RPN10/YHR200W Literature Guide Help

Other names published for RPN10: MCB1, SUN1, proteasome regulatory particle base subunit RPN10, YHR200W

RPN10 - Techniques and Reagents (23)

ReferenceOther Genes Addressed
Enenkel C  (2012) Using Native Gel Electrophoresis and Phosphofluoroimaging to Analyze GFP-Tagged Proteasomes. Methods Mol Biol 832():339-48
Henderson A, et al.  (2011) Dependence of proteasome processing rate on substrate unfolding. J Biol Chem 286(20):17495-502
Keren-Kaplan T, et al.  (2011) Synthetic biology approach to reconstituting the ubiquitylation cascade in bacteria. EMBO J 31(2):378-90
Sakata E, et al.  (2011) The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle. Mol Cell 42(5):637-49
Wu S, et al.  (2011) An integrated top-down and bottom-up strategy for characterization of protein isoforms and modifications. Methods Mol Biol 694():291-304
Peth A, et al.  (2010) ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation. Mol Cell 40(4):671-81
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
Prakash S, et al.  (2009) Substrate selection by the proteasome during degradation of protein complexes. Nat Chem Biol 5(1):29-36
Gaczynska M and Osmulski PA  (2008) Atomic force microscopy as a tool to study the proteasome assemblies. Methods Cell Biol 90():39-60
Guerrero C, et al.  (2008) Characterization of the proteasome interaction network using a QTAX-based tag-team strategy and protein interaction network analysis. Proc Natl Acad Sci U S A 105(36):13333-8
Liu C, et al.  (2007) Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells. Biotechniques 42(2):158, 160, 162
Romero-Perez L, et al.  (2007) Sts1 can overcome the loss of Rad23 and Rpn10 and represents a novel regulator of the ubiquitin/proteasome pathway. J Biol Chem 282(49):35574-82
Freimoser FM, et al.  (2006) Systematic screening of polyphosphate (poly P) levels in yeast mutant cells reveals strong interdependence with primary metabolism. Genome Biol 7(11):R109
Babbitt SE, et al.  (2005) ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle. Cell 121(4):553-65
Leggett DS, et al.  (2005) Purification of proteasomes, proteasome subcomplexes, and proteasome-associated proteins from budding yeast. Methods Mol Biol 301:57-70
Mayor T, et al.  (2005) Analysis of polyubiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets. Mol Cell Proteomics 4(6):741-51
Saeki Y, et al.  (2005) Knocking out Ubiquitin Proteasome System Function In Vivo and In Vitro with Genetically Encodable Tandem Ubiquitin. Methods Enzymol 399:64-74
Denison C and Kodadek T  (2004) Toward a general chemical method for rapidly mapping multi-protein complexes. J Proteome Res 3(3):417-25
Fujimuro M, et al.  (1998) Growth-dependent change of the 26S proteasome in budding yeast. Biochem Biophys Res Commun 251(3):818-23
Fujimuro M, et al.  (1998) Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Lett 423(2):149-54
Glickman MH, et al.  (1998) The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol 18(6):3149-62
van Nocker S, et al.  (1996) The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol Cell Biol 16(11):6020-8
Fischer M, et al.  (1994) The 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Lett 355(1):69-75