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1.

Research article   Open Access Highly Accessed

Rapid evolution of fluoroquinolone-resistant Escherichia coli in Nigeria is temporally associated with fluoroquinolone use

Adebayo Lamikanra, Jennifer L Crowe, Rebeccah S Lijek, Babatunde W Odetoyin, John Wain, A Oladipo Aboderin, Iruka N Okeke BMC Infectious Diseases 2011, 11:312 (7 November 2011)

Abstract | Full text | PDF | PubMed

2.

Research   Open Access

IS3 profiling identifies the enterohaemorrhagic Escherichia coli O-island 62 in a distinct enteroaggregative E. coli lineage

Iruka N Okeke, Louissa R Macfarlane-Smith, Jonathan N Fletcher, Anna M Snelling Gut Pathogens 2011, 3:4 (30 March 2011)

Abstract | Full text | PDF | PubMed

3.

Research article   Open Access Highly Accessed

Quinolone resistance in Escherichia coli from Accra, Ghana

Sreela S Namboodiri, Japheth A Opintan, Rebeccah S Lijek, Mercy J Newman, Iruka N Okeke BMC Microbiology 2011, 11:44 (27 February 2011)

Abstract | Full text | PDF | PubMed | Cited on BioMed Central

4.

Research article   Open Access Highly Accessed

Genetic elements associated with antimicrobial resistance in enteropathogenic Escherichia coli (EPEC) from Brazil

Isabel CA Scaletsky, Tamara B Souza, Katia RS Aranda, Iruka N Okeke BMC Microbiology 2010, 10:25 (27 January 2010)

Abstract | Full text | PDF | PubMed

5.

Methodology article   Open Access

The commonly-used DNA probe for diffusely-adherent Escherichia coli cross-reacts with a subset of enteroaggregative E. coli

Anna M Snelling, Louissa R Macfarlane-Smith, Jonathan N Fletcher, Iruka N Okeke BMC Microbiology 2009, 9:269 (21 December 2009)

Abstract | Full text | PDF | PubMed

6.

Research article   Open Access

Rhodobacter capsulatus porphobilinogen synthase, a high activity metal ion independent hexamer

David W Bollivar, Cheryl Clauson, Rachel Lighthall, Siiri Forbes, Bashkim Kokona, Robert Fairman, Lenka Kundrat, Eileen K Jaffe BMC Biochemistry 2004, 5:17 (22 November 2004)

Abstract | Full text | PDF | PubMed |  Editor’s summary

Porphobilinogen synthase from Rhodobacter capsulatus is unusual in not requiring a metal ion for activity and in forming hexamers rather than the octamers formed by its counterparts in other organisms.

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