PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
14630927-3	2004	Here we show that, although cytoplasmic at steady state, Axin shuttles in fact in and out of the nucleus; Axin accumulates in the nucleus of cells treated with leptomycin B, a specific inhibitor of the CRM1-mediated nuclear export pathway and is efficiently exported from Xenopus oocyte nuclei in a RanGTP- and CRM1-dependent manner.	rangtp	299-305	exportin 1 S homeolog	Xenopus laevis	202-206	
14630927-4	2004	We have characterized the sequence requirement for export and identified two export domains, which do not contain classical nuclear export consensus sequences, and we show that Axin binds directly to the export factor CRM1 in the presence of RanGTP.	rangtp	242-248	exportin 1 S homeolog	Xenopus laevis	218-222	
9323133-5	1997	We conclude that CRM1 is an export receptor for leucine-rich nuclear export signals and discuss a model for the role of RanGTP in CRM1 function and in nuclear export in general.	rangtp	120-126	exportin 1 S homeolog	Xenopus laevis	17-21	
10454574-2	1999	CRM1 export cargoes include proteins with a leucine-rich nuclear export signal (NES) that bind directly to CRM1 in a trimeric complex with RanGTP.	rangtp	139-145	exportin 1 S homeolog	Xenopus laevis	0-4	
10454574-2	1999	CRM1 export cargoes include proteins with a leucine-rich nuclear export signal (NES) that bind directly to CRM1 in a trimeric complex with RanGTP.	rangtp	139-145	exportin 1 S homeolog	Xenopus laevis	107-111	
10454574-4	1999	We also show that a trimeric CRM1-NES-RanGTP complex is disassembled by RanBP1 in the presence of RanGAP, even though RanBP1 itself contains a leucine-rich NES.	rangtp	38-44	exportin 1 S homeolog	Xenopus laevis	29-33	
10454574-6	1999	In addition, we identify the Xenopus homologue of the nucleoporin CAN/Nup214 as a RanGTP- and NES cargo-specific binding site for CRM1, suggesting that this nucleoporin plays a role in export complex disassembly and/or CRM1 recycling.	rangtp	82-88	exportin 1 S homeolog	Xenopus laevis	130-134	
10454574-6	1999	In addition, we identify the Xenopus homologue of the nucleoporin CAN/Nup214 as a RanGTP- and NES cargo-specific binding site for CRM1, suggesting that this nucleoporin plays a role in export complex disassembly and/or CRM1 recycling.	rangtp	82-88	exportin 1 S homeolog	Xenopus laevis	219-223	
9323133-5	1997	We conclude that CRM1 is an export receptor for leucine-rich nuclear export signals and discuss a model for the role of RanGTP in CRM1 function and in nuclear export in general.	rangtp	120-126	exportin 1 S homeolog	Xenopus laevis	130-134