| Rank | Title | Journal | Year | PubWeight™‹?› |
|---|---|---|---|---|
| 1 | The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site. | J Biol Chem | 2003 | 1.33 |
| 2 | Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases. | J Mol Biol | 2005 | 1.09 |
| 3 | Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains. | Protein Sci | 2006 | 1.03 |
| 4 | Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains. | Eur J Biochem | 2004 | 1.00 |
| 5 | Crystal structure of the N-terminal domain of E. coli Lon protease. | Protein Sci | 2005 | 0.99 |
| 6 | Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution. | J Struct Biol | 2004 | 0.99 |
| 7 | Structure of the N-terminal fragment of Escherichia coli Lon protease. | Acta Crystallogr D Biol Crystallogr | 2010 | 0.83 |