PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22928037-5	2012	Recently, we found that both CIP29 and Aly associate with the DEAD box helicase UAP56 and with the TREX complex in an ATP-dependent manner.	Adenosine Triphosphate	118-121	SAP domain containing ribonucleoprotein	Homo sapiens	29-34	
20844015-0	2010	ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex.	Adenosine Triphosphate	0-3	SAP domain containing ribonucleoprotein	Homo sapiens	95-100	
20844015-5	2010	We show that UAP56 mediates an ATP-dependent interaction between the THO complex and both CIP29 and Aly, indicating that TREX assembly is ATP-dependent.	Adenosine Triphosphate	31-34	SAP domain containing ribonucleoprotein	Homo sapiens	90-95	
20844015-5	2010	We show that UAP56 mediates an ATP-dependent interaction between the THO complex and both CIP29 and Aly, indicating that TREX assembly is ATP-dependent.	Adenosine Triphosphate	138-141	SAP domain containing ribonucleoprotein	Homo sapiens	90-95	
20844015-6	2010	Using recombinant proteins expressed in Escherichia coli, we show that UAP56, Aly, and CIP29 form an ATP-dependent trimeric complex, and UAP56 bridges the interaction between CIP29 and Aly.	Adenosine Triphosphate	101-104	SAP domain containing ribonucleoprotein	Homo sapiens	87-92	
20844015-6	2010	Using recombinant proteins expressed in Escherichia coli, we show that UAP56, Aly, and CIP29 form an ATP-dependent trimeric complex, and UAP56 bridges the interaction between CIP29 and Aly.	Adenosine Triphosphate	101-104	SAP domain containing ribonucleoprotein	Homo sapiens	175-180	
20844015-7	2010	We conclude that the interaction of two conserved export proteins, CIP29 and Aly, with UAP56 is strictly regulated by ATP during assembly of the TREX complex.	Adenosine Triphosphate	118-121	SAP domain containing ribonucleoprotein	Homo sapiens	67-72	
31917363-8	2020	However, with the addition of ATP, both the Apo-TREX complex and the Apo-AREX complex were remodeled to highly similar ATP-TREX complex containing the THO subcomplex, ALYREF and CIP29.	Adenosine Triphosphate	30-33	SAP domain containing ribonucleoprotein	Homo sapiens	178-183	
31917363-8	2020	However, with the addition of ATP, both the Apo-TREX complex and the Apo-AREX complex were remodeled to highly similar ATP-TREX complex containing the THO subcomplex, ALYREF and CIP29.	Adenosine Triphosphate	119-122	SAP domain containing ribonucleoprotein	Homo sapiens	178-183