ライフサイエンスコーパス: Citrobacter freundii

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1 robacter aerogenes, Morganella morganii, and Citrobacter freundii.

2 using primers specific for the ampC gene of Citrobacter freundii.

3 lass C enzymes from Enterobacter cloacae and Citrobacter freundii.

4 e, Escherichia coli, Klebsiella oxytoca, and Citrobacter freundii.

5 bilis (4.0%), Klebsiella oxytoca (2.7%), and Citrobacter freundii (2.0%).

6 , Pseudomonas aeruginosa (40% identity), and Citrobacter freundii (38% identity).

7 ll-free supernatants from Proteus mirabilis, Citrobacter freundii and Enterobacter agglomerans [cyclo

8 detected in carbapenem-resistant isolates of Citrobacter freundii and Klebsiella oxytoca recovered fr

9 yme B12-dependent glycerol dehydratases from Citrobacter freundii and Klebsiella pneumoniae.

10 tatively for Gram-negative Escherichia coli, Citrobacter freundii, and Enterobacter aerogenes, as wel

11 alyze transcription from the tpl promoter of Citrobacter freundii ATCC 29063 (C. braakii).

12 Citrobacter rodentium (formerly Citrobacter freundii biotype 4280 and Citrobacter genomo

13 Citrobacter rodentium (formally Citrobacter freundii biotype 4280) is a highly infectiou

14 We have previously shown that the Citrobacter freundii BMC associated with 1,2-propanediol

15 with colonization of the intestinal tract by Citrobacter freundii, Clostridium species, Enterobacter

16 Neither the class C Citrobacter freundii CMY-2 AmpC beta-lactamase nor the c

17 The tpl gene of Citrobacter freundii encodes an enzyme that catalyzes th

18 e (WT) forms, such as the E. cloacae P99 and Citrobacter freundii enzymes, the ES GC1 beta-lactamase

19 iae, Klebsiella oxytoca, Citrobacter koseri, Citrobacter freundii group, Enterobacter spp., and Serra

20 rosine with tyrosine phenol-lyase (TPL) from Citrobacter freundii have been examined.

21 similar species such as Escherichia coli and Citrobacter freundii in real-time PCR assays.

22 Tyrosine phenol-lyase (TPL) from Citrobacter freundii is a pyridoxal 5'-phosphate (PLP)-d

23 Tyrosine phenol-lyase (TPL) from Citrobacter freundii is activated about 30-fold by monov

24 Tyrosine phenol-lyase (TPL) from Citrobacter freundii is dependent on monovalent cations,

25 lle and propanediol utilization enzymes from Citrobacter freundii is fully functional when cloned in

26 he molecular interactions between AmpR (from Citrobacter freundii), its DNA operator, and repressor U

27 c inhibition was also observed in strains of Citrobacter freundii, Klebsiella pneumoniae, Enterobacte

28 ve selectivity of these ligands for E. coli, Citrobacter freundii, Staphylococcus epidermidis were 10

29 lococcus aureus, Pseudomonas aeruginosa, and Citrobacter freundii to ensure the species specificity o

30 lococcus aureus, Pseudomonas aeruginosa, and Citrobacter freundii, to ensure the species-specificity

31 ophan indole-lyase and to wild type and Y71F Citrobacter freundii tyrosine phenol-lyase was investiga

32 five enterobacteria (Salmonella typhimurium, Citrobacter freundii, Yersinia enterocolitica, Serratia

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