Search


Current filters:


Start a new search
Add filters:

Use filters to refine the search results.


Results 1-9 of 9 (Search time: 0.003 seconds).
  • previous
  • 1
  • next
Item hits:
PreviewIssue DateTitleAuthor(s)
2014AdcA and AdcAII employ distinct zinc acquisition mechanisms and contribute additively to zinc homeostasis in Streptococcus pneumoniaePlumptre, C.; Eijkelkamp, B.; Morey, J.; Behr, F.; Couñago, R.; Ogunniyi, A.; Kobe, B.; O'Mara, M.; Paton, J.; McDevitt, C.
2014A functional genomics catalogue of activated transcription factors during pathogenesis of pneumococcal diseaseMahdi, L.; Deihimi, T.; Zamansani, F.; Fruzangohar, M.; Adelson, D.; Paton, J.; Ogunniyi, A.; Ebrahimie, E.
2014Dual roles of F123 in protein homodimerization and inhibitor binding to biotin protein ligase from Staphylococcus aureusSoares da Costa, T.; Yap, M.; Perugini, M.; Wallace, J.; Abell, A.; Wilce, M.; Polyak, S.; Booker, G.
2014Relationship between O-antigen chain length and resistance to colicin E2 in Shigella flexneriTran, N.; Papadopoulos, M.; Morona, R.
2014IcsA is a Shigella flexneri adhesin regulated by the type III secretion system and required for pathogenesisZumsteg, A.; Goosmann, C.; Brinkmann, V.; Morona, R.; Zychlinsky, A.
2014Road rules for traffic on DNA - systematic analysis of transcriptional roadblocking in vivoHao, N.; Krishna, S.; Ahlgren-Berg, A.; Cutts, E.; Shearwin, K.; Dodd, I.
2014Overlapping functionality of the Pht proteins in zinc homeostasis of Streptococcus pneumoniaePlumptre, C.; Hughes, C.; Harvey, R.; Eijkelkamp, B.; McDevitt, C.; Paton, J.; Camilli, A.
2014Structure, activity, and inhibition of the carboxyltransferase β-Subunit of acetyl coenzyme a carboxylase (AccD6) from mycobacterium tuberculosisReddy, M.; Breda, A.; Bruning, J.; Sherekar, M.; Valluru, S.; Thurman, C.; Ehrenfeld, H.; Sacchettini, J.
2014The impact of pneumolysin on the macrophage response to Streptococcus pneumoniae is strain-dependentHarvey, R.; Hughes, C.; Paton, A.; Trappetti, C.; Paton, J.; Tweten, R.; Neyrolles, O.