The Xmas-2 Protein of Drosophila melanogaster Undergoes Cleavage into Two Fragments
Author:
Publisher
Pleiades Publishing Ltd
Subject
General Chemistry,Biochemistry,General Medicine,Biophysics
Link
https://link.springer.com/content/pdf/10.1134/S1607672923700163.pdf
Reference12 articles.
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2. Fischer, T. et al., The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores, EMBO J., 2002, vol. 21, no. 21, pp. 5843–5852.
3. Jani, D. et al., Functional and structural characterization of the mammalian TREX-2 complex that links transcription with nuclear messenger RNA export, Nucleic Acids Res., 2012, vol. 40, no. 10, pp. 4562–4573.
4. Kurshakova, M.M. et al., SAGA and a novel Drosophila export complex anchor efficient transcription and mRNA export to NPC, EMBO J., 2007, vol. 26, no. 24, pp. 4956–4965.
5. Rodríguez-Navarro, S. et al., Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery, Cell, 2004, vol. 116, no. 1, pp. 75–86.
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Xmas-2 Protein, the Core Protein of the TREX-2 mRNA Export Complex, Does not Determine the Specificity of ras2 mRNA Binding by the Complex;Doklady Biochemistry and Biophysics;2024-08-28
2. The Human TREX-2 Complex Interacts with Subunits of the ORC Complex;Doklady Biochemistry and Biophysics;2023-12
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