| pubmed-article:9742395 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9742395 | lifeskim:mentions | umls-concept:C0178453 | lld:lifeskim |
| pubmed-article:9742395 | lifeskim:mentions | umls-concept:C0795953 | lld:lifeskim |
| pubmed-article:9742395 | lifeskim:mentions | umls-concept:C0018296 | lld:lifeskim |
| pubmed-article:9742395 | lifeskim:mentions | umls-concept:C0061928 | lld:lifeskim |
| pubmed-article:9742395 | lifeskim:mentions | umls-concept:C1413255 | lld:lifeskim |
| pubmed-article:9742395 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:9742395 | lifeskim:mentions | umls-concept:C1748481 | lld:lifeskim |
| pubmed-article:9742395 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:9742395 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:9742395 | pubmed:dateCreated | 1998-11-18 | lld:pubmed |
| pubmed-article:9742395 | pubmed:abstractText | Spatial and temporal control of cytokinesis ensures the accurate transmission of genetic material and the correct development of multicellular organisms. An excellent model system in which to study cytokinesis is Schizosaccharomyces pombe because there are similarities between cytokinesis in S. pombe and mammals and because genes involved in S. pombe cytokinesis have been characterized. In particular, formation of the septum is positively regulated by the Spg1 GTPase and its effector, the Cdc7 kinase. Septation is negatively regulated by Cdc16, a protein similar to GTPase-activating proteins (GAPs) for Ypt GTPases, and by Byr4, a protein of unknown biochemical function. This study investigates the relationship between Byr4, Cdc16, and Spg1. | lld:pubmed |
| pubmed-article:9742395 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9742395 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9742395 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9742395 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9742395 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9742395 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9742395 | pubmed:issn | 0960-9822 | lld:pubmed |
| pubmed-article:9742395 | pubmed:author | pubmed-author:WongKK | lld:pubmed |
| pubmed-article:9742395 | pubmed:author | pubmed-author:ArmstrongJJ | lld:pubmed |
| pubmed-article:9742395 | pubmed:author | pubmed-author:Balasubramani... | lld:pubmed |
| pubmed-article:9742395 | pubmed:author | pubmed-author:AlbrightC FCF | lld:pubmed |
| pubmed-article:9742395 | pubmed:author | pubmed-author:FurgeK AKA | lld:pubmed |
| pubmed-article:9742395 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9742395 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:9742395 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:9742395 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9742395 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9742395 | pubmed:pagination | 947-54 | lld:pubmed |
| pubmed-article:9742395 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9742395 | pubmed:meshHeading | pubmed-meshheading:9742395-... | lld:pubmed |
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| pubmed-article:9742395 | pubmed:meshHeading | pubmed-meshheading:9742395-... | lld:pubmed |
| pubmed-article:9742395 | pubmed:meshHeading | pubmed-meshheading:9742395-... | lld:pubmed |
| pubmed-article:9742395 | pubmed:meshHeading | pubmed-meshheading:9742395-... | lld:pubmed |
| pubmed-article:9742395 | pubmed:meshHeading | pubmed-meshheading:9742395-... | lld:pubmed |
| pubmed-article:9742395 | pubmed:meshHeading | pubmed-meshheading:9742395-... | lld:pubmed |
| pubmed-article:9742395 | pubmed:meshHeading | pubmed-meshheading:9742395-... | lld:pubmed |
| pubmed-article:9742395 | pubmed:meshHeading | pubmed-meshheading:9742395-... | lld:pubmed |
| pubmed-article:9742395 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9742395 | pubmed:articleTitle | Byr4 and Cdc16 form a two-component GTPase-activating protein for the Spg1 GTPase that controls septation in fission yeast. | lld:pubmed |
| pubmed-article:9742395 | pubmed:affiliation | Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA. | lld:pubmed |
| pubmed-article:9742395 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9742395 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9742395 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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