RPN11/YFR004W Literature Guide Help

Other names published for RPN11: MPR1, proteasome regulatory particle lid subunit RPN11, YFR004W

RPN11 - Substrates/Ligands/Cofactors (9)

ReferenceOther Genes Addressed
Ha SW, et al.  (2012) The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits. Biochem Biophys Res Commun 419(2):226-31
Lander GC, et al.  (2012) Complete subunit architecture of the proteasome regulatory particle.LID - 10.1038/nature10774 [doi] Nature ()
Henderson A, et al.  (2011) Dependence of proteasome processing rate on substrate unfolding. J Biol Chem 286(20):17495-502
Inobe T, et al.  (2011) Defining the geometry of the two-component proteasome degron. Nat Chem Biol 7(3):161-7
Kraut DA and Matouschek A  (2011) Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization. ACS Chem Biol 6(10):1087-95
Schaefer JB and Morgan DO  (2011) Protein-linked ubiquitin chain structure restricts activity of deubiquitinating enzymes. J Biol Chem 286(52):45186-96
Guterman A and Glickman MH  (2004) Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome. J Biol Chem 279(3):1729-38
Gaczynska M, et al.  (2003) Proline- and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity. Biochemistry 42(29):8663-70
Verma R, et al.  (2002) Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298(5593):611-5