PRE3/YJL001W Literature Guide Help

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

PRE3 - Primary Literature (30)

ReferenceOther Genes Addressed
Sukhai MA, et al.  (2013) Lysosomal disruption preferentially targets acute myeloid leukemia cells and progenitors. J Clin Invest 123(1):315-28
Huber EM, et al.  (2012) Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity. Cell 148(4):727-38
Mishto M, et al.  (2012) Driving forces of proteasome-catalyzed peptide splicing in yeast and humans. Mol Cell Proteomics 11(10):1008-23
Silva GM, et al.  (2012) Redox control of 20S proteasome gating. Antioxid Redox Signal 16(11):1183-94
Park S, et al.  (2011) Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress response. J Biol Chem 286(42):36652-66
Collins GA, et al.  (2010) Combined chemical and genetic approach to inhibit proteolysis by the proteasome. Yeast 27(11):965-74
Baugh JM, et al.  (2009) Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination. J Mol Biol 386(3):814-27
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
Laporte D, et al.  (2008) Reversible cytoplasmic localization of the proteasome in quiescent yeast cells. J Cell Biol 181(5):737-45
Hervas-Aguilar A, et al.  (2007) Evidence for the Direct Involvement of the Proteasome in the Proteolytic Processing of the Aspergillus nidulans Zinc Finger Transcription Factor PacC. J Biol Chem 282(48):34735-47
Guerrero C, et al.  (2006) An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network. Mol Cell Proteomics 5(2):366-78
Ramos PC, et al.  (2004) Role of C-terminal extensions of subunits beta2 and beta7 in assembly and activity of eukaryotic proteasomes. J Biol Chem 279(14):14323-30
Podlaska A, et al.  (2003) The link between 20S proteasome activity and post-replication DNA repair in Saccharomyces cerevisiae. Mol Microbiol 49(5):1321-32
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
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
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
Jager S, et al.  (1999) Proteasome beta-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function. J Mol Biol 291(4):997-1013
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
Gueckel R, et al.  (1998) Mutations in the yeast proteasome beta-type subunit Pre3 uncover position-dependent effects on proteasomal peptidase activity and in vivo function. J Biol Chem 273(31):19443-52
Nussbaum AK, et al.  (1998) Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digests of enolase 1. Proc Natl Acad Sci U S A 95(21):12504-9
Ramos PC, et al.  (1998) Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell 92(4):489-99
Arendt CS and Hochstrasser M  (1997) Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation. Proc Natl Acad Sci U S A 94(14):7156-61
Gerlinger UM, et al.  (1997) Yeast cycloheximide-resistant crl mutants are proteasome mutants defective in protein degradation. Mol Biol Cell 8(12):2487-99
Groll M, et al.  (1997) Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386(6624):463-71
Heinemeyer W, et al.  (1997) The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing. J Biol Chem 272(40):25200-9
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
McCusker JH and Haber JE  (1988) Cycloheximide-resistant temperature-sensitive lethal mutations of Saccharomyces cerevisiae. Genetics 119(2):303-15