| pubmed-article:341159 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:341159 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:341159 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:341159 | lifeskim:mentions | umls-concept:C0243102 | lld:lifeskim |
| pubmed-article:341159 | lifeskim:mentions | umls-concept:C1156162 | lld:lifeskim |
| pubmed-article:341159 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:341159 | lifeskim:mentions | umls-concept:C0243067 | lld:lifeskim |
| pubmed-article:341159 | lifeskim:mentions | umls-concept:C0678227 | lld:lifeskim |
| pubmed-article:341159 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:341159 | pubmed:dateCreated | 1978-3-21 | lld:pubmed |
| pubmed-article:341159 | pubmed:abstractText | A thermosensitive mutant of Escherichia coli K-12 was isolated in which the membrane fractions were deficient both in penicillin-binding protein-1Bs, the major components of protein 1 [Spratt, B.G. & Pardee, A.B. (1975) Nature 254, 516-517] and in activity for in vitro peptidoglycan synthesis. The mutant was also supersensitive to many kinds of beta-lactam antibiotics. All these phenotypic changes were found to be caused by a single mutation (mrc). Genetic mapping studies show that the mrc mutation was located at about 3.3 min on the E. coli chromosome linkage map [Bachmann, B.J., Low, K.B. & Taylor, A.L. (1976) Bacteriol. Rev. 40, 116-167]. Penicillin-binding protein-1Bs seemed to be identical to one of the essential enzymes involved in crosslinking of peptidoglycan and the target of cell-lytic action of penicillins. Possible functions of some other penicillin-binding proteins in compensating for lack of protein-1Bs were also proposed. | lld:pubmed |
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| pubmed-article:341159 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:341159 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:341159 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:341159 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:341159 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:341159 | pubmed:author | pubmed-author:NakajimaSS | lld:pubmed |
| pubmed-article:341159 | pubmed:author | pubmed-author:MatsuhashiMM | lld:pubmed |
| pubmed-article:341159 | pubmed:author | pubmed-author:TamakiSS | lld:pubmed |
| pubmed-article:341159 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:341159 | pubmed:volume | 74 | lld:pubmed |
| pubmed-article:341159 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:341159 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:341159 | pubmed:pagination | 5472-6 | lld:pubmed |
| pubmed-article:341159 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:341159 | pubmed:year | 1977 | lld:pubmed |
| pubmed-article:341159 | pubmed:articleTitle | Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro. | lld:pubmed |
| pubmed-article:341159 | pubmed:publicationType | Journal Article | lld:pubmed |
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