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

Year Number of Results
1961 3
1962 1
1965 1
1966 3
1967 5
1968 2
1969 8
1970 7
1971 7
1972 10
1973 6
1974 18
1975 25
1976 36
1977 22
1978 25
1979 31
1980 23
1981 33
1982 41
1983 44
1984 46
1985 60
1986 52
1987 46
1988 59
1989 47
1990 75
1991 68
1992 81
1993 89
1994 76
1995 115
1996 142
1997 165
1998 157
1999 175
2000 169
2001 175
2002 208
2003 177
2004 218
2005 274
2006 302
2007 332
2008 357
2009 363
2010 382
2011 346
2012 390
2013 418
2014 419
2015 428
2016 427
2017 434
2018 429
2019 379
2020 425
2021 456
2022 566
2023 585
2024 200

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9,589 results

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Page 1
The Contribution of the 20S Proteasome to Proteostasis.
Kumar Deshmukh F, Yaffe D, Olshina MA, Ben-Nissan G, Sharon M. Kumar Deshmukh F, et al. Biomolecules. 2019 May 16;9(5):190. doi: 10.3390/biom9050190. Biomolecules. 2019. PMID: 31100951 Free PMC article. Review.
The last decade has seen accumulating evidence of various proteins being degraded by the core 20S proteasome, without its regulatory particle(s). Here, we will describe recent advances in our knowledge of the functional aspects of the 20S proteasome, exploring sever …
The last decade has seen accumulating evidence of various proteins being degraded by the core 20S proteasome, without its regulatory …
ECPAS/Ecm29-mediated 26S proteasome disassembly is an adaptive response to glucose starvation.
Choi WH, Yun Y, Byun I, Kim S, Lee S, Sim J, Levi S, Park SH, Jun J, Kleifeld O, Kim KP, Han D, Chiba T, Seok C, Kwon YT, Glickman MH, Lee MJ. Choi WH, et al. Cell Rep. 2023 Jul 25;42(7):112701. doi: 10.1016/j.celrep.2023.112701. Epub 2023 Jun 27. Cell Rep. 2023. PMID: 37384533 Free article.
The 26S proteasome comprises 20S catalytic and 19S regulatory complexes. Approximately half of the proteasomes in cells exist as free 20S complexes; however, our mechanistic understanding of what determines the ratio of 26S to 20S species remains incomplete. …
The 26S proteasome comprises 20S catalytic and 19S regulatory complexes. Approximately half of the proteasomes in cells exist as free …
Beyond cells: The extracellular circulating 20S proteasomes.
Dwivedi V, Yaniv K, Sharon M. Dwivedi V, et al. Biochim Biophys Acta Mol Basis Dis. 2021 Mar 1;1867(3):166041. doi: 10.1016/j.bbadis.2020.166041. Epub 2020 Dec 16. Biochim Biophys Acta Mol Basis Dis. 2021. PMID: 33338594 Free article. Review.
Accumulating evidence arising from numerous clinical studies indicate that assembled and functional 20S proteasome complexes circulate freely in plasma. Elevated levels of this core proteolytic complex have been found in the plasma of patients suffering from blood, skin an …
Accumulating evidence arising from numerous clinical studies indicate that assembled and functional 20S proteasome complexes circulat …
Small-Molecule Inhibitors of the Proteasome's Regulatory Particle.
Muli CS, Tian W, Trader DJ. Muli CS, et al. Chembiochem. 2019 Jul 15;20(14):1739-1753. doi: 10.1002/cbic.201900017. Epub 2019 May 24. Chembiochem. 2019. PMID: 30740849 Free PMC article. Review.
The second is the regulatory complex (19S RP), which has a myriad of activities including recognizing proteins marked for degradation and shuttling the protein into the 20S CP to be degraded. Small-molecule inhibitors of the 20S CP have been developed and are except …
The second is the regulatory complex (19S RP), which has a myriad of activities including recognizing proteins marked for degradation and sh …
Regulating the 20S proteasome ubiquitin-independent degradation pathway.
Ben-Nissan G, Sharon M. Ben-Nissan G, et al. Biomolecules. 2014 Sep 23;4(3):862-84. doi: 10.3390/biom4030862. Biomolecules. 2014. PMID: 25250704 Free PMC article. Review.
However, it is now becoming clear that proteins can also be targeted for degradation by the core 20S proteasome itself. Degradation by the 20S proteasome does not require ubiquitin tagging or the presence of the 19S regulatory particle; rather, it relies on the inhe …
However, it is now becoming clear that proteins can also be targeted for degradation by the core 20S proteasome itself. Degradation b …
Redox regulation of the proteasome via S-glutathionylation.
Demasi M, Netto LE, Silva GM, Hand A, de Oliveira CL, Bicev RN, Gozzo F, Barros MH, Leme JM, Ohara E. Demasi M, et al. Redox Biol. 2013 Dec 14;2:44-51. doi: 10.1016/j.redox.2013.12.003. Redox Biol. 2013. PMID: 24396728 Free PMC article. Review.
Alternatively, the proteasome is also active when dissociated from regulatory units. This free pool of 20S proteasome is described in yeast to mammalian cells. The free 20S proteasome degrades proteins by a process independent of poly-ubiquitinylation and ATP consum …
Alternatively, the proteasome is also active when dissociated from regulatory units. This free pool of 20S proteasome is described in …
Proteasomes: Isolation and Activity Assays.
Li Y, Tomko RJ Jr, Hochstrasser M. Li Y, et al. Curr Protoc. 2023 Apr;3(4):e717. doi: 10.1002/cpz1.717. Curr Protoc. 2023. PMID: 37026813 Free PMC article.
Here we describe simple, one-step purification schemes for isolating the 26S proteasome and its 19S RP and 20S CP subcomplexes from the yeast Saccharomyces cerevisiae. A gel filtration step can be added to further enhance purity. ...Basic Protocol 1: Purification of active …
Here we describe simple, one-step purification schemes for isolating the 26S proteasome and its 19S RP and 20S CP subcomplexes from t …
Molecular biology of proteasomes.
Tanaka K. Tanaka K. Mol Biol Rep. 1995;21(1):21-6. doi: 10.1007/BF00990966. Mol Biol Rep. 1995. PMID: 7565659 Review.
Eukaryotic proteasomes are unusually large proteins with a heterogeneous subunit composition and have been classified into two isoforms with apparently distinct sedimentation coefficients of 20S and 26S. The 20S proteasome is composed of a set of small subunits with …
Eukaryotic proteasomes are unusually large proteins with a heterogeneous subunit composition and have been classified into two isoforms with …
Structural Insights into Substrate Recognition and Processing by the 20S Proteasome.
Sahu I, Glickman MH. Sahu I, et al. Biomolecules. 2021 Jan 24;11(2):148. doi: 10.3390/biom11020148. Biomolecules. 2021. PMID: 33498876 Free PMC article. Review.
Since roughly half of all proteasomes in most eukaryotic cells are free 20S complexes, ubiquitin-independent protein degradation may coexist with ubiquitin-dependent degradation by the highly regulated 26S proteasome. This article reviews recent advances in our understandi …
Since roughly half of all proteasomes in most eukaryotic cells are free 20S complexes, ubiquitin-independent protein degradation may …
9,589 results