SEM1/YDR363W-A Literature Guide Help

Other names published for SEM1: DSS1, HOD1, proteasome regulatory particle lid subunit SEM1, YDR363W-A

SEM1 - Protein-protein Interactions (23)

ReferenceOther Genes Addressed
Ellisdon AM, et al.  (2012) Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex.LID - 10.1038/nsmb.2235 [doi] Nat Struct Mol Biol ()
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
Lander GC, et al.  (2012) Complete subunit architecture of the proteasome regulatory particle.LID - 10.1038/nature10774 [doi] Nature ()
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
Tomko RJ Jr and Hochstrasser M  (2011) Incorporation of the Rpn12 subunit couples completion of proteasome regulatory particle lid assembly to lid-base joining. Mol Cell 44(6):907-17
Fukunaga K, et al.  (2010) Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae. Biochem Biophys Res Commun 396(4):1048-53
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
Faza MB, et al.  (2009) Sem1 is a functional component of the nuclear pore complex-associated messenger RNA export machinery. J Cell Biol 184(6):833-46
Funakoshi M, et al.  (2009) Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell 137(5):887-99
Le Tallec B, et al.  (2009) Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome. Mol Cell 33(3):389-99
Saeki Y, et al.  (2009) Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle. Cell 137(5):900-13
Taverner T, et al.  (2008) Subunit architecture of intact protein complexes from mass spectrometry and homology modeling. Acc Chem Res 41(5):617-27
Wilmes GM, et al.  (2008) A genetic interaction map of RNA-processing factors reveals links between Sem1/Dss1-containing complexes and mRNA export and splicing. Mol Cell 32(5):735-46
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
Sharon M, et al.  (2006) Structural organization of the 19S proteasome lid: insights from MS of intact complexes. PLoS Biol 4(8):e267
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
Funakoshi M, et al.  (2004) Sem1, the yeast ortholog of a human BRCA2-binding protein, is a component of the proteasome regulatory particle that enhances proteasome stability. J Cell Sci 117(Pt 26):6447-54
Krogan NJ, et al.  (2004) Proteasome involvement in the repair of DNA double-strand breaks. Mol Cell 16(6):1027-34
Sone T, et al.  (2004) Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae. J Biol Chem 279(27):28807-16