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rdf:type |
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lifeskim:mentions |
umls-concept:C0014834,
umls-concept:C0026651,
umls-concept:C0030551,
umls-concept:C0033684,
umls-concept:C0080194,
umls-concept:C0205250,
umls-concept:C0205321,
umls-concept:C0332325,
umls-concept:C0596988,
umls-concept:C0814810,
umls-concept:C1521840,
umls-concept:C1707455
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pubmed:issue |
5
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pubmed:dateCreated |
1982-3-13
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pubmed:abstractText |
An eschericia coli K-12 mutant highly resistant to moxalactam but only slightly resistant to other beta-lactam antibiotics was obtained by mutagen treatment. The affinity of moxalactam for its target penicillin-binding proteins was unchanged, as was the level of beta-lactamase activity. The penetration of [14C] moxalactam, however, was markedly reduced in the mutant. Electrophoretic analysis revealed alterations of the outer membrane proteins. A reduction in the amount of one of the pore-forming proteins (porins) was especially noteworthy. These data suggest that moxalactam resistance is the result of an alteration in the outer membrane structure.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6459762-319999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6459762-346560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6459762-378942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6459762-389623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6459762-4591127,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6459762-4725679,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6459762-4946509,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6459762-6448572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6459762-6448573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6459762-773686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6459762-783110,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6459762-786294
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0066-4804
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
613-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6459762-Bacterial Proteins,
pubmed-meshheading:6459762-Cell Membrane,
pubmed-meshheading:6459762-Cephalosporins,
pubmed-meshheading:6459762-Cephamycins,
pubmed-meshheading:6459762-Drug Resistance, Microbial,
pubmed-meshheading:6459762-Escherichia coli,
pubmed-meshheading:6459762-Moxalactam,
pubmed-meshheading:6459762-Mutation,
pubmed-meshheading:6459762-Protein Binding,
pubmed-meshheading:6459762-beta-Lactamases
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pubmed:year |
1981
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pubmed:articleTitle |
Penetration of moxalactam into its target proteins in Escherichia coli K-12: comparison of a highly moxalactam resistant mutant with its parent strain.
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pubmed:publicationType |
Journal Article,
Comparative Study
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