Primary Literature
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- Gomar-Alba M, et al. (2022) Nuclear pore complex acetylation regulates mRNA export and cell cycle commitment in budding yeast. EMBO J 41(15):e110271 PMID: 35735140
- Whale AJ, et al. (2022) Stimulation of adaptive gene amplification by origin firing under replication fork constraint. Nucleic Acids Res 50(2):915-936 PMID: 35018465
- Bharati AP, et al. (2020) An insight into structural plasticity and conformational transitions of transcriptional co-activator Sus1. PLoS One 15(3):e0229216 PMID: 32134955
- Stewart M (2019) Structure and Function of the TREX-2 Complex. Subcell Biochem 93:461-470 PMID: 31939161
- Xie Y and Ren Y (2019) Mechanisms of nuclear mRNA export: A structural perspective. Traffic 20(11):829-840 PMID: 31513326
- Aibara S, et al. (2016) The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. J Struct Biol 195(3):316-324 PMID: 27422657
- Eshleman N, et al. (2016) Defects in THO/TREX-2 function cause accumulation of novel cytoplasmic mRNP granules that can be cleared by autophagy. RNA 22(8):1200-14 PMID: 27251550
- Dimitrova L, et al. (2015) Structural Characterization of the Chaetomium thermophilum TREX-2 Complex and its Interaction with the mRNA Nuclear Export Factor Mex67:Mtr2. Structure 23(7):1246-57 PMID: 26051714
- Schneider M, et al. (2015) The Nuclear Pore-Associated TREX-2 Complex Employs Mediator to Regulate Gene Expression. Cell 162(5):1016-28 PMID: 26317468
- Valkov E and Stewart M (2015) 1.25\u2005Å resolution structure of an RNA 20-mer that binds to the TREX2 complex. Acta Crystallogr F Struct Biol Commun 71(Pt 10):1318-21 PMID: 26457524
- Santos-Pereira JM, et al. (2014) A genome-wide function of THSC/TREX-2 at active genes prevents transcription-replication collisions. Nucleic Acids Res 42(19):12000-14 PMID: 25294824
- Ellisdon AM and Stewart M (2012) Structural biology of the PCI-protein fold. Bioarchitecture 2(4):118-23 PMID: 22960705
- Ellisdon AM, et al. (2012) Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex. Nat Struct Mol Biol 19(3):328-36 PMID: 22343721
- Jani D, et al. (2012) Functional and structural characterization of the mammalian TREX-2 complex that links transcription with nuclear messenger RNA export. Nucleic Acids Res 40(10):4562-73 PMID: 22307388
- Valkov E, et al. (2012) Structural basis for the assembly and disassembly of mRNA nuclear export complexes. Biochim Biophys Acta 1819(6):578-92 PMID: 22406340
- Cuenca-Bono B, et al. (2011) SUS1 introns are required for efficient mRNA nuclear export in yeast. Nucleic Acids Res 39(19):8599-611 PMID: 21749979
- Ellisdon AM, et al. (2010) Structural basis for the interaction between yeast Spt-Ada-Gcn5 acetyltransferase (SAGA) complex components Sgf11 and Sus1. J Biol Chem 285(6):3850-3856 PMID: 20007317
- Faza MB, et al. (2010) Sem1: a versatile "molecular glue"? Nucleus 1(1):12-7 PMID: 21327099
- Lu Q, et al. (2010) Arabidopsis homolog of the yeast TREX-2 mRNA export complex: components and anchoring nucleoporin. Plant J 61(2):259-70 PMID: 19843313
- Wickramasinghe VO, et al. (2010) GANP enhances the efficiency of mRNA nuclear export in mammalian cells. Nucleus 1(5):393-6 PMID: 21326821
- 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 PMID: 19289793
- Skruzný M, et al. (2009) An endoribonuclease functionally linked to perinuclear mRNP quality control associates with the nuclear pore complexes. PLoS Biol 7(1):e8 PMID: 19127978
- Rodríguez-Navarro S, et al. (2004) Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. Cell 116(1):75-86 PMID: 14718168