pubmed-article:8107139 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C0036126 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C2755837 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C1260969 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:8107139 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
pubmed-article:8107139 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:8107139 | pubmed:dateCreated | 1994-3-23 | lld:pubmed |
pubmed-article:8107139 | pubmed:abstractText | The proximal end of the flagellar basal body consists of a structure called the MS ring complex: two (M and S) rings with different thicknesses closely apposed and a rod extending from the center of the S ring. It has been shown that the MS ring complex consists of multiple copies of single protein FliF (molecular mass 61 kDa). We analyzed the domains of FliF to elucidate how a single protein can be used to construct a complicated particle with several distinct sub-structures. Tryptic digestion of the MS ring complex gave rise to a structure which lacked most of the M ring portion by electron microscopy and showed a major band at 25 kDa by SDS/gel electrophoresis. Amino acid sequence analysis of this band showed that both terminal regions of FliF have been digested, leaving a semi-stable peptide starting from Phe120 and ending at around 400. In addition, we constructed a truncated fliF gene which encodes a FliF lacking 103 amino acid residues from the C terminus. Amplification of the truncated FliF gave rise to a ring complex lacking the rim of the M ring. From these results we assign both terminal regions of FliF to the M ring. Possible domain structures of FliF corresponding to the S ring and the rod are also discussed. | lld:pubmed |
pubmed-article:8107139 | pubmed:language | eng | lld:pubmed |
pubmed-article:8107139 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8107139 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8107139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8107139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8107139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8107139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8107139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8107139 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8107139 | pubmed:month | Feb | lld:pubmed |
pubmed-article:8107139 | pubmed:issn | 0022-2836 | lld:pubmed |
pubmed-article:8107139 | pubmed:author | pubmed-author:AizawaSS | lld:pubmed |
pubmed-article:8107139 | pubmed:author | pubmed-author:UenoTT | lld:pubmed |
pubmed-article:8107139 | pubmed:author | pubmed-author:OosawaKK | lld:pubmed |
pubmed-article:8107139 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8107139 | pubmed:day | 18 | lld:pubmed |
pubmed-article:8107139 | pubmed:volume | 236 | lld:pubmed |
pubmed-article:8107139 | pubmed:geneSymbol | fliF | lld:pubmed |
pubmed-article:8107139 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8107139 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8107139 | pubmed:pagination | 546-55 | lld:pubmed |
pubmed-article:8107139 | pubmed:dateRevised | 2004-1-16 | lld:pubmed |
pubmed-article:8107139 | pubmed:meshHeading | pubmed-meshheading:8107139-... | lld:pubmed |
pubmed-article:8107139 | pubmed:meshHeading | pubmed-meshheading:8107139-... | lld:pubmed |
pubmed-article:8107139 | pubmed:meshHeading | pubmed-meshheading:8107139-... | lld:pubmed |
pubmed-article:8107139 | pubmed:meshHeading | pubmed-meshheading:8107139-... | lld:pubmed |
pubmed-article:8107139 | pubmed:meshHeading | pubmed-meshheading:8107139-... | lld:pubmed |
pubmed-article:8107139 | pubmed:meshHeading | pubmed-meshheading:8107139-... | lld:pubmed |
pubmed-article:8107139 | pubmed:meshHeading | pubmed-meshheading:8107139-... | lld:pubmed |
pubmed-article:8107139 | pubmed:meshHeading | pubmed-meshheading:8107139-... | lld:pubmed |
pubmed-article:8107139 | pubmed:meshHeading | pubmed-meshheading:8107139-... | lld:pubmed |
pubmed-article:8107139 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:8107139 | pubmed:articleTitle | Domain structures of the MS ring component protein (FliF) of the flagellar basal body of Salmonella typhimurium. | lld:pubmed |
pubmed-article:8107139 | pubmed:affiliation | Pharmaceuticals and Biotechnology Laboratory, Japan Energy Co. Ltd., Saitama. | lld:pubmed |
pubmed-article:8107139 | pubmed:publicationType | Journal Article | lld:pubmed |
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