Crossref
journal-article
Elsevier BV
Biochemical and Biophysical Research Communications (78)
References
34
Referenced
28
10.1146/annurev.biochem.68.1.1015
/ Annu. Rev. Biochem. / The 26S proteasome: a molecular machine designed for controlled proteolysis by Voges (1999)10.1038/80384
/ Nat. Med. / Basic medical research award. The ubiquitin system by Hershko (2000)10.1126/science.7725097
/ Science / Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution by Lowe (1995)10.1038/386463a0
/ Nature / Structure of 20S proteasome from yeast at 2.4 A resolution by Groll (1997)10.1038/nature10774
/ Nature / Complete subunit architecture of the proteasome regulatory particle by Lander (2012)10.1073/pnas.1120559109
/ Proc. Natl. Acad. Sci. USA / Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach by Lasker (2012)10.1073/pnas.1213333109
/ Proc. Natl. Acad. Sci. USA / Near-atomic resolution structural model of the yeast 26S proteasome by Beck (2012)10.1074/jbc.M403165200
/ J. Biol. Chem. / Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae by Sone (2004)10.1242/jcs.01575
/ J. Cell Sci. / Sem1, the yeast ortholog of a human BRCA2-binding protein, is a component of the proteasome regulatory particle that enhances proteasome stability by Funakoshi (2004)10.1016/j.molcel.2011.04.021
/ Mol. Cell / The catalytic activity of ubp6 enhances maturation of the proteasomal regulatory particle by Sakata (2011)10.1371/journal.pbio.0040267
/ PLoS Biol. / Structural organization of the 19S proteasome lid: insights from MS of intact complexes by Sharon (2006)10.1016/j.bbrc.2010.05.061
/ Biochem. Biophys. Res. Commun. / Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae by Fukunaga (2010)10.1016/j.molcel.2011.11.020
/ Mol. Cell / Incorporation of the Rpn12 subunit couples completion of proteasome regulatory particle lid assembly to lid-base joining by Tomko (2011)10.1016/j.molcel.2004.11.033
/ Mol. Cell / Proteasome involvement in the repair of DNA double-strand breaks by Krogan (2004)10.1128/MCB.19.7.4633
/ Mol. Cell. Biol. / Interaction between the product of the breast cancer susceptibility gene BRCA2 and DSS1, a protein functionally conserved from yeast to mammals by Marston (1999)10.1083/jcb.200810059
/ J. Cell Biol. / Sem1 is a functional component of the nuclear pore complex-associated messenger RNA export machinery by Faza (2009)10.1016/j.molcel.2008.11.012
/ Mol. Cell / A genetic interaction map of RNA-processing factors reveals links between Sem1/Dss1-containing complexes and mRNA export and splicing by Wilmes (2008)10.1128/MCB.01188-10
/ Mol. Cell. Biol. / New suppressors of THO mutations identify Thp3 (Ypr045c)–Csn12 as a protein complex involved in transcription elongation by Jimeno (2011)10.1093/hmg/5.5.571
/ Hum. Mol. Genet. / Characterization of the split hand/split foot malformation locus SHFM1 at 7q21.3–q22.1 and analysis of a candidate gene for its expression during limb development by Crackower (1996)10.1126/science.297.5588.1837
/ Science / BRCA2 function in DNA binding and recombination from a BRCA2–DSS1–ssDNA structure by Yang (2002)10.1038/nsmb.2235
/ Nat. Struct. Mol. Biol. / Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex by Ellisdon (2012)10.1016/j.cell.2009.05.005
/ Cell / Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle by Saeki (2009)10.1073/pnas.1119394109
/ Proc. Natl. Acad. Sci. USA / Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy by Sakata (2012)10.1016/j.jsb.2011.06.003
/ J. Struct. Biol. / Computer controlled cryo-electron microscopy–TOM(2) a software package for high-throughput applications by Korinek (2011)10.1016/j.jsb.2004.10.006
/ J. Struct. Biol. / TOM software toolbox: acquisition and analysis for electron tomography by Nickell (2005){'key': '10.1016/j.bbrc.2013.04.069_b0130', 'first-page': '1', 'article-title': 'Automated particle picking based on correlation Peak shape analysis and Iterative classification', 'volume': '6', 'author': 'Hrabe', 'year': '2012', 'journal-title': 'Int. J. Med. Biol. Sci.'}
/ Int. J. Med. Biol. Sci. / Automated particle picking based on correlation Peak shape analysis and Iterative classification by Hrabe (2012)10.1038/nprot.2008.62
/ Nat. Protoc. / Image processing for electron microscopy single-particle analysis using XMIPP by Scheres (2008)10.1073/pnas.1117648108
/ Proc. Natl. Acad. Sci. USA / The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together by Pathare (2012)10.1016/S0959-440X(99)00057-3
/ Curr. Opin. Struct. Biol. / Winged helix proteins by Gajiwala (2000)10.1074/mcp.M112.018374
/ Mol. Cell. Proteomics / Mapping the structural topology of the yeast 19S proteasomal regulatory particle using chemical cross-linking and probabilistic modeling by Kao (2012)10.1074/mcp.R000001-MCP201
/ Mol. Cell. Proteomics / Probing native protein structures by chemical cross-linking, mass spectrometry and bioinformatics by Leitner (2010)10.1016/j.jmb.2008.08.044
/ J. Mol. Biol. / Identification of a specific motif of the DSS1 protein required for proteasome interaction and p53 protein degradation by Wei (2008)10.4161/nucl.1.1.10424
/ Nucleus / Sem1: a versatile “molecular glue”? by Faza (2010)10.1002/prot.20921
/ Proteins / MUSTANG: a multiple structural alignment algorithm by Konagurthu (2006)
Dates
Type | When |
---|---|
Created | 12 years, 4 months ago (April 30, 2013, 8:42 p.m.) |
Deposited | 6 years, 1 month ago (July 12, 2019, 11:04 p.m.) |
Indexed | 1 year, 2 months ago (June 18, 2024, 2:29 a.m.) |
Issued | 12 years, 4 months ago (May 1, 2013) |
Published | 12 years, 4 months ago (May 1, 2013) |
Published Print | 12 years, 4 months ago (May 1, 2013) |
@article{Bohn_2013, title={Localization of the regulatory particle subunit Sem1 in the 26S proteasome}, volume={435}, ISSN={0006-291X}, url={http://dx.doi.org/10.1016/j.bbrc.2013.04.069}, DOI={10.1016/j.bbrc.2013.04.069}, number={2}, journal={Biochemical and Biophysical Research Communications}, publisher={Elsevier BV}, author={Bohn, Stefan and Sakata, Eri and Beck, Florian and Pathare, Ganesh R. and Schnitger, Jérôme and Nágy, Istvan and Baumeister, Wolfgang and Förster, Friedrich}, year={2013}, month=may, pages={250–254} }