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   https://doi.org/10.1021/acs.jpclett.3c01040  

   Henderson, Lucas W.; Sharon, Edie M.; Gautam, Amit K.; Anthony, Adam J.; Jarrold, Martin F.; Russell, David H.; Matouschek, Andreas; Clemmer, David E. (June 2023, The Journal of Physical Chemistry Letters)
2. Degradation of SERRATE via ubiquitin-independent 20S proteasome to survey RNA metabolism

   https://doi.org/10.1038/s41477-020-0721-4  

   Li, Yanjun; Sun, Di; Ma, Zeyang; Yamaguchi, Karissa; Wang, Lin; Zhong, Songxiao; Yan, Xingxing; Shang, Baoshuan; Nagashima, Yukihiro; Koiwa, Hisashi; et al (August 2020, Nature Plants)
3. The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag

   https://doi.org/10.1038/s41467-021-26427-0  

   Sahu, Indrajit; Mali, Sachitanand M.; Sulkshane, Prasad; Xu, Cong; Rozenberg, Andrey; Morag, Roni; Sahoo, Manisha Priyadarsini; Singh, Sumeet K.; Ding, Zhanyu; Wang, Yifan; et al (December 2021, Nature Communications)

   Abstract The proteasome, the primary protease for ubiquitin-dependent proteolysis in eukaryotes, is usually found as a mixture of 30S, 26S, and 20S complexes. These complexes have common catalytic sites, which makes it challenging to determine their distinctive roles in intracellular proteolysis. Here, we chemically synthesize a panel of homogenous ubiquitinated proteins, and use them to compare 20S and 26S proteasomes with respect to substrate selection and peptide-product generation. We show that 20S proteasomes can degrade the ubiquitin tag along with the conjugated substrate. Ubiquitin remnants on branched peptide products identified by LC-MS/MS, and flexibility in the 20S gate observed by cryo-EM, reflect the ability of the 20S proteasome to proteolyze an isopeptide-linked ubiquitin-conjugate. Peptidomics identifies proteasome-trapped ubiquitin-derived peptides and peptides of potential 20S substrates in Hi20S cells, hypoxic cells, and human failing-heart. Moreover, elevated levels of 20S proteasomes appear to contribute to cell survival under stress associated with damaged proteins. 

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4. Dihydroquinazolines enhance 20S proteasome activity and induce degradation of α-synuclein, an intrinsically disordered protein associated with neurodegeneration

   https://doi.org/10.1016/j.bmcl.2021.127821  

   Fiolek, Taylor J.; Magyar, Christina L.; Wall, Tyler J.; Davies, Steven B.; Campbell, Molly V.; Savich, Christopher J.; Tepe, Jetze J.; Mosey, R. Adam (March 2021, Bioorganic & Medicinal Chemistry Letters)

   null (Ed.)
5. Fast and Effective Prediction of the Absolute Binding Free Energies of Covalent Inhibitors of SARS-CoV-2 Main Protease and 20S Proteasome

   https://doi.org/10.1021/jacs.2c00853  

   Zhou, Jiao; Saha, Arjun; Huang, Ziwei; Warshel, Arieh (May 2022, Journal of the American Chemical Society)