Similar articles for PMID: 19169257

Year	Number of Results
1994	2
1995	3
1996	1
1997	1
1998	1
1999	1
2000	5
2001	1
2002	4
2004	1
2005	8
2006	5
2007	4
2008	5
2009	8
2010	6
2011	7
2012	4
2013	5
2014	10
2015	4
2016	2
2017	4
2018	4
2019	2
2020	3
2021	3
2022	8
2023	3
2024	0

1

Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome.

Bech-Otschir D, Helfrich A, Enenkel C, Consiglieri G, Seeger M, Holzhütter HG, Dahlmann B, Kloetzel PM. Bech-Otschir D, et al. Nat Struct Mol Biol. 2009 Feb;16(2):219-25. doi: 10.1038/nsmb.1547. Epub 2009 Jan 25. Nat Struct Mol Biol. 2009. PMID: 19169257

2

Variably modulated gating of the 26S proteasome by ATP and polyubiquitin.

Li X, Demartino GN. Li X, et al. Biochem J. 2009 Jul 15;421(3):397-404. doi: 10.1042/BJ20090528. Biochem J. 2009. PMID: 19435460 Free PMC article.

3

The Cellular Location of Rad23, a Polyubiquitin Chain-Binding Protein, Plays a Key Role in Its Interaction with Substrates of the Proteasome.

Okeke E, Chen L, Madura K. Okeke E, et al. J Mol Biol. 2020 Mar 27;432(7):2388-2404. doi: 10.1016/j.jmb.2020.03.001. Epub 2020 Mar 6. J Mol Biol. 2020. PMID: 32147457

4

PiZ mouse liver accumulates polyubiquitin conjugates that associate with catalytically active 26S proteasomes.

Haddock CJ, Blomenkamp K, Gautam M, James J, Mielcarska J, Gogol E, Teckman J, Skowyra D. Haddock CJ, et al. PLoS One. 2014 Sep 11;9(9):e106371. doi: 10.1371/journal.pone.0106371. eCollection 2014. PLoS One. 2014. PMID: 25210780 Free PMC article.

5

Inherent asymmetry in the 26S proteasome is defined by the ubiquitin receptor RPN13.

Berko D, Herkon O, Braunstein I, Isakov E, David Y, Ziv T, Navon A, Stanhill A. Berko D, et al. J Biol Chem. 2014 Feb 28;289(9):5609-18. doi: 10.1074/jbc.M113.509380. Epub 2014 Jan 15. J Biol Chem. 2014. PMID: 24429290 Free PMC article.

6

ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins.

Smith DM, Kafri G, Cheng Y, Ng D, Walz T, Goldberg AL. Smith DM, et al. Mol Cell. 2005 Dec 9;20(5):687-98. doi: 10.1016/j.molcel.2005.10.019. Mol Cell. 2005. PMID: 16337593 Free article.

7

Assembly and function of the proteasome.

Saeki Y, Tanaka K. Saeki Y, et al. Methods Mol Biol. 2012;832:315-37. doi: 10.1007/978-1-61779-474-2_22. Methods Mol Biol. 2012. PMID: 22350895 Review.

8

Proteasomes: Isolation and Activity Assays.

Li Y, Tomko RJ Jr, Hochstrasser M. Li Y, et al. Curr Protoc Cell Biol. 2015 Jun 1;67:3.43.1-3.43.20. doi: 10.1002/0471143030.cb0343s67. Curr Protoc Cell Biol. 2015. PMID: 26061243 Free PMC article.

9

The complexity of recognition of ubiquitinated substrates by the 26S proteasome.

Ciechanover A, Stanhill A. Ciechanover A, et al. Biochim Biophys Acta. 2014 Jan;1843(1):86-96. doi: 10.1016/j.bbamcr.2013.07.007. Epub 2013 Jul 18. Biochim Biophys Acta. 2014. PMID: 23872423 Free article. Review.

10

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.

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