| review article | Q7318358 |
| scholarly article | Q13442814 |
| P356 | DOI | 10.1111/J.1574-6968.1999.TB13542.X |
| P8608 | Fatcat ID | release_mbmxdiwp3bf5bmcs5vqi3w5i2a |
| P698 | PubMed publication ID | 10234816 |
| P5875 | ResearchGate publication ID | 227965122 |
| P2093 | author name string | B G Hall | |
| P2860 | cites work | The catalytic consequences of experimental evolution. Transition-state structure during catalysis by the evolved beta-galactosidases of Escherichia coli (ebg enzymes) changed by a single mutational event | Q28341139 |
| The catalytic consequences of experimental evolution. Studies on the subunit structure of the second (ebg) beta-galactosidase of Escherichia coli, and on catalysis by ebgab, an experimental evolvant containing two amino acid substitutions | Q34351811 | ||
| Catalytic consequences of experimental evolution: catalysis by a 'third-generation' evolvant of the second beta-galactosidase of Escherichia coli, ebgabcde, and by ebgabcd, a 'second-generation' evolvant containing two supposedly 'kinetically silent | Q41844922 | ||
| Catalysis by the large subunit of the second beta-galactosidase of Escherichia coli in the absence of the small subunit | Q41972517 | ||
| Large changes of transition-state structure during experimental evolution of an enzyme | Q42021013 | ||
| Determining the evolutionary potential of a gene | Q47751361 | ||
| P433 | issue | 1 | |
| P921 | main subject | experimental evolution | Q3592884 |
| P304 | page(s) | 1-8 | |
| P577 | publication date | 1999-05-01 | |
| P1433 | published in | FEMS Microbiology Letters | Q15756366 |
| P1476 | title | Experimental evolution of Ebg enzyme provides clues about the evolution of catalysis and to evolutionary potential | |
| P478 | volume | 174 |
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