| pubmed-article:8982012 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8982012 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:8982012 | lifeskim:mentions | umls-concept:C0008018 | lld:lifeskim |
| pubmed-article:8982012 | lifeskim:mentions | umls-concept:C1180347 | lld:lifeskim |
| pubmed-article:8982012 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8982012 | pubmed:dateCreated | 1997-2-6 | lld:pubmed |
| pubmed-article:8982012 | pubmed:abstractText | During optimal motility conditions, a 1:1 stoichiometry of CheA(L) (654 amino acids) to CheA(S) (557 amino acids) was determined. It was also found that CheZ binding to CheA(S) was inhibited by CheA(L)-CheA(S)-CheW interaction. This suggests that CheA(S) has different functions in the phosphorylating complex (CheA(L)-CheA(S)-CheW) and in the dephosphorylating complex (CheA(S)-CheZ). | lld:pubmed |
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| pubmed-article:8982012 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8982012 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982012 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8982012 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982012 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982012 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8982012 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8982012 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8982012 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:8982012 | pubmed:author | pubmed-author:WangHH | lld:pubmed |
| pubmed-article:8982012 | pubmed:author | pubmed-author:MatsumuraPP | lld:pubmed |
| pubmed-article:8982012 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8982012 | pubmed:volume | 179 | lld:pubmed |
| pubmed-article:8982012 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8982012 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8982012 | pubmed:pagination | 287-9 | lld:pubmed |
| pubmed-article:8982012 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:8982012 | pubmed:meshHeading | pubmed-meshheading:8982012-... | lld:pubmed |
| pubmed-article:8982012 | pubmed:meshHeading | pubmed-meshheading:8982012-... | lld:pubmed |
| pubmed-article:8982012 | pubmed:meshHeading | pubmed-meshheading:8982012-... | lld:pubmed |
| pubmed-article:8982012 | pubmed:meshHeading | pubmed-meshheading:8982012-... | lld:pubmed |
| pubmed-article:8982012 | pubmed:meshHeading | pubmed-meshheading:8982012-... | lld:pubmed |
| pubmed-article:8982012 | pubmed:meshHeading | pubmed-meshheading:8982012-... | lld:pubmed |
| pubmed-article:8982012 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:8982012 | pubmed:articleTitle | Phosphorylating and dephosphorylating protein complexes in bacterial chemotaxis. | lld:pubmed |
| pubmed-article:8982012 | pubmed:affiliation | Department of Microbiology and Immunology, University of Illinois at Chicago, 60612-7344, USA. | lld:pubmed |
| pubmed-article:8982012 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8982012 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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