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Molecular Cell|October 5, 2001
Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factorS Fribourg, I C Braun, E Izaurralde, et al.The EMBO Journal|April 15, 1999
TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleusI C Braun, E Rohrbach, C Schmitt, et al.The Journal of Biological Chemistry|March 22, 2001
Overexpression of TAP/p15 heterodimers bypasses nuclear retention and stimulates nuclear mRNA exportI C Braun, A Herold, M Rode, et al.EMBO Reports|December 18, 2001
The protein Mago provides a link between splicing and mRNA localizationH Le Hir, D Gatfield, I C Braun, et al.EMBO Reports|March 21, 2001
Prediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporinsM Suyama, T Doerks, I C Braun, et al.Current Biology : CB|November 7, 2001
The DExH/D box protein HEL/UAP56 is essential for mRNA nuclear export in DrosophilaD Gatfield, H Le Hir, C Schmitt, et al.RNA (New York, N.Y.)|April 29, 2000
REF, an evolutionary conserved family of hnRNP-like proteins, interacts with TAP/Mex67p and participates in mRNA nuclear exportF Stutz, A Bachi, T Doerks, et al.Molecular and Cellular Biology|November 14, 2000
TAP (NXF1) belongs to a multigene family of putative RNA export factors with a conserved modular architectureA Herold, M Suyama, J P Rodrigues, et al.RNA (New York, N.Y.)|February 11, 2000
The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substratesA Bachi, I C Braun, J P Rodrigues, et al.Pageof 1