RPN10/YHR200W Literature Guide Help

Other names published for RPN10: MCB1, SUN1, proteasome regulatory particle base subunit RPN10, YHR200W

RPN10 - Protein Physical Properties (13)

ReferenceOther Genes Addressed
Keren-Kaplan T and Prag G  (2012) Purification and crystallization of mono-ubiquitylated ubiquitin receptor Rpn10. Acta Crystallogr Sect F Struct Biol Cryst Commun 68(Pt 9):1120-3
Henderson A, et al.  (2011) Dependence of proteasome processing rate on substrate unfolding. J Biol Chem 286(20):17495-502
Chandra A, et al.  (2010) Synthetic lethality of rpn11-1 rpn10Delta is linked to altered proteasome assembly and activity. Curr Genet 56(6):543-57
Isasa M, et al.  (2010) Monoubiquitination of RPN10 regulates substrate recruitment to the proteasome. Mol Cell 38(5):733-45
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
Prakash S, et al.  (2009) Substrate selection by the proteasome during degradation of protein complexes. Nat Chem Biol 5(1):29-36
Zhang D, et al.  (2009) Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor. Mol Cell 36(6):1018-33
Smith DM, et al.  (2007) Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry. Mol Cell 27(5):731-44
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
Braun BC, et al.  (1999) The base of the proteasome regulatory particle exhibits chaperone-like activity. Nat Cell Biol 1(4):221-6
Loidl G, et al.  (1999) Bivalency as a principle for proteasome inhibition. Proc Natl Acad Sci U S A 96(10):5418-22
Kominami K, et al.  (1997) Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1. Mol Biol Cell 8(1):171-87
van Nocker S, et al.  (1996) The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol Cell Biol 16(11):6020-8