PRE2/YPR103W Literature Guide Help

Other names published for PRE2: DOA3, PRG1, SRR2, proteasome core particle subunit beta 5, YPR103W

PRE2 - Protein Physical Properties (14)

ReferenceOther Genes Addressed
Huber EM, et al.  (2012) Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity. Cell 148(4):727-38
Silva GM, et al.  (2012) Redox control of 20S proteasome gating. Antioxid Redox Signal 16(11):1183-94
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
Groll M, et al.  (2009) Snapshots of the fluorosalinosporamide/20S complex offer mechanistic insights for fine tuning proteasome inhibition. J Med Chem 52(17):5420-8
Osmulski PA, et al.  (2009) A tetrahedral transition state at the active sites of the 20S proteasome is coupled to opening of the alpha-ring channel. Structure 17(8):1137-47
Prakash S, et al.  (2009) Substrate selection by the proteasome during degradation of protein complexes. Nat Chem Biol 5(1):29-36
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
Whitby FG, et al.  (2000) Structural basis for the activation of 20S proteasomes by 11S regulators. Nature 408(6808):115-20
Arendt CS and Hochstrasser M  (1999) Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly. EMBO J 18(13):3575-85
Loidl G, et al.  (1999) Bivalency as a principle for proteasome inhibition. Proc Natl Acad Sci U S A 96(10):5418-22
Chen P and Hochstrasser M  (1996) Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell 86(6):961-72
Heinemeyer W, et al.  (1993) PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins. J Biol Chem 268(7):5115-20