ライフサイエンスコーパス: freundii

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1 ogenes, Morganella morganii, and Citrobacter freundii.

2 rs specific for the ampC gene of Citrobacter freundii.

3 es from Enterobacter cloacae and Citrobacter freundii.

4 ia coli, Klebsiella oxytoca, and Citrobacter freundii.

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

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

7 rnatants from Proteus mirabilis, Citrobacter freundii and Enterobacter agglomerans [cyclo(DeltaAla-L-

8 (HBMEC) to study the interaction between C. freundii and HBMEC.

9 carbapenem-resistant isolates of Citrobacter freundii and Klebsiella oxytoca recovered from different

10 ndent glycerol dehydratases from Citrobacter freundii and Klebsiella pneumoniae.

11 Gram-negative Escherichia coli, Citrobacter freundii, and Enterobacter aerogenes, as well as Gram-po

12 ription from the tpl promoter of Citrobacter freundii ATCC 29063 (C. braakii).

13 Citrobacter rodentium (formerly Citrobacter freundii biotype 4280 and Citrobacter genomospecies 9) w

14 Citrobacter rodentium (formally Citrobacter freundii biotype 4280) is a highly infectious pathogen t

15 umans and Citrobacter rodentium (formerly C. freundii biotype 4280)-mediated transmissible colonic hy

16 e have previously shown that the Citrobacter freundii BMC associated with 1,2-propanediol utilization

17 regation was time dependent and seen with C. freundii but not with noninvasive E. coli HB101 and meni

18 rtant determinants of the pathogenesis of C. freundii causing meningitis and brain abscess may relate

19 ation of the intestinal tract by Citrobacter freundii, Clostridium species, Enterobacter cloacae, Ent

20 Neither the class C Citrobacter freundii CMY-2 AmpC beta-lactamase nor the class A TEM-1

21 a number of species (Acinetobacter spp., C. freundii, E. aerogenes, K. pneumoniae, P. aeruginosa, an

22 SAs (AmpC beta-lactamases of M. morganii, C. freundii, E. coli, and E. cloacae).

23 The tpl gene of Citrobacter freundii encodes an enzyme that catalyzes the conversion

24 , such as the E. cloacae P99 and Citrobacter freundii enzymes, the ES GC1 beta-lactamase is able to r

25 gregated after HBMEC came in contact with C. freundii; furthermore, the microtubule aggregation was t

26 f the phosphonate with both ES GC1 and WT C. freundii GN346 beta-lactamases have been determined to h

27 lla oxytoca, Citrobacter koseri, Citrobacter freundii group, Enterobacter spp., and Serratia marcesce

28 tyrosine phenol-lyase (TPL) from Citrobacter freundii have been examined.

29 ies such as Escherichia coli and Citrobacter freundii in real-time PCR assays.

30 Tyrosine phenol-lyase (TPL) from Citrobacter freundii is a pyridoxal 5'-phosphate (PLP)-dependent enz

31 ast to other meningitis-causing bacteria, C. freundii is able to replicate within HBMEC.

32 Tyrosine phenol-lyase (TPL) from Citrobacter freundii is activated about 30-fold by monovalent cation

33 In this study, we show that C. freundii is capable of invading and trancytosing HBMEC i

34 Tyrosine phenol-lyase (TPL) from Citrobacter freundii is dependent on monovalent cations, K(+) or NH(

35 anediol utilization enzymes from Citrobacter freundii is fully functional when cloned in Escherichia

36 interactions between AmpR (from Citrobacter freundii), its DNA operator, and repressor UDP-MurNAc-pe

37 was also observed in strains of Citrobacter freundii, Klebsiella pneumoniae, Enterobacter agglomeran

38 ty of these ligands for E. coli, Citrobacter freundii, Staphylococcus epidermidis were 100%, 2.6% and

39 eus, Pseudomonas aeruginosa, and Citrobacter freundii to ensure the species specificity of the select

40 eus, Pseudomonas aeruginosa, and Citrobacter freundii, to ensure the species-specificity of the selec

41 -lyase and to wild type and Y71F Citrobacter freundii tyrosine phenol-lyase was investigated in the c

42 Invasion of HBMEC by C. freundii was determined to be dependent on microfilament

43 acteria (Salmonella typhimurium, Citrobacter freundii, Yersinia enterocolitica, Serratia marcescens,

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