Crossref
journal-article
Elsevier BV
Molecular Cell (78)
References
37
Referenced
136
10.1101/gad.13.16.2148
/ Genes Dev. / The yeast exosome and human PM-Scl are related complexes of 3′ → 5′ exonucleases by Allmang (1999)10.1093/embo-reports/kvf135
/ EMBO Rep. / A complex prediction: three-dimensional model of the yeast exosome by Aloy (2002)10.1038/nature01181
/ Nature / The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila by Andrulis (2002)10.1093/emboj/20.17.4684
/ EMBO J. / Ski7p G protein interacts with the exosome and the Ski complex for 3′-to-5′ mRNA decay in yeast by Araki (2001)10.1126/science.289.5481.905
/ Science / The complete atomic structure of the large ribosomal subunit at 2.4 A resolution by Ban (2000)10.1017/S1355838200991787
/ RNA / The yeast antiviral proteins Ski2p, Ski3p, and Ski8p exist as a complex in vivo by Brown (2000)10.1107/S0907444998003254
/ Acta Crystallogr. D Biol. Crystallogr. / Crystallography & NMR system: A new software suite for macromolecular structure determination by Brunger (1998)10.1016/S0962-8924(01)02225-5
/ Trends Cell Biol. / The yin and yang of the exosome by Butler (2002)10.1093/nar/30.3.695
/ Nucleic Acids Res. / Arabidopsis thaliana exosome subunit AtRrp4p is a hydrolytic 3′→5′ exonuclease containing S1 and KH RNA-binding domains by Chekanova (2002)10.1093/emboj/20.14.3831
/ EMBO J. / The exosome of Trypanosoma brucei by Estevez (2001)10.1074/jbc.M305333200
/ J. Biol. Chem. / The roles of intersubunit interactions in exosome stability by Estevez (2003)10.1038/sj.embor.embor929
/ EMBO Rep. / An exosome-like complex in Sulfolobus solfataricus by Evguenieva-Hackenberg (2003)10.1074/mcp.M500171-MCP200
/ Mol. Cell Proteomics / Protein complexes in the archaeon methanothermobacter thermautotrophicus analyzed by blue native/SDS-PAGE and mass spectrometry by Farhoud (2005)10.1038/35097110
/ Nature / Quality control of mRNA 3′-end processing is linked to the nuclear exosome by Hilleren (2001)10.1016/0022-2836(70)90199-3
/ J. Mol. Biol. / Conformation of polyribouridylic acid in solution by Inners (1970)10.1107/S0021889893005588
/ J. Appl. Crystallogr. / Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants by Kabsch (1993)10.1101/gr.162001
/ Genome Res. / Prediction of the archaeal exosome and its connections with the proteasome and the translation and transcription machineries by a comparative-genomic approach by Koonin (2001)10.1016/j.cell.2005.04.029
/ Cell / RNA degradation by the exosome is promoted by a nuclear polyadenylation complex by LaCava (2005)10.1016/j.cub.2004.09.044
/ Curr. Biol. / Structural biochemistry of ATP-driven dimerization and DNA-stimulated activation of SMC ATPases by Lammens (2004)10.1038/nsmb952
/ Nat. Struct. Mol. Biol. / The archaeal exosome core is a hexameric ring structure with three catalytic subunits by Lorentzen (2005)10.1038/82817
/ Nat. Struct. Biol. / Musing on the structural organization of the exosome complex by Mitchell (2000)10.1016/S0092-8674(00)80432-8
/ Cell / The exosome: a conserved eukaryotic RNA processing complex containing multiple 3′→5′ exoribonucleases by Mitchell (1997)10.1261/rna.7231505
/ RNA / Decay of mRNAs targeted by RISC requires XRN1, the Ski complex, and the exosome by Orban (2005)10.1016/S0022-2836(02)00947-6
/ J. Mol. Biol. / Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring by Raijmakers (2002)10.1006/jmbi.2001.5265
/ J. Mol. Biol. / Protein-protein interactions of hCsl4p with other human exosome subunits by Raijmakers (2002)10.1078/0171-9335-00385
/ Eur. J. Cell Biol. / The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm by Raijmakers (2004)10.1107/S0907444902011678
/ Acta Crystallogr. D Biol. Crystallogr. / Substructure solution with SHELXD by Schneider (2002)10.1016/j.sbi.2004.10.006
/ Curr. Opin. Struct. Biol. / The polynucleotide ligase and RNA capping enzyme superfamily of covalent nucleotidyltransferases by Shuman (2004)10.1016/S0969-2126(00)00521-9
/ Struct. Fold. Des. / A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation by Symmons (2000)10.1016/S0968-0004(01)01999-5
/ Trends Biochem. Sci. / Running rings around RNA: a superfamily of phosphate-dependent RNases by Symmons (2002)10.1107/S0108767302087378
/ Acta Crystallogr. / Automated structure solution, density modification and model building by Terwilliger (2002)- Turk, D. (1992). Weiterentwicklung eines Programms fuer Molekuelgraphik und Elektrondichte-Manipulation und seine Anwendung auf verschiedene Protein-Strukturaufklaerungen. PhD thesis, Technical University, Munich, Germany.
10.1016/S0092-8674(00)81520-2
/ Cell / The exosome: a proteasome for RNA? by van Hoof (1999)10.1128/MCB.20.21.8230-8243.2000
/ Mol. Cell. Biol. / Function of the ski4p (Csl4p) and Ski7p proteins in 3′-to-5′ degradation of mRNA by van Hoof (2000)10.1016/S0955-0674(03)00051-6
/ Curr. Opin. Cell Biol. / Nuclear mRNA surveillance by Vasudevan (2003)10.1110/ps.04864904
/ Protein Sci. / Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8 by Wang (2004)10.1016/j.cell.2005.04.030
/ Cell / Cryptic pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase by Wyers (2005)
Dates
Type | When |
---|---|
Created | 19 years, 9 months ago (Nov. 11, 2005, 7:14 a.m.) |
Deposited | 1 year, 3 months ago (May 11, 2024, 3:02 a.m.) |
Indexed | 1 month, 2 weeks ago (July 1, 2025, 3:17 p.m.) |
Issued | 19 years, 9 months ago (Nov. 1, 2005) |
Published | 19 years, 9 months ago (Nov. 1, 2005) |
Published Print | 19 years, 9 months ago (Nov. 1, 2005) |
Funders
2
European Molecular Biology Organization
10.13039/100004410
Region: Europe
pri (International organizations)
Labels
2
- The European Molecular Biology Organization
- EMBO
Deutsche Forschungsgemeinschaft
10.13039/501100001659
Region: Europe
gov (National government)
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3
- German Research Association
- German Research Foundation
- DFG