pubmed-article:14617146 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14617146 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:14617146 | lifeskim:mentions | umls-concept:C0038410 | lld:lifeskim |
pubmed-article:14617146 | lifeskim:mentions | umls-concept:C0007586 | lld:lifeskim |
pubmed-article:14617146 | lifeskim:mentions | umls-concept:C0070235 | lld:lifeskim |
pubmed-article:14617146 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
pubmed-article:14617146 | lifeskim:mentions | umls-concept:C1293097 | lld:lifeskim |
pubmed-article:14617146 | lifeskim:mentions | umls-concept:C1979900 | lld:lifeskim |
pubmed-article:14617146 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
pubmed-article:14617146 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:14617146 | pubmed:dateCreated | 2003-11-17 | lld:pubmed |
pubmed-article:14617146 | pubmed:abstractText | The bacterial peptidoglycan, the main component of the cell wall, is synthesized by the penicillin-binding proteins (PBPs). We used immunofluorescence microscopy to determine the cellular localization of all the high molecular weight PBPs of the human pathogen Streptococcus pneumoniae, for a wild type and for several PBP-deficient strains. Progression through the cell cycle was investigated by the simultaneous labelling of DNA and the FtsZ protein. Our main findings are: (i) the temporal dissociation of cell wall synthesis, inferred by the localization of PBP2x and PBP1a, from the constriction of the FtsZ-ring; (ii) the localization of PBP2b and PBP2a at duplicated equatorial sites indicating the existence of peripheral peptidoglycan synthesis, which implies a similarity between the mechanism of cell division in bacilli and streptococci; (iii) the abnormal localization of some class A PBPs in PBP-defective mutants which may explain the apparent redundancy of these proteins in S. pneumoniae. | lld:pubmed |
pubmed-article:14617146 | pubmed:language | eng | lld:pubmed |
pubmed-article:14617146 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14617146 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14617146 | pubmed:month | Nov | lld:pubmed |
pubmed-article:14617146 | pubmed:issn | 0950-382X | lld:pubmed |
pubmed-article:14617146 | pubmed:author | pubmed-author:VernetThierry... | lld:pubmed |
pubmed-article:14617146 | pubmed:author | pubmed-author:ZapunAndréA | lld:pubmed |
pubmed-article:14617146 | pubmed:author | pubmed-author:DidebergOttoO | lld:pubmed |
pubmed-article:14617146 | pubmed:author | pubmed-author:MorlotCécileC | lld:pubmed |
pubmed-article:14617146 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14617146 | pubmed:volume | 50 | lld:pubmed |
pubmed-article:14617146 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14617146 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14617146 | pubmed:pagination | 845-55 | lld:pubmed |
pubmed-article:14617146 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:14617146 | pubmed:meshHeading | pubmed-meshheading:14617146... | lld:pubmed |
pubmed-article:14617146 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:14617146 | pubmed:articleTitle | Growth and division of Streptococcus pneumoniae: localization of the high molecular weight penicillin-binding proteins during the cell cycle. | lld:pubmed |
pubmed-article:14617146 | pubmed:affiliation | Institut de Biologie Structurale J. -P. Ebel (CEA/CNRS/UJF, UMR 5075), 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France. | lld:pubmed |
pubmed-article:14617146 | pubmed:publicationType | Journal Article | lld:pubmed |
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