478
2007 450
2008 437
2009 451
2010 507
2011 468
2012 515
2013 532
2014 497
2015 451
2016 465
2017 403
2018 373
2019 154
2020 2
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5,943 results
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Page 1
Structure and Function of the 26S Proteasome.
Bard JAM, et al. Annu Rev Biochem 2018 - Review. PMID 29652515 Free PMC article.
To reliably process all the proteins presented to it in the complex cellular environment, the proteasome must combine high promiscuity with exceptional substrate selectivity. ...In addition, these studies revealed a complex conformational landscape that ensures proper substrate selection before the proteasome commits to processive degradation. ...
To reliably process all the proteins presented to it in the complex cellular environment, the proteasome must combine high pro …
The Logic of the 26S Proteasome.
Collins GA and Goldberg AL. Cell 2017 - Review. PMID 28525752 Free PMC article.
However, recent studies indicate that proteasome function is also tightly regulated and determines whether a ubiquitylated protein is destroyed or deubiquitylated and survives longer. This article reviews recent advances in our understanding of the proteasome's multistep ATP-dependent mechanism, its biochemical and structural features that ensure efficient proteolysis and ubiquitin recycling while preventing nonselective proteolysis, and the regulation of proteasome activity by interacting proteins and subunit modifications, especially phosphorylation....
However, recent studies indicate that proteasome function is also tightly regulated and determines whether a ubiquitylated protein is …
The ubiquitin-proteasome system.
Nandi D, et al. J Biosci 2006 - Review. PMID 16595883 Free article.
Eukaryotic proteins targeted for degradation by this pathway are first 'tagged' by multimers of a protein known as ubiquitin and are later proteolyzed by a giant enzyme known as the proteasome. This article recounts the key observations that led to the discovery of ubiquitin-proteasome system (UPS). In addition, different aspects of proteasome biology are highlighted. ...
Eukaryotic proteins targeted for degradation by this pathway are first 'tagged' by multimers of a protein known as ubiquitin and are later p …
Regulation of proteasome assembly and activity in health and disease.
Rousseau A and Bertolotti A. Nat Rev Mol Cell Biol 2018 - Review. PMID 30065390
Central to the regulation of proteasome assembly is TOR complex 1 (TORC1), which is the master regulator of cell growth and stress. This Review discusses how proteasome assembly and the regulation of proteasomal degradation are integrated with cellular physiology, including the interplay between the proteasome and autophagy pathways. ...
Central to the regulation of proteasome assembly is TOR complex 1 (TORC1), which is the master regulator of cell growth and st …
The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy.
Kwon YT and Ciechanover A. Trends Biochem Sci 2017 - Review. PMID 28947091
We overview here the complexity of the ubiquitin code, with an emphasis on the emerging role of linkage-specific degradation signals (degrons) in the ubiquitin-proteasome system (UPS) and the autophagy-lysosome system (hereafter autophagy)....
We overview here the complexity of the ubiquitin code, with an emphasis on the emerging role of linkage-specific degradation signals (degron …
Emerging Paradigm of Crosstalk between Autophagy and the Ubiquitin-Proteasome System.
Nam T, et al. Mol Cells 2017 - Review. PMID 29237114 Free PMC article.
Cellular protein homeostasis is maintained by two major degradation pathways, namely the ubiquitin-proteasome system (UPS) and autophagy. Until recently, the UPS and autophagy were considered to be largely independent systems targeting proteins for degradation in the proteasome and lysosome, respectively. ...
Cellular protein homeostasis is maintained by two major degradation pathways, namely the ubiquitin-proteasome system (UPS) and autoph …
Tools to investigate the ubiquitin proteasome system.
Leestemaker Y and Ovaa H. Drug Discov Today Technol 2017 - Review. PMID 29249239 Free article.
Ubiquitination affects substrate proteins in different ways, for example by resulting in degradation of the substrate protein by the 26S proteasome. ...
Ubiquitination affects substrate proteins in different ways, for example by resulting in degradation of the substrate protein by the 26S …
The recognition of ubiquitinated proteins by the proteasome.
Grice GL and Nathan JA. Cell Mol Life Sci 2016 - Review. PMID 27137187 Free PMC article.
A major function of ubiquitination is to signal degradation of intracellular proteins by the 26S proteasome. Lysine-48 (K48) linked polyubiquitin chains are well established as the canonical signal for proteasomal degradation, but recent studies show a role for other ubiquitin linked chains in facilitating degradation by the 26S proteasome. Here, we review how different types of polyubiquitin linkage bind to ubiquitin receptors on the 26S proteasome, how they signal degradation and discuss the implications of ubiquitin chain linkage in regulating protein breakdown by the proteasome....
A major function of ubiquitination is to signal degradation of intracellular proteins by the 26S proteasome. Lysine-48 (K48) linked p …
An evolutionarily conserved pathway controls proteasome homeostasis.
Rousseau A and Bertolotti A. Nature 2016. PMID 27462806 Free PMC article.
The proteasome is essential for the selective degradation of most cellular proteins, but how cells maintain adequate amounts of proteasome is unclear. Here we show that there is an evolutionarily conserved signalling pathway controlling proteasome homeostasis. Central to this pathway is TORC1, the inhibition of which induced all known yeast 19S regulatory particle assembly-chaperones (RACs), as well as proteasome subunits. ...
The proteasome is essential for the selective degradation of most cellular proteins, but how cells maintain adequate amounts of pr
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