Pub. Date : 2010 Sep 15
PMID : 20844015
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex. | Adenosine Triphosphate | SAP domain containing ribonucleoprotein | Homo sapiens |
| 2 | 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 | SAP domain containing ribonucleoprotein | Homo sapiens |
| 3 | 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 | SAP domain containing ribonucleoprotein | Homo sapiens |
| 4 | 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 | SAP domain containing ribonucleoprotein | Homo sapiens |
| 5 | 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 | SAP domain containing ribonucleoprotein | Homo sapiens |
| 6 | 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 | SAP domain containing ribonucleoprotein | Homo sapiens |