| pubmed-article:10629199 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10629199 | lifeskim:mentions | umls-concept:C0085448 | lld:lifeskim |
| pubmed-article:10629199 | lifeskim:mentions | umls-concept:C0008010 | lld:lifeskim |
| pubmed-article:10629199 | lifeskim:mentions | umls-concept:C0008018 | lld:lifeskim |
| pubmed-article:10629199 | lifeskim:mentions | umls-concept:C0029073 | lld:lifeskim |
| pubmed-article:10629199 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:10629199 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:10629199 | lifeskim:mentions | umls-concept:C1546856 | lld:lifeskim |
| pubmed-article:10629199 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10629199 | pubmed:dateCreated | 2000-2-4 | lld:pubmed |
| pubmed-article:10629199 | pubmed:abstractText | The degradation of the McpA chemoreceptor in Caulobacter crescentus accompanies the swarmer cell to the stalked-cell differentiation event. To further analyze the requirements for its degradation, we have constructed a series of strains that have deletions in the mcpA gene and in the mcpA chemotaxis operon. Internal deletions of the mcpA gene demonstrate that the highly conserved domain (signalling unit) and the methylation domains are not required for cell cycle-regulated proteolysis. The deletion of the chemotaxis operon, which is absolutely required for chemotaxis and McpA chemoreceptor methylation, has no effect on McpA proteolysis. | lld:pubmed |
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| pubmed-article:10629199 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10629199 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10629199 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10629199 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10629199 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:10629199 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:10629199 | pubmed:author | pubmed-author:AlleyM RMR | lld:pubmed |
| pubmed-article:10629199 | pubmed:author | pubmed-author:UGONV AVA | lld:pubmed |
| pubmed-article:10629199 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10629199 | pubmed:volume | 182 | lld:pubmed |
| pubmed-article:10629199 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10629199 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10629199 | pubmed:pagination | 504-7 | lld:pubmed |
| pubmed-article:10629199 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:10629199 | pubmed:meshHeading | pubmed-meshheading:10629199... | lld:pubmed |
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| pubmed-article:10629199 | pubmed:meshHeading | pubmed-meshheading:10629199... | lld:pubmed |
| pubmed-article:10629199 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10629199 | pubmed:articleTitle | Proteolysis of the McpA chemoreceptor does not require the Caulobacter major chemotaxis operon. | lld:pubmed |
| pubmed-article:10629199 | pubmed:affiliation | Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY, United Kingdom. | lld:pubmed |
| pubmed-article:10629199 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10629199 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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