CRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals
- M. Fornerod, M. Ohno, Minoru Yoshida, I. Mattaj
- BiologyCell
- 19 September 1997
Nucleocytoplasmic transport: the soluble phase.
- I. Mattaj, L. Englmeier
- BiologyAnnual Review of Biochemistry
- 1998
Directionality of either import or export depends on association between a substrate and its receptor on one side of the nuclear envelope and dissociation on the other, and the Ran GTPase is critical in generating this asymmetry.
The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus
- E. Izaurralde, U. Kutay, C. von Kobbe, I. Mattaj, D. Görlich
- BiologyEMBO Journal
- 3 November 1997
The GTPase Ran is essential for nuclear import of proteins with a classical nuclear localization signal (NLS). Ran's nucleotide‐bound state is determined by the chromatin‐bound exchange factor RCC1…
A nuclear cap binding protein complex involved in pre-mRNA splicing
- E. Izaurralde, Joe D. Lewis, C. McGuigan, M. Jankowska, E. Darżynkiewicz, I. Mattaj
- BiologyCell
- 26 August 1994
The Conserved Nup107-160 Complex Is Critical for Nuclear Pore Complex Assembly
- T. Walther, A. Alves, V. Doye
- BiologyCell
- 18 April 2003
Herpes simplex virus ICP27 protein provides viral mRNAs with access to the cellular mRNA export pathway
- M. Koffa, J. Clements, S. Kuersten
- Biology, ChemistryEMBO Journal
- 15 October 2001
It is proposed that ICP27 associates with viral mRNAs and recruits TAP/NXF1 via its interaction with REF proteins, allowing the otherwise inefficiently exported viral m RNAs to access the TAP‐mediated export pathway.
Ran Induces Spindle Assembly by Reversing the Inhibitory Effect of Importin α on TPX2 Activity
- O. Gruss, R. Carazo-Salas, I. Mattaj
- Biology, ChemistryCell
- 12 January 2001
HURP Is Part of a Ran-Dependent Complex Involved in Spindle Formation
- M. Koffa, Claudia M. Casanova, Rachel A Santarella, T. Köcher, M. Wilm, I. Mattaj
- BiologyCurrent Biology
- 18 April 2006
Dominant‐negative mutants of importin‐β block multiple pathways of import and export through the nuclear pore complex
- U. Kutay, E. Izaurralde, F. Bischoff, I. Mattaj, D. Görlich
- Biology, ChemistryEMBO Journal
- 15 March 1997
These importin‐β mutants are very efficient inhibitors of NLS‐dependent protein import, however, they also inhibit M9 signal‐mediated nuclear import as well as nuclear export of mRNA, U snRNA, and the NES‐containing Rev protein, which suggests that mediators of these various transport events share binding sites on the NPC and/or that mechanisms exist to coordinate translocation through the NPC via different nucleocytoplasmic transport pathways.
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