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Items: 20

1.

ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation.

Peth A, Uchiki T, Goldberg AL.

Mol Cell. 2010 Nov 24;40(4):671-81. doi: 10.1016/j.molcel.2010.11.002.

2.

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

Ciechanover A, Stanhill A.

Biochim Biophys Acta. 2014 Jan;1843(1):86-96. doi: 10.1016/j.bbamcr.2013.07.007. Epub 2013 Jul 18. Review.

3.

Deubiquitinating enzymes are IN/(trinsic to proteasome function).

Guterman A, Glickman MH.

Curr Protein Pept Sci. 2004 Jun;5(3):201-11. Review.

PMID:
15188770
4.

Design principles of a universal protein degradation machine.

Matyskiela ME, Martin A.

J Mol Biol. 2013 Jan 23;425(2):199-213. doi: 10.1016/j.jmb.2012.11.001. Epub 2012 Nov 9. Review.

5.

Assembly and function of the proteasome.

Saeki Y, Tanaka K.

Methods Mol Biol. 2012;832:315-37. doi: 10.1007/978-1-61779-474-2_22. Review.

PMID:
22350895
6.

Recognition and processing of ubiquitin-protein conjugates by the proteasome.

Finley D.

Annu Rev Biochem. 2009;78:477-513. doi: 10.1146/annurev.biochem.78.081507.101607. Review.

7.

Structure characterization of the 26S proteasome.

Kim HM, Yu Y, Cheng Y.

Biochim Biophys Acta. 2011 Feb;1809(2):67-79. doi: 10.1016/j.bbagrm.2010.08.008. Epub 2010 Aug 26. Review.

8.

Ubiquitin-binding domains.

Hurley JH, Lee S, Prag G.

Biochem J. 2006 Nov 1;399(3):361-72. Review.

9.

Proteasome activators.

Stadtmueller BM, Hill CP.

Mol Cell. 2011 Jan 7;41(1):8-19. doi: 10.1016/j.molcel.2010.12.020. Review.

10.

Biological significance of co- and post-translational modifications of the yeast 26S proteasome.

Hirano H, Kimura Y, Kimura A.

J Proteomics. 2016 Feb 16;134:37-46. doi: 10.1016/j.jprot.2015.11.016. Epub 2015 Nov 28. Review.

PMID:
26642761
11.

The recognition of ubiquitinated proteins by the proteasome.

Grice GL, Nathan JA.

Cell Mol Life Sci. 2016 Sep;73(18):3497-506. doi: 10.1007/s00018-016-2255-5. Epub 2016 May 2. Review.

12.

Dissecting the ubiquitin pathway by mass spectrometry.

Xu P, Peng J.

Biochim Biophys Acta. 2006 Dec;1764(12):1940-7. Epub 2006 Sep 14. Review.

13.

Properties of natural and artificial proteins displaying multiple ubiquitin-binding domains.

Lopitz-Otsoa F, Rodríguez MS, Aillet F.

Biochem Soc Trans. 2010 Feb;38(Pt 1):40-5. doi: 10.1042/BST0380040. Review.

PMID:
20074032
14.

Ubiquitin system: JAMMing in the name of the lid.

Berndt C, Bech-Otschir D, Dubiel W, Seeger M.

Curr Biol. 2002 Dec 10;12(23):R815-7. Review.

15.

The evolving world of ubiquitin: transformed polyubiquitin chains.

Morimoto D, Shirakawa M.

Biomol Concepts. 2016 Jun 1;7(3):157-67. doi: 10.1515/bmc-2016-0009. Review.

PMID:
27226101
16.

Protein targeting to ATP-dependent proteases.

Inobe T, Matouschek A.

Curr Opin Struct Biol. 2008 Feb;18(1):43-51. doi: 10.1016/j.sbi.2007.12.014. Epub 2008 Feb 13. Review.

17.

[Structural biology of ubiquitin and ubiquitin binding domain/motif].

Kenichiro F, Hidehito T.

Tanpakushitsu Kakusan Koso. 2004 May;49(7 Suppl):1042-3. Review. Japanese. No abstract available.

PMID:
15168522
18.

Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy.

Goldberg AL.

Biochem Soc Trans. 2007 Feb;35(Pt 1):12-7. Review.

PMID:
17212580
19.

Gates, Channels, and Switches: Elements of the Proteasome Machine.

Finley D, Chen X, Walters KJ.

Trends Biochem Sci. 2016 Jan;41(1):77-93. doi: 10.1016/j.tibs.2015.10.009. Epub 2015 Nov 28. Review.

20.

[Roles and action mechanisms of two ubiquitin-like conjugation systems in autophagy].

Nakatogawa H.

Seikagaku. 2014 Aug;86(4):441-51. Review. Japanese. No abstract available.

PMID:
25255626

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