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1  Serratia marcescens, Proteus mirabilis, and Proteus vulgaris).
2 perative infection with antibiotic-resistant Proteus vulgaris.
3 by expressing an L-amino acid deaminase from Proteus vulgaris.
4 nzymes, cABCI and cABCII, were identified in Proteus vulgaris.
5                                              Proteus vulgaris accounted for 81% (13/16) of the sample
6 udomonas aeruginosa, Enterococcus aerogenes, Proteus vulgaris and Enterobacter sakazakii) bacteria, w
7  Two commercial enzymes, chondroitinase ABC (Proteus vulgaris) and chondroitinase ACII (Arthrobacter
8 eas MICs for E. coli, Klebsiella pneumoniae, Proteus vulgaris, and Pseudomonas aeruginosa were > 100
9  we solve the crystal structure of CodB from Proteus vulgaris, at 2.4 angstrom resolution in complex
10      The rtn gene, identified as coming from Proteus vulgaris ATCC 13315, is present in Escherichia c
11 Serratia marcescens, Erwinia carotovora, and Proteus vulgaris but not in several nonenteric bacteria.
12       We placed 43 isolates belonging to the Proteus vulgaris complex into proposed DNA groups (genom
13  of these enzymes, chondroitinase ABC I from Proteus vulgaris, has the broadest substrate specificity
14 gA antitoxin regulates the expression of the Proteus vulgaris higBA toxin-antitoxin operon from the R
15 of the tna operon of Escherichia coli and of Proteus vulgaris is induced by L-tryptophan.
16 species-specific class A beta-lactamase from Proteus vulgaris K1 was crystallized at pH 6.25 and its
17 oaceticus BD413, Vibrio cholerae El Tor, and Proteus vulgaris K80, were members of a previously descr
18                                              Proteus vulgaris L-amino acid deaminase (pvLAAD) belongs
19  of the PvuII plasmid pPvu1, originally from Proteus vulgaris, making this the first completely seque
20 erived from either Salmonella typhimurium or Proteus vulgaris, microorganisms that have diverged from
21 ound in the O-polysaccharide of the LPS from Proteus vulgaris OX19 used in the Weil-Felix test, sugge
22 ression of the tryptophanase (tna) operon of Proteus vulgaris, short deletions were introduced in the
23 st Listeria monocytogenes, Escherichia coli, Proteus vulgaris, Staphylococcus aureus, and Candida alb
24 Serratia marcescens, Erwinia carotovora, and Proteus vulgaris, strongly suggesting that the physiolog
25 ith deletion constructs of the tna operon of Proteus vulgaris supported this interpretation.
26 e solved two x-ray crystal structures of the Proteus vulgaris tetrameric HigB-(HigA)2-HigB TA complex
27 ng of substrates and inhibitors to wild-type Proteus vulgaris tryptophan indole-lyase and to wild typ
28           Urinary tract infections caused by Proteus vulgaris typically form biofilms and are resista
29 scherichia coli, Salmonella typhimurium, and Proteus vulgaris) We also isolated transposition events
30 with serum antibodies cross-reactive against Proteus vulgaris (Weil-Felix reaction).