title: The proteasome and the degradation of oxidized proteins: Part I-structure of proteasomes.
abstract: The main machinery responsible for cellular protein maintenance is the ubiquitin-proteasomal system, with its core particle the 20S proteasome. The main task of the system is a fast and efficient degradation of proteins not needed anymore in cellular metabolism. For this aim a complex system of regulators evolved, modifying the function of the 20S core proteasome. Here we summarize shortly the structure of the 20S proteasome as well as its associated regulator proteins.
authors.affiliation: Department of Nutritional Toxicology, Institute of Nutrition, Friedrich Schiller University Jena, Dornburger Str. 24, 07743 Jena, Germany.
authors.forename: Tobias
authors.initials: T
authors.lastname: Jung
authors.forename: Tilman
authors.initials: T
authors.lastname: Grune
mesh_terms: D000818:Animals; D006801:Humans; D010084:Oxidation-Reduction; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry* / Q000378:metabolism*; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D011506:Proteins; D046988:Proteasome Endopeptidase Complex
keywords: 20S proteasome; 26S proteasome; Proteasomal regulators
references.citation: Biochem Biophys Res Commun. 1989 Mar 31;159(3):1309-15
references.pmid: 2649098
references.citation: Mol Cell. 2007 Sep 7;27(5):731-44
references.pmid: 17803938
references.citation: J Neuroimmunol. 2003 Feb;135(1-2):135-40
references.pmid: 12576233
references.citation: EMBO J. 2002 Jul 1;21(13):3516-25
references.pmid: 12093752
references.citation: Metab Eng. 2003 Jul;5(3):151-63
references.pmid: 12948749
references.citation: J Biol Chem. 1994 Aug 19;269(33):20878-84
references.pmid: 8063704
references.citation: Semin Cell Dev Biol. 2007 Dec;18(6):780-91
references.pmid: 17942349
references.citation: J Biol Chem. 2008 Jan 4;283(1):66-75
references.pmid: 17965458
references.citation: Curr Opin Microbiol. 2005 Dec;8(6):720-8
references.pmid: 16256423
references.citation: Mol Cell. 2008 May 9;30(3):360-8
references.pmid: 18471981
references.citation: EMBO J. 2011 Jul 08;30(15):3065-77
references.pmid: 21743439
references.citation: EMBO J. 2000 Jan 4;19(1):94-102
references.pmid: 10619848
references.citation: Mol Cell. 2001 Jun;7(6):1143-52
references.pmid: 11430818
references.citation: J Biol Chem. 2002 Jul 26;277(30):26815-20
references.pmid: 12011044
references.citation: Radiat Res. 2007 Jun;167(6):663-74
references.pmid: 17523843
references.citation: Nat Struct Biol. 2000 Nov;7(11):1062-7
references.pmid: 11062564
references.citation: Curr Biol. 2003 Jul 1;13(13):1140-4
references.pmid: 12842014
references.citation: Mol Aspects Med. 2009 Aug;30(4):191-296
references.pmid: 19371762
references.citation: Arch Biochem Biophys. 1996 May 1;329(1):87-96
references.pmid: 8619639
references.citation: Exp Biol Med (Maywood). 2010 Mar;235(3):278-89
references.pmid: 20404045
references.citation: Mol Cell Biol. 2006 Apr;26(8):2999-3007
references.pmid: 16581775
references.citation: FEBS Lett. 2006 Jul 10;580(16):3989-94
references.pmid: 16806194
references.citation: Biochim Biophys Acta. 2004 Nov 29;1695(1-3):33-44
references.pmid: 15571807
references.citation: Ital J Biochem. 1992 Jul-Aug;41(4):213-24
references.pmid: 1428780
references.citation: J Biochem. 2000 Jun;127(6):941-3
references.pmid: 10833260
references.citation: Biochim Biophys Acta. 2012 Jan;1823(1):67-82
references.pmid: 21820014
references.citation: Mol Cell. 2003 Jan;11(1):69-78
references.pmid: 12535522
references.citation: J Biol Chem. 2000 May 12;275(19):14336-45
references.pmid: 10799514
references.citation: Curr Protein Pept Sci. 2004 Jun;5(3):153-61
references.pmid: 15180520
references.citation: J Lab Clin Med. 2000 Apr;135(4):324-31
references.pmid: 10779048