| pubmed-article:11226160 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11226160 | lifeskim:mentions | umls-concept:C0027922 | lld:lifeskim |
| pubmed-article:11226160 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:11226160 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:11226160 | lifeskim:mentions | umls-concept:C1516692 | lld:lifeskim |
| pubmed-article:11226160 | lifeskim:mentions | umls-concept:C2936272 | lld:lifeskim |
| pubmed-article:11226160 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:11226160 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:11226160 | pubmed:dateCreated | 2001-3-15 | lld:pubmed |
| pubmed-article:11226160 | pubmed:abstractText | The frequency (frq) gene, the central component of the frq-based circadian negative feedback loop, regulates various aspects of the circadian clock in NEUROSPORA: However, the biochemical function of its protein products, FRQ, is poorly understood. In this study, we demonstrated that the most conserved region of FRQ forms a coiled-coil domain. FRQ interacts with itself in vivo, and the deletion of the coiled-coil region results in loss of the interaction. Point mutations, which are designed to disrupt the coiled-coil structure, weaken or completely abolish the FRQ self-association and lead to the arrhythmicity of the overt rhythm. Mutations of the FRQ coiled-coil that inhibit self-association also prevent its interaction with two other key components of the NEUROSPORA: circadian clock, namely WC-1 and WC-2, the two PAS domain-containing transcription factors. Taken together, these data strongly suggest that the formation of the FRQ-FRQ and FRQ-WC complexes is essential for the function of the NEUROSPORA: clock. | lld:pubmed |
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| pubmed-article:11226160 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11226160 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11226160 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11226160 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11226160 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11226160 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11226160 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11226160 | pubmed:author | pubmed-author:YangYY | lld:pubmed |
| pubmed-article:11226160 | pubmed:author | pubmed-author:ChengPP | lld:pubmed |
| pubmed-article:11226160 | pubmed:author | pubmed-author:LieII | lld:pubmed |
| pubmed-article:11226160 | pubmed:author | pubmed-author:HeintzenCC | lld:pubmed |
| pubmed-article:11226160 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11226160 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11226160 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:11226160 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11226160 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11226160 | pubmed:pagination | 101-8 | lld:pubmed |
| pubmed-article:11226160 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:meshHeading | pubmed-meshheading:11226160... | lld:pubmed |
| pubmed-article:11226160 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11226160 | pubmed:articleTitle | Coiled-coil domain-mediated FRQ-FRQ interaction is essential for its circadian clock function in Neurospora. | lld:pubmed |
| pubmed-article:11226160 | pubmed:affiliation | Department of Physiology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9040, USA. | lld:pubmed |
| pubmed-article:11226160 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11226160 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
