RPN13/YLR421C Literature Guide Help

Other names published for RPN13: proteasome regulatory particle lid subunit RPN13, YLR421C

RPN13 - Protein-protein Interactions (17)

ReferenceOther Genes Addressed
Enenkel C  (2012) Using Native Gel Electrophoresis and Phosphofluoroimaging to Analyze GFP-Tagged Proteasomes. Methods Mol Biol 832():339-48
Kao A, et al.  (2012) Mapping the structural topology of the yeast 19S proteasomal regulatory particle using chemical cross-linking and probabilistic modeling. Mol Cell Proteomics 11(12):1566-77
Rosenzweig R, et al.  (2012) Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome. J Biol Chem 287(18):14659-71
Gomez TA, et al.  (2011) Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1. BMC Biol 9(1):33
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
Sakata E, et al.  (2011) The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle. Mol Cell 42(5):637-49
Fatimababy AS, et al.  (2010) Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis. FEBS J 277(3):796-816
Voloshin O, et al.  (2010) Tubulin chaperone E binds microtubules and proteasomes and protects against misfolded protein stress. Cell Mol Life Sci 67(12):2025-38
Funakoshi M, et al.  (2009) Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell 137(5):887-99
Saeki Y, et al.  (2009) Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle. Cell 137(5):900-13
Husnjak K, et al.  (2008) Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature 453(7194):481-488
Brandina I, et al.  (2007) tRNA import into yeast mitochondria is regulated by the ubiquitin-proteasome system. FEBS Lett 581(22):4248-54
Kleijnen MF, et al.  (2007) Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites. Nat Struct Mol Biol 14(12):1180-8
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
Lee D, et al.  (2005) The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators. Cell 123(3):423-36
Denison C and Kodadek T  (2004) Toward a general chemical method for rapidly mapping multi-protein complexes. J Proteome Res 3(3):417-25
Verma R, et al.  (2000) Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol Biol Cell 11(10):3425-39