RPN13/YLR421C Literature Guide Help

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

RPN13 - Non-Fungal Related Genes/Proteins (10)

ReferenceOther Genes Addressed
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
White RR, et al.  (2011) Characterisation of the Trichinella spiralis Deubiquitinating Enzyme, TsUCH37, an Evolutionarily Conserved Proteasome Interaction Partner. PLoS Negl Trop Dis 5(10):e1340
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
Bech-Otschir D, et al.  (2009) Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome. Nat Struct Mol Biol 16(2):219-25
Husnjak K, et al.  (2008) Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature 453(7194):481-488
Hamazaki J, et al.  (2006) A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes. EMBO J 25(19):4524-36
Jorgensen JP, et al.  (2006) Adrm1, a putative cell adhesion regulating protein, is a novel proteasome-associated factor. J Mol Biol 360(5):1043-52
Qiu XB, et al.  (2006) hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37. EMBO J 25(24):5742-53
Yao T, et al.  (2006) Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Nat Cell Biol 8(9):994-1002
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