| pubmed-article:17240087 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17240087 | lifeskim:mentions | umls-concept:C0162740 | lld:lifeskim |
| pubmed-article:17240087 | lifeskim:mentions | umls-concept:C0038435 | lld:lifeskim |
| pubmed-article:17240087 | lifeskim:mentions | umls-concept:C0040711 | lld:lifeskim |
| pubmed-article:17240087 | lifeskim:mentions | umls-concept:C1257945 | lld:lifeskim |
| pubmed-article:17240087 | lifeskim:mentions | umls-concept:C0039476 | lld:lifeskim |
| pubmed-article:17240087 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:17240087 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:17240087 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:17240087 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:17240087 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:17240087 | pubmed:dateCreated | 2007-4-2 | lld:pubmed |
| pubmed-article:17240087 | pubmed:abstractText | In eukaryotes, E3 ubiquitin ligases (E3s) mediate the ubiquitylation of proteins that are destined for degradation by the ubiquitin-proteasome system. In SKP1/CDC53/F-box protein (SCF)-type E3 complexes, the interchangeable F-box protein confers specificity to the E3 ligase through direct physical interactions with the degradation substrate. The vast majority of the approximately 700 F-box proteins from the plant model organism Arabidopsis thaliana remain to be characterized. Here, we investigate the previously uncharacterized and evolutionarily conserved Arabidopsis F-box protein 7 (AtFBP7), which is encoded by a unique gene in Arabidopsis (At1g21760). Several apparent fbp7 loss-of-function alleles do not have an obvious phenotype. AtFBP7 is ubiquitously expressed and its expression is induced after cold and heat stress. When following up on a reported co-purification of the eukaryotic elongation factor-2 (eEF-2) with YLR097c, the apparent budding yeast orthologue of AtFBP7, we discovered a general defect in protein biosynthesis after cold and heat stress in fbp7 mutants. Thus, our findings suggest that AtFBP7 is required for protein synthesis during temperature stress. | lld:pubmed |
| pubmed-article:17240087 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17240087 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17240087 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17240087 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17240087 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17240087 | pubmed:month | May | lld:pubmed |
| pubmed-article:17240087 | pubmed:issn | 0378-1119 | lld:pubmed |
| pubmed-article:17240087 | pubmed:author | pubmed-author:Schwechheimer... | lld:pubmed |
| pubmed-article:17240087 | pubmed:author | pubmed-author:KretschThomas... | lld:pubmed |
| pubmed-article:17240087 | pubmed:author | pubmed-author:MarroccoKatia... | lld:pubmed |
| pubmed-article:17240087 | pubmed:author | pubmed-author:Calderón-Vill... | lld:pubmed |
| pubmed-article:17240087 | pubmed:author | pubmed-author:NillCarolaC | lld:pubmed |
| pubmed-article:17240087 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17240087 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17240087 | pubmed:volume | 392 | lld:pubmed |
| pubmed-article:17240087 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17240087 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17240087 | pubmed:pagination | 106-16 | lld:pubmed |
| pubmed-article:17240087 | pubmed:meshHeading | pubmed-meshheading:17240087... | lld:pubmed |
| pubmed-article:17240087 | pubmed:meshHeading | pubmed-meshheading:17240087... | lld:pubmed |
| pubmed-article:17240087 | pubmed:meshHeading | pubmed-meshheading:17240087... | lld:pubmed |
| pubmed-article:17240087 | pubmed:meshHeading | pubmed-meshheading:17240087... | lld:pubmed |
| pubmed-article:17240087 | pubmed:meshHeading | pubmed-meshheading:17240087... | lld:pubmed |
| pubmed-article:17240087 | pubmed:meshHeading | pubmed-meshheading:17240087... | lld:pubmed |
| pubmed-article:17240087 | pubmed:meshHeading | pubmed-meshheading:17240087... | lld:pubmed |
| pubmed-article:17240087 | pubmed:meshHeading | pubmed-meshheading:17240087... | lld:pubmed |
| pubmed-article:17240087 | pubmed:meshHeading | pubmed-meshheading:17240087... | lld:pubmed |
| pubmed-article:17240087 | pubmed:meshHeading | pubmed-meshheading:17240087... | lld:pubmed |
| pubmed-article:17240087 | pubmed:meshHeading | pubmed-meshheading:17240087... | lld:pubmed |
| pubmed-article:17240087 | pubmed:meshHeading | pubmed-meshheading:17240087... | lld:pubmed |
| pubmed-article:17240087 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17240087 | pubmed:articleTitle | The evolutionarily conserved Arabidopsis thaliana F-box protein AtFBP7 is required for efficient translation during temperature stress. | lld:pubmed |
| pubmed-article:17240087 | pubmed:affiliation | Department of Developmental Genetics, Centre for Plant Molecular Biology, Tübingen University, Auf der Morgenstelle 5, 72076 Tübingen, Germany. | lld:pubmed |
| pubmed-article:17240087 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17240087 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:814885 | entrezgene:pubmed | pubmed-article:17240087 | lld:entrezgene |
| entrez-gene:838780 | entrezgene:pubmed | pubmed-article:17240087 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17240087 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17240087 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17240087 | lld:pubmed |
