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Items: 1 to 20 of 24

1.

Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes.

Lee MJ, Lee BH, Hanna J, King RW, Finley D.

Mol Cell Proteomics. 2011 May;10(5):R110.003871. doi: 10.1074/mcp.R110.003871. Epub 2010 Sep 7. Review.

2.

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
3.

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.

4.

Role of the ubiquitin-proteasome system in brain ischemia: friend or foe?

Caldeira MV, Salazar IL, Curcio M, Canzoniero LM, Duarte CB.

Prog Neurobiol. 2014 Jan;112:50-69. doi: 10.1016/j.pneurobio.2013.10.003. Epub 2013 Oct 22. Review.

PMID:
24157661
5.

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.

6.

Ubiquitin recognition by the proteasome.

Saeki Y.

J Biochem. 2017 Feb 1;161(2):113-124. doi: 10.1093/jb/mvw091. Review.

PMID:
28069863
7.

New insights into the role of the ubiquitin-proteasome pathway in the regulation of apoptosis.

Liu CH, Goldberg AL, Qiu XB.

Chang Gung Med J. 2007 Nov-Dec;30(6):469-79. Review.

8.

Effects of ethanol on the proteasome interacting proteins.

Bardag-Gorce F.

World J Gastroenterol. 2010 Mar 21;16(11):1349-57. Review.

9.

Natural substrates of the proteasome and their recognition by the ubiquitin system.

Ulrich HD.

Curr Top Microbiol Immunol. 2002;268:137-74. Review.

PMID:
12083004
10.

Sperm proteasome and fertilization.

Sutovsky P.

Reproduction. 2011 Jul;142(1):1-14. doi: 10.1530/REP-11-0041. Epub 2011 May 23. Review.

11.

Proteasome-associated proteins: regulation of a proteolytic machine.

Schmidt M, Hanna J, Elsasser S, Finley D.

Biol Chem. 2005 Aug;386(8):725-37. Review.

PMID:
16201867
12.

The potential role of ubiquitin c-terminal hydrolases in oncogenesis.

Fang Y, Fu D, Shen XZ.

Biochim Biophys Acta. 2010 Aug;1806(1):1-6. doi: 10.1016/j.bbcan.2010.03.001. Epub 2010 Mar 17. Review.

PMID:
20302916
13.

The therapeutic potential of deubiquitinating enzyme inhibitors.

Colland F.

Biochem Soc Trans. 2010 Feb;38(Pt 1):137-43. doi: 10.1042/BST0380137. Review.

PMID:
20074048
14.

Deubiquitinating enzymes as cellular regulators.

Kim JH, Park KC, Chung SS, Bang O, Chung CH.

J Biochem. 2003 Jul;134(1):9-18. Review.

15.

Protein partners of deubiquitinating enzymes.

Ventii KH, Wilkinson KD.

Biochem J. 2008 Sep 1;414(2):161-75. doi: 10.1042/BJ20080798. Review.

16.

Emerging mechanistic insights into AAA complexes regulating proteasomal degradation.

Förster F, Schuller JM, Unverdorben P, Aufderheide A.

Biomolecules. 2014 Aug 6;4(3):774-94. doi: 10.3390/biom4030774. Review.

17.

Feeding the machine: mechanisms of proteasome-catalyzed degradation of ubiquitinated proteins.

Crews CM.

Curr Opin Chem Biol. 2003 Oct;7(5):534-9. Review.

PMID:
14580555
18.

A genomic and functional inventory of deubiquitinating enzymes.

Nijman SM, Luna-Vargas MP, Velds A, Brummelkamp TR, Dirac AM, Sixma TK, Bernards R.

Cell. 2005 Dec 2;123(5):773-86. Review.

19.

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.

20.

Power and promise of ubiquitin carboxyl-terminal hydrolase 37 as a target of cancer therapy.

Chen YJ, Ma YS, Fang Y, Wang Y, Fu D, Shen XZ.

Asian Pac J Cancer Prev. 2013;14(4):2173-9. Review.

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