PRE7/YBL041W Literature Guide Help

Other names published for PRE7: PRS3, proteasome core particle subunit beta 6, YBL041W

PRE7 - Substrates/Ligands/Cofactors (20)

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
Mishto M, et al.  (2012) Driving forces of proteasome-catalyzed peptide splicing in yeast and humans. Mol Cell Proteomics 11(10):1008-23
Henderson A, et al.  (2011) Dependence of proteasome processing rate on substrate unfolding. J Biol Chem 286(20):17495-502
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
Archer CT and Kodadek T  (2010) The hydrophobic patch of ubiquitin is required to protect transactivator-promoter complexes from destabilization by the proteasomal ATPases. Nucleic Acids Res 38(3):789-96
Wakata A, et al.  (2010) Simultaneous fluorescent monitoring of proteasomal subunit catalysis. J Am Chem Soc 132(5):1578-82
Baugh JM, et al.  (2009) Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination. J Mol Biol 386(3):814-27
Dimitrova LN, et al.  (2009) Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome. J Biol Chem 284(16):10343-52
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
Prakash S, et al.  (2009) Substrate selection by the proteasome during degradation of protein complexes. Nat Chem Biol 5(1):29-36
Silva GM, et al.  (2008) Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome. FEBS J 275(11):2942-55
Groll M, et al.  (2006) Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome. Structure 14(3):451-6
Groll M, et al.  (2006) Inhibitor-binding mode of homobelactosin C to proteasomes: new insights into class I MHC ligand generation. Proc Natl Acad Sci U S A 103(12):4576-9
Demasi M, et al.  (2003) 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated. J Biol Chem 278(1):679-85
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.  (2001) Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S phase cyclin-Cdk. Mol Cell 8(2):439-48
Groll M, et al.  (1999) The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study. Proc Natl Acad Sci U S A 96(20):10976-83
Loidl G, et al.  (1999) Bivalency as a principle for proteasome inhibition. Proc Natl Acad Sci U S A 96(10):5418-22
Niedermann G, et al.  (1997) Potential immunocompetence of proteolytic fragments produced by proteasomes before evolution of the vertebrate immune system. J Exp Med 186(2):209-20
Fischer M, et al.  (1994) The 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Lett 355(1):69-75