| pubmed-article:10628867 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10628867 | lifeskim:mentions | umls-concept:C0162741 | lld:lifeskim |
| pubmed-article:10628867 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:10628867 | lifeskim:mentions | umls-concept:C0136073 | lld:lifeskim |
| pubmed-article:10628867 | lifeskim:mentions | umls-concept:C0917877 | lld:lifeskim |
| pubmed-article:10628867 | lifeskim:mentions | umls-concept:C1704708 | lld:lifeskim |
| pubmed-article:10628867 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10628867 | pubmed:issue | 4-5 | lld:pubmed |
| pubmed-article:10628867 | pubmed:dateCreated | 2000-1-31 | lld:pubmed |
| pubmed-article:10628867 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10628867 | pubmed:abstractText | The heterotrimeric protein phosphatase 2A (PP2A) is a component of multiple signaling pathways in eukaryotes. Disruption of PP2A activity in Arabidopsis is known to alter auxin transport and growth response pathways. We demonstrated that the regulatory subunit A of an Arabidopsis PP2A interacts with a novel cyclophilin, ROC7. The gene for this cyclophilin encodes a protein that contains a unique 30-amino acid extension at the N-terminus, which distinguishes the gene product from all previously identified Arabidopsis cyclophilins. Altered forms of ROC7 cyclophilin with mutations in the conserved DENFKL domain did not bind to PP2A. Unlike protein phosphatase 2B, PP2A activity in Arabidopsis extracts was not affected by the presence of the cyclophilin-binding molecule cyclosporin. The ROC7 transcript was expressed to high levels in all tissues tested. Expression of an ROC7 antisense transcript gave rise to increased root growth. These results indicate that cyclophilin may have a role in regulating PP2A activity, by a mechanism that differs from that employed for cyclophilin regulation of PP2B. | lld:pubmed |
| pubmed-article:10628867 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10628867 | pubmed:keyword | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10628867 | pubmed:keyword | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10628867 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10628867 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10628867 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10628867 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10628867 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10628867 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10628867 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10628867 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:10628867 | pubmed:issn | 0026-8925 | lld:pubmed |
| pubmed-article:10628867 | pubmed:author | pubmed-author:SöllDD | lld:pubmed |
| pubmed-article:10628867 | pubmed:author | pubmed-author:JacksonKK | lld:pubmed |
| pubmed-article:10628867 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10628867 | pubmed:volume | 262 | lld:pubmed |
| pubmed-article:10628867 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10628867 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10628867 | pubmed:pagination | 830-8 | lld:pubmed |
| pubmed-article:10628867 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:10628867 | pubmed:meshHeading | pubmed-meshheading:10628867... | lld:pubmed |
| pubmed-article:10628867 | pubmed:meshHeading | pubmed-meshheading:10628867... | lld:pubmed |
| pubmed-article:10628867 | pubmed:meshHeading | pubmed-meshheading:10628867... | lld:pubmed |
| pubmed-article:10628867 | pubmed:meshHeading | pubmed-meshheading:10628867... | lld:pubmed |
| pubmed-article:10628867 | pubmed:meshHeading | pubmed-meshheading:10628867... | lld:pubmed |
| pubmed-article:10628867 | pubmed:meshHeading | pubmed-meshheading:10628867... | lld:pubmed |
| pubmed-article:10628867 | pubmed:meshHeading | pubmed-meshheading:10628867... | lld:pubmed |
| pubmed-article:10628867 | pubmed:meshHeading | pubmed-meshheading:10628867... | lld:pubmed |
| pubmed-article:10628867 | pubmed:meshHeading | pubmed-meshheading:10628867... | lld:pubmed |
| pubmed-article:10628867 | pubmed:meshHeading | pubmed-meshheading:10628867... | lld:pubmed |
| pubmed-article:10628867 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10628867 | pubmed:articleTitle | Mutations in a new Arabidopsis cyclophilin disrupt its interaction with protein phosphatase 2A. | lld:pubmed |
| pubmed-article:10628867 | pubmed:affiliation | Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA. | lld:pubmed |
| pubmed-article:10628867 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10628867 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10628867 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| entrez-gene:835985 | entrezgene:pubmed | pubmed-article:10628867 | lld:entrezgene |
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