| pubmed-article:9119498 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9119498 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:9119498 | lifeskim:mentions | umls-concept:C0008151 | lld:lifeskim |
| pubmed-article:9119498 | lifeskim:mentions | umls-concept:C0023689 | lld:lifeskim |
| pubmed-article:9119498 | lifeskim:mentions | umls-concept:C0678723 | lld:lifeskim |
| pubmed-article:9119498 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:9119498 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9119498 | lifeskim:mentions | umls-concept:C0047355 | lld:lifeskim |
| pubmed-article:9119498 | lifeskim:mentions | umls-concept:C0458003 | lld:lifeskim |
| pubmed-article:9119498 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9119498 | pubmed:dateCreated | 1997-4-24 | lld:pubmed |
| pubmed-article:9119498 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9119498 | pubmed:abstractText | The kdsA and kdsB genes from Chlamydia trachomatis encoding 3-deoxy-D-manno-octulosonate (KDO)-8-phosphate synthetase and CMP-KDO synthetase were identified by functional complementation of temperature-sensitive Salmonella typhimurium mutants, homology to known KDO-8-phosphate synthetase and CMP-KDO synthetase proteins, and in vitro enzyme activity. The kdsA gene was transcribed as part of a polycistronic mRNA with two downstream open reading frames (ORFs). One of these ORFs appeared to encode a membrane-anchored protein, while the second encoded a protein showing homology to the ATP-binding component of periplasmic binding protein-dependent ABC transporters. Transcription of kdsA and kdsB in C. trachomatis was evident within 4 h of initiation of the C. trachomatis infection process and continued throughout the chlamydial life cycle. | lld:pubmed |
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| pubmed-article:9119498 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9119498 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9119498 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9119498 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9119498 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9119498 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9119498 | pubmed:issn | 0019-9567 | lld:pubmed |
| pubmed-article:9119498 | pubmed:author | pubmed-author:WangL LLL | lld:pubmed |
| pubmed-article:9119498 | pubmed:author | pubmed-author:McClartyGG | lld:pubmed |
| pubmed-article:9119498 | pubmed:author | pubmed-author:WylieJ LJL | lld:pubmed |
| pubmed-article:9119498 | pubmed:author | pubmed-author:IliffeE RER | lld:pubmed |
| pubmed-article:9119498 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9119498 | pubmed:volume | 65 | lld:pubmed |
| pubmed-article:9119498 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9119498 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9119498 | pubmed:pagination | 1527-30 | lld:pubmed |
| pubmed-article:9119498 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:9119498 | pubmed:meshHeading | pubmed-meshheading:9119498-... | lld:pubmed |
| pubmed-article:9119498 | pubmed:meshHeading | pubmed-meshheading:9119498-... | lld:pubmed |
| pubmed-article:9119498 | pubmed:meshHeading | pubmed-meshheading:9119498-... | lld:pubmed |
| pubmed-article:9119498 | pubmed:meshHeading | pubmed-meshheading:9119498-... | lld:pubmed |
| pubmed-article:9119498 | pubmed:meshHeading | pubmed-meshheading:9119498-... | lld:pubmed |
| pubmed-article:9119498 | pubmed:meshHeading | pubmed-meshheading:9119498-... | lld:pubmed |
| pubmed-article:9119498 | pubmed:meshHeading | pubmed-meshheading:9119498-... | lld:pubmed |
| pubmed-article:9119498 | pubmed:meshHeading | pubmed-meshheading:9119498-... | lld:pubmed |
| pubmed-article:9119498 | pubmed:meshHeading | pubmed-meshheading:9119498-... | lld:pubmed |
| pubmed-article:9119498 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9119498 | pubmed:articleTitle | Identification, characterization, and developmental regulation of Chlamydia trachomatis 3-deoxy-D-manno-octulosonate (KDO)-8-phosphate synthetase and CMP-KDO synthetase. | lld:pubmed |
| pubmed-article:9119498 | pubmed:affiliation | Department of Medical Microbiology, University of Manitoba, Winnipeg, Canada. | lld:pubmed |
| pubmed-article:9119498 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9119498 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
