ライフサイエンスコーパス: cephalothin

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1 and oxidase positive, and it is sensitive to cephalothin.

2 sensitive to nalidixic acid but resistant to cephalothin.

3 Our first model suggests that this chiral cephalothin analogue adopts a novel conformation in the

4 intermediate with (i) the meta-carboxyphenyl cephalothin analogue and (ii) the carbapenems, imipenem

5 In antimicrobial susceptibility tests, this cephalothin analogue lowered the ceftazidime and cefotax

6 In the boronic acid series, a chiral cephalothin analogue with a meta-carboxyphenyl moiety co

7 sidered two beta-lactam antibiotics, namely, cephalothin and aztreonam, belonging to two different su

8 The permeability of cephalothin and cephaloridine in A. baumannii was decrea

9 thermore, the outer membrane permeability to cephalothin and cephaloridine, measured in intact cells,

10 nic acid transition state analogs that mimic cephalothin and found substitutions at Arg-244 markedly

11 of acyl-enzyme intermediates formed between cephalothin and the dd-peptidase of Streptomyces sp. R61

12 xhibiting enhanced hydrolysis of nitrocefin, cephalothin, and cefotaxime relative to IMP-1.

13 educed nitrate to nitrite, were resistant to cephalothin, and exhibited intermediate susceptibility t

14 s combined was more than 20% for ampicillin, cephalothin, and sulfamethoxazole in each year studied.

15 hatase, and was resistant to nalidixic acid, cephalothin, and trimethoprim-sulfamethoxazole.

16 actam antibiotics (penicillin G, ampicillin, cephalothin, cefaclor, cefuroxime, cefoperazone, and cef

17 For other compounds (cephalothin, cefamandole, and cephaloridine) that showed

18 -four of 49 isolates (49%) were sensitive to cephalothin, cefazolin, and cefuroxime.

19 K(i) value for cefotaxime as an inhibitor of cephalothin hydrolysis is 27 nM.

20 imethoprim-sulfamethoxazole, ampicillin, and cephalothin increased significantly among uropathogens c

21 The thiol intermediate generated from cephalothin is a slow binding inhibitor.

22 mical analyses, testing of susceptibility to cephalothin, lysis by a Hafnia-specific phage, and ampli

23 demonstrate that other beta-lactams, such as cephalothin, meropenem, and penicillin G, proceed throug

24 cefazolin (P = 0.02), cefotetan (P = 0.006), cephalothin (P<0.0001), clindamycin (P = 0.04), erythrom

25 ates combined to ampicillin (P<.002), and to cephalothin, trimethoprim, and trimethoprim-sulfamethoxa

26 nt complexes of the beta-lactamase substrate cephalothin were determined by X-ray crystallography.

27 vieae, the MICs of penicillin and, possibly, cephalothin were higher than for L. lactis, and unlike L

28 ) by 50-70% against "good" substrates (i.e., cephalothin) while increasing k(cat)/K(m) against "poor"

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