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Items: 11

1.
The binary protein-protein interaction landscape of Escherichia coli
Seesandra V. Rajagopala, Patricia Sikorski, Ashwani Kumar, Roberto Mosca, James Vlasblom, Roland Arnold, Jonathan Franca-Koh, Suman B. Pakala, Sadhna Phanse, Arnaud Ceol, Roman Häuser, Gabriella Siszler, Stefan Wuchty, Andrew Emili, Mohan Babu, Patrick Aloy, Rembert Pieper, Peter Uetz
Nat Biotechnol. Author manuscript; available in PMC 2014 Sep 1.
Published in final edited form as: Nat Biotechnol. 2014 Mar; 32(3): 285–290. Published online 2014 Feb 23. doi: 10.1038/nbt.2831
PMCID:
PMC4123855
AbstractArticlePDF–1.1M
2.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110
Koji Hayashi, Naoki Morooka, Yoshihiro Yamamoto, Katsutoshi Fujita, Katsumi Isono, Sunju Choi, Eiichi Ohtsubo, Tomoya Baba, Barry L Wanner, Hirotada Mori, Takashi Horiuchi
Mol Syst Biol. 2006; 2: 2006.0007. Published online 2006 Feb 21. doi: 10.1038/msb4100049
PMCID:
PMC1681481
AbstractArticlePDF–141K
3.
Escherichia coli K-12: a cooperatively developed annotation snapshot—2005
Monica Riley, Takashi Abe, Martha B. Arnaud, Mary K.B. Berlyn, Frederick R. Blattner, Roy R. Chaudhuri, Jeremy D. Glasner, Takashi Horiuchi, Ingrid M. Keseler, Takehide Kosuge, Hirotada Mori, Nicole T. Perna, Guy Plunkett, III, Kenneth E. Rudd, Margrethe H. Serres, Gavin H. Thomas, Nicholas R. Thomson, David Wishart, Barry L. Wanner
Nucleic Acids Res. 2006; 34(1): 1–9. Published online 2006 Jan 5. doi: 10.1093/nar/gkj405
PMCID:
PMC1325200
AbstractArticlePDF–204K
4.
Larger increases in sensitivity to paracatalytic inactivation than in catalytic competence during experimental evolution of the second beta-galactosidase of Escherichia coli.
S V Calugaru, S Krishnan, C J Chany, 2nd, B G Hall, M L Sinnott
Biochem J. 1997 Jul 1; 325(Pt 1): 117–121. doi: 10.1042/bj3250117
PMCID:
PMC1218535
SummaryPDF–376K
5.
DNA Sequence Analysis of Artificially Evolved Ebg Enzyme and Ebg Repressor Genes
B. G. Hall, P. W. Betts, J. C. Wootton
Genetics. 1989 Dec; 123(4): 635–648. doi: 10.1093/genetics/123.4.635
PMCID:
PMC1203876
SummaryPDF–1.2M
6.
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.
B F Li, D Holdup, C A Morton, M L Sinnott
Biochem J. 1989 May 15; 260(1): 109–114. doi: 10.1042/bj2600109
PMCID:
PMC1138632
SummaryPage BrowsePDF–1.0M
7.
Catalysis by the large subunit of the second beta-galactosidase of Escherichia coli in the absence of the small subunit.
S V Calugaru, B G Hall, M L Sinnott
Biochem J. 1995 Nov 15; 312(Pt 1): 281–286. doi: 10.1042/bj3120281
PMCID:
PMC1136256
SummaryPage BrowsePDF–1.1M
8.
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' mutations.
S Krishnan, B G Hall, M L Sinnott
Biochem J. 1995 Dec 15; 312(Pt 3): 971–977. doi: 10.1042/bj3120971
PMCID:
PMC1136208
SummaryPage BrowsePDF–1.3M
9.
Large changes of transition-state structure during experimental evolution of an enzyme.
K Srinivasan, A Konstantinidis, M L Sinnott, B G Hall
Biochem J. 1993 Apr 1; 291(Pt 1): 15–17. doi: 10.1042/bj2910015
PMCID:
PMC1132473
SummaryPage BrowsePDF–602K
10.
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.
A C Elliott, S K, M L Sinnott, P J Smith, J Bommuswamy, Z Guo, B G Hall, Y Zhang
Biochem J. 1992 Feb 15; 282(Pt 1): 155–164. doi: 10.1042/bj2820155
PMCID:
PMC1130902
SummaryPage BrowsePDF–2.6M
11.
Evolution of a Second Gene for β-Galactosidase in Escherichia coli
John H. Campbell, Judith A. Lengyel, John Langridge
Proc Natl Acad Sci U S A. 1973 Jun; 70(6): 1841–1845. doi: 10.1073/pnas.70.6.1841
PMCID:
PMC433609
SummaryPage BrowsePDF–1007K

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