| pubmed-article:16927206 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16927206 | lifeskim:mentions | umls-concept:C0162740 | lld:lifeskim |
| pubmed-article:16927206 | lifeskim:mentions | umls-concept:C1383501 | lld:lifeskim |
| pubmed-article:16927206 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:16927206 | lifeskim:mentions | umls-concept:C2248806 | lld:lifeskim |
| pubmed-article:16927206 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:16927206 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:16927206 | pubmed:dateCreated | 2006-8-23 | lld:pubmed |
| pubmed-article:16927206 | pubmed:abstractText | Non-phosphorylating glyceraldehyde- 3-phosphate dehydrogenase (NP-GAPDH) is a conserved cytosolic protein found in higher plants. In photosynthetic cells, the enzyme is involved in a shuttle transfer mechanism to export NADPH from the chloroplast to the cytosol. To investigate the role of this enzyme in plant tissues, we characterized a mutant from Arabidopsis thaliana having an insertion at the NP-GAPDH gene locus. The homozygous mutant was determined to be null respect to NP-GAPDH, as it exhibited undetectable levels of both transcription of NP-GAPDH mRNA, protein expression and enzyme activity. Transcriptome analysis demonstrated that the insertion mutant plant shows altered expression of several enzymes involved in carbohydrate metabolism. Significantly, cytosolic phosphorylating (NAD-dependent) glyceraldehyde-3-phosphate dehydrogenase mRNA levels are induced in the mutant, which correlates with an increase in enzyme activity. mRNA levels and enzymatic activity of glucose-6-phosphate dehydrogenase were also elevated, correlating with an increase in NADPH concentration. Moreover, increased ROS levels were measured in the mutant plants. Down-regulation of several glycolytic and photosynthetic genes suggests that NP-GAPDH is important for the efficiency of both metabolic processes. The results presented demonstrate that NP-GAPDH has a relevant role in plant growth and development. | lld:pubmed |
| pubmed-article:16927206 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16927206 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16927206 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16927206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16927206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16927206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16927206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16927206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16927206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16927206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16927206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16927206 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16927206 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16927206 | pubmed:issn | 0167-4412 | lld:pubmed |
| pubmed-article:16927206 | pubmed:author | pubmed-author:IglesiasAlber... | lld:pubmed |
| pubmed-article:16927206 | pubmed:author | pubmed-author:CasatiPaulaP | lld:pubmed |
| pubmed-article:16927206 | pubmed:author | pubmed-author:Gomez-CasatiD... | lld:pubmed |
| pubmed-article:16927206 | pubmed:author | pubmed-author:RiusSebastián... | lld:pubmed |
| pubmed-article:16927206 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16927206 | pubmed:volume | 61 | lld:pubmed |
| pubmed-article:16927206 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16927206 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16927206 | pubmed:pagination | 945-57 | lld:pubmed |
| pubmed-article:16927206 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:meshHeading | pubmed-meshheading:16927206... | lld:pubmed |
| pubmed-article:16927206 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16927206 | pubmed:articleTitle | Characterization of an Arabidopsis thaliana mutant lacking a cytosolic non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase. | lld:pubmed |
| pubmed-article:16927206 | pubmed:affiliation | IIB-INTECH, UNSAM-CONICET, CC 164 (7130), Chascomús, Argentina. | lld:pubmed |
| pubmed-article:16927206 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16927206 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:816962 | entrezgene:pubmed | pubmed-article:16927206 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16927206 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16927206 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16927206 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16927206 | lld:pubmed |
