RPN13/YLR421C Literature Guide Help

Other names published for RPN13: proteasome regulatory particle lid subunit RPN13, YLR421C

RPN13 - Substrates/Ligands/Cofactors (11)

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
Sakata E, et al.  (2012) Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy. Proc Natl Acad Sci U S A 109(5):1479-84
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
Fatimababy AS, et al.  (2010) Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis. FEBS J 277(3):796-816
Nixon CE, et al.  (2010) Degradation of the Saccharomyces cerevisiae mating-type regulator alpha1: genetic dissection of cis-determinants and trans-acting pathways. Genetics 185(2):497-511
Peth A, et al.  (2010) ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation. Mol Cell 40(4):671-81
Seong KM, et al.  (2007) Rpn13p and Rpn14p are involved in the recognition of ubiquitinated Gcn4p by the 26S proteasome. FEBS Lett 581(13):2567-73
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
Fischer M, et al.  (1994) The 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Lett 355(1):69-75