PRE3/YJL001W Literature Guide Help

Other names published for PRE3: CRL21, proteasome core particle subunit beta 1, YJL001W

PRE3 - Non-Fungal Related Genes/Proteins (16)

ReferenceOther Genes Addressed
Dengjel J, et al.  (2012) Identification of autophagosome-associated proteins and regulators by quantitative proteomic analysis and genetic screens. Mol Cell Proteomics 11(3):M111.014035
Huber EM, et al.  (2012) Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity. Cell 148(4):727-38
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
Baugh JM, et al.  (2009) Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination. J Mol Biol 386(3):814-27
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
Prakash S, et al.  (2009) Substrate selection by the proteasome during degradation of protein complexes. Nat Chem Biol 5(1):29-36
Forster A, et al.  (2003) The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation. EMBO J 22(17):4356-64
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
Dahlmann B, et al.  (1999) Identical subunit topographies of human and yeast 20S proteasomes. Arch Biochem Biophys 363(2):296-300
Chervitz SA, et al.  (1998) Comparison of the complete protein sets of worm and yeast: orthology and divergence. Science 282(5396):2022-8
Dick TP, et al.  (1998) Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants. J Biol Chem 273(40):25637-46
Ditzel L, et al.  (1998) Conformational constraints for protein self-cleavage in the proteasome. J Mol Biol 279(5):1187-91
Fu H, et al.  (1998) Molecular organization of the 20S proteasome gene family from Arabidopsis thaliana. Genetics 149(2):677-92
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
Chen P and Hochstrasser M  (1995) Biogenesis, structure and function of the yeast 20S proteasome. EMBO J 14(11):2620-30
Enenkel C, et al.  (1994) PRE3, highly homologous to the human major histocompatibility complex-linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl-peptide hydrolyzing activity. FEBS Lett 341(2-3):193-6