pubmed-article:16321658 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16321658 | lifeskim:mentions | umls-concept:C0596981 | lld:lifeskim |
pubmed-article:16321658 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:16321658 | lifeskim:mentions | umls-concept:C0034987 | lld:lifeskim |
pubmed-article:16321658 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:16321658 | pubmed:dateCreated | 2005-12-2 | lld:pubmed |
pubmed-article:16321658 | pubmed:abstractText | The Mfap2 gene encodes the microfibril-associated glycoprotein-1 (MAGP1), an extracellular matrix protein of microfibrillar structures. The gene is transcribed from a major transcription start site embedded in a CpG island. Mapping of transcriptionally active regions in the 5' flanking sequence identified a region, located between nucleotides -339 and -109 as the Mfap2 basal promoter. Site-directed and random mutagenesis demonstrated that a KLF sequence motif at -256/-270, an E-box at -222/-229, and a GC-box at -117/-125, are critical for the promoter function. Using electrophoresis mobility shift assays, we find that the KLF motif mediates the binding of GKLF/KLF4, whereas the E-box is a target for both Upstream Stimulatory Factors 1 and 2, and the GC box at -117/-125 forms complexes with Sp1 and Sp3, but not with Sp4 or AP2alpha. A sequence element spanning position -150 may represent the binding motif of an uncharacterized transcription factor. The basal transcriptional regulation of Mfap2 in muscle cells is discussed. | lld:pubmed |
pubmed-article:16321658 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16321658 | pubmed:language | eng | lld:pubmed |
pubmed-article:16321658 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16321658 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16321658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16321658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16321658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16321658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16321658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16321658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16321658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16321658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16321658 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16321658 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16321658 | pubmed:month | Dec | lld:pubmed |
pubmed-article:16321658 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:16321658 | pubmed:author | pubmed-author:MechamRobert... | lld:pubmed |
pubmed-article:16321658 | pubmed:author | pubmed-author:SegadeFernand... | lld:pubmed |
pubmed-article:16321658 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16321658 | pubmed:day | 20 | lld:pubmed |
pubmed-article:16321658 | pubmed:volume | 1731 | lld:pubmed |
pubmed-article:16321658 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16321658 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16321658 | pubmed:pagination | 215-24 | lld:pubmed |
pubmed-article:16321658 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:meshHeading | pubmed-meshheading:16321658... | lld:pubmed |
pubmed-article:16321658 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:16321658 | pubmed:articleTitle | Regulatory elements of microfibril-associated glycoprotein-1 gene expression in muscle cells. | lld:pubmed |
pubmed-article:16321658 | pubmed:affiliation | Department of Internal Medicine, Wake Forest University School of Medicine, Winston-Salem, NC 27157, USA. fsegade@wfubmc.edu | lld:pubmed |
pubmed-article:16321658 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16321658 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
entrez-gene:17150 | entrezgene:pubmed | pubmed-article:16321658 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16321658 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16321658 | lld:pubmed |