| Title | Date | PubMed ID |
|---|
| The ATPase activity and the functional domain of PotA, a component of the sermidine-preferential uptake system in Escherichia coli. | 2002 Jul 5 | 11976340 |
| Polyamine uptake systems in Escherichia coli. | 2001 Apr-May | 11421274 |
| Polyamine transport in bacteria and yeast. | 1999 Dec 15 | 10585849 |
| Formation of a complex containing ATP, Mg2+, and spermine. Structural evidence and biological significance. | 1998 Nov 20 | 9812989 |
| The 1.8-A X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding. | 1996 Oct | 8897598 |
| Spermidine-preferential uptake system in Escherichia coli. Identification of amino acids involved in polyamine binding in PotD protein. | 1996 May 24 | 8647815 |
| Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli. | 1996 Apr 19 | 8621624 |
| Spermidine-preferential uptake system in Escherichia coli. ATP hydrolysis by PotA protein and its association with membrane. | 1995 Oct 27 | 7592703 |
| Functions of potA and potD proteins in spermidine-preferential uptake system in Escherichia coli. | 1993 Sep 15 | 8366082 |