rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2002-9-17
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pubmed:abstractText |
A mecA-containing Staphylococcus aureus strain was grown in the presence of high concentrations of D-serine, D-threonine, and D-phenylalanine. These growth conditions resulted in the replacement of the carboxyl-terminal (fifth) D-alanine residue of peptidoglycan stem peptides with the D-amino acid present in the growth medium and a reduced ability to grow in the presence of methicillin. The most dramatic effect was seen with D-serine. With 32 mM D-serine, strains that had been able to grow in the presence of 800 micro g of methicillin per ml were only able to grow in the presence of less than 50 micro g/ml. The results also suggest that in S. aureus vancomycin resistance mediated through the incorporation of precursors not terminating in D-alanyl-D-alanine would be mutually exclusive with expression of mecA-mediated methicillin resistance.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-10430946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-11418146,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-1317861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-1510429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-1512190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-1597460,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-1993184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-2045371,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-2345297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-2806258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-3638304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-7034001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-775943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-7872753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-7961632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-8157576,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-8215264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-825075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-8253748,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-8452368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-8478340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-9177719
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Hexosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Methicillin,
http://linkedlifedata.com/resource/pubmed/chemical/Muramoylpentapeptide...,
http://linkedlifedata.com/resource/pubmed/chemical/Penicillin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidoglycan,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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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 |
46
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3151-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12234837-Amino Acids,
pubmed-meshheading:12234837-Bacterial Proteins,
pubmed-meshheading:12234837-Carrier Proteins,
pubmed-meshheading:12234837-Chromatography, High Pressure Liquid,
pubmed-meshheading:12234837-Culture Media,
pubmed-meshheading:12234837-Hexosyltransferases,
pubmed-meshheading:12234837-Mass Spectrometry,
pubmed-meshheading:12234837-Methicillin,
pubmed-meshheading:12234837-Methicillin Resistance,
pubmed-meshheading:12234837-Muramoylpentapeptide Carboxypeptidase,
pubmed-meshheading:12234837-Penicillin-Binding Proteins,
pubmed-meshheading:12234837-Peptides,
pubmed-meshheading:12234837-Peptidoglycan,
pubmed-meshheading:12234837-Peptidyl Transferases,
pubmed-meshheading:12234837-Serine,
pubmed-meshheading:12234837-Staphylococcus aureus,
pubmed-meshheading:12234837-Threonine
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pubmed:year |
2002
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pubmed:articleTitle |
The carboxyl terminus of peptidoglycan stem peptides is a determinant for methicillin resistance in Staphylococcus aureus.
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pubmed:affiliation |
Laboratory of Microbiology, The Rockefeller University, New York, New York 10021, USA. boudewijn.dejonge@astrazeneca.com
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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