| pubmed-article:11889039 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C0162741 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C0682323 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C0250581 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C1428564 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C1554080 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C1706198 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:11889039 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:11889039 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:11889039 | pubmed:dateCreated | 2002-3-12 | lld:pubmed |
| pubmed-article:11889039 | pubmed:abstractText | In Arabidopsis, phytochrome A (phyA) is the primary photoreceptor mediating various plant responses to far-red (FR) light. Here we show that phyA signaling involves a combinatorial action of downstream intermediates, which controls overlapping yet distinctive sets of FR responses. FHY3 is a prominent phyA signaling intermediate sharing structural similarity to FAR1, a previously identified phyA signaling component. The fhy3 and far1 mutants display similar yet distinctive defects in phyA signaling; however, overexpression of either FHY3 or FAR1 suppresses the mutant phenotype of both genes. Moreover, overexpression of partial fragments of FHY3 can cause a dominant-negative interference phenotype on phyA signaling that is stronger than those of the fhy3 or far1 null mutants. Further, we demonstrate that FHY3 and FAR1 are capable of homo- and hetero-interaction. Our data indicate that FHY3, together with FAR1, defines a key module in a signaling network underlying phyA-mediated FR light responses. | lld:pubmed |
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| pubmed-article:11889039 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11889039 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11889039 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11889039 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11889039 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11889039 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11889039 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11889039 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11889039 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11889039 | pubmed:author | pubmed-author:WangHaiyangH | lld:pubmed |
| pubmed-article:11889039 | pubmed:author | pubmed-author:DengXing... | lld:pubmed |
| pubmed-article:11889039 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11889039 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11889039 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:11889039 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11889039 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11889039 | pubmed:pagination | 1339-49 | lld:pubmed |
| pubmed-article:11889039 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
| pubmed-article:11889039 | pubmed:meshHeading | pubmed-meshheading:11889039... | lld:pubmed |
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| pubmed-article:11889039 | pubmed:meshHeading | pubmed-meshheading:11889039... | lld:pubmed |
| pubmed-article:11889039 | pubmed:meshHeading | pubmed-meshheading:11889039... | lld:pubmed |
| pubmed-article:11889039 | pubmed:meshHeading | pubmed-meshheading:11889039... | lld:pubmed |
| pubmed-article:11889039 | pubmed:meshHeading | pubmed-meshheading:11889039... | lld:pubmed |
| pubmed-article:11889039 | pubmed:meshHeading | pubmed-meshheading:11889039... | lld:pubmed |
| pubmed-article:11889039 | pubmed:meshHeading | pubmed-meshheading:11889039... | lld:pubmed |
| pubmed-article:11889039 | pubmed:meshHeading | pubmed-meshheading:11889039... | lld:pubmed |
| pubmed-article:11889039 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11889039 | pubmed:articleTitle | Arabidopsis FHY3 defines a key phytochrome A signaling component directly interacting with its homologous partner FAR1. | lld:pubmed |
| pubmed-article:11889039 | pubmed:affiliation | Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520-8104, USA. | lld:pubmed |
| pubmed-article:11889039 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11889039 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
