| pubmed-article:2323814 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2323814 | lifeskim:mentions | umls-concept:C0006017 | lld:lifeskim |
| pubmed-article:2323814 | lifeskim:mentions | umls-concept:C0036536 | lld:lifeskim |
| pubmed-article:2323814 | lifeskim:mentions | umls-concept:C0036537 | lld:lifeskim |
| pubmed-article:2323814 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2323814 | lifeskim:mentions | umls-concept:C0001492 | lld:lifeskim |
| pubmed-article:2323814 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:2323814 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:2323814 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:2323814 | pubmed:dateCreated | 1990-5-24 | lld:pubmed |
| pubmed-article:2323814 | pubmed:abstractText | Bordetella pertussis, the etiological agent of whooping cough, synthesizes a calmodulin-sensitive adenylate cyclase that is suspected to play a major role in the virulence of this bacterium. We show that adenylate cyclase synthesized as a 200-kilodalton protein is the product of the cyaA gene and that various virulent Bordetella species secrete this high-molecular-weight polypeptide without apparent proteolytic processing. When submitted to trypsin digestion, the 200-kilodalton protein was converted to a stable 45- to 50-kilodalton species. This corresponds to the size of the enzyme previously purified from a culture supernatant. The molecular heterogeneity reported for the various identified forms of adenylate cyclase could therefore result in part from proteolytic degradation or molecular aggregation of the major 200-kilodalton form of the enzyme. | lld:pubmed |
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| pubmed-article:2323814 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2323814 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2323814 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2323814 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2323814 | pubmed:month | May | lld:pubmed |
| pubmed-article:2323814 | pubmed:issn | 0019-9567 | lld:pubmed |
| pubmed-article:2323814 | pubmed:author | pubmed-author:SakamotoHH | lld:pubmed |
| pubmed-article:2323814 | pubmed:author | pubmed-author:BellalouJJ | lld:pubmed |
| pubmed-article:2323814 | pubmed:author | pubmed-author:LadantDD | lld:pubmed |
| pubmed-article:2323814 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2323814 | pubmed:volume | 58 | lld:pubmed |
| pubmed-article:2323814 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2323814 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2323814 | pubmed:pagination | 1195-200 | lld:pubmed |
| pubmed-article:2323814 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2323814 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2323814 | pubmed:articleTitle | Synthesis and secretion of Bordetella pertussis adenylate cyclase as a 200-kilodalton protein. | lld:pubmed |
| pubmed-article:2323814 | pubmed:affiliation | Unité de Biochimie des Régulations Cellulaires, Institut Pasteur, Paris, France. | lld:pubmed |
| pubmed-article:2323814 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2323814 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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