| pubmed-article:12074582 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12074582 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
| pubmed-article:12074582 | lifeskim:mentions | umls-concept:C0213553 | lld:lifeskim |
| pubmed-article:12074582 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:12074582 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:12074582 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12074582 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:12074582 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:12074582 | pubmed:dateCreated | 2002-6-20 | lld:pubmed |
| pubmed-article:12074582 | pubmed:abstractText | The solution structure of the EGF-like domain of betacellulin (BTCe), a newly discovered member of the epidermal growth factor (EGF) family, has been determined using two-dimensional nuclear magnetic resonance spectroscopy. This is the first report to identify the solution structure of the EGF-family ligand monomers that interact with both ErbB-1 and ErbB-4. The solution structure of BTCe was calculated using 538 NMR-derived restraints. The overall structure of BTCe was stabilized by three disulfide bonds, a hydrophobic core, and 23 hydrogen bonds. It appears that BTCe is comprised of five beta-strands and one short 3(10) helical turn. The secondary structural elements of BTCe are basically similar to those of the other EGF-family proteins, except that several significant variations of the structural properties were found. It is suggested that the structural variations between BTCe and the other EGF-family ligands may affect the specific receptor-recognition properties of EGF-family ligands. | lld:pubmed |
| pubmed-article:12074582 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12074582 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12074582 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12074582 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12074582 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12074582 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12074582 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12074582 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12074582 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12074582 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12074582 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:12074582 | pubmed:author | pubmed-author:AizawaTomoyas... | lld:pubmed |
| pubmed-article:12074582 | pubmed:author | pubmed-author:KawanoKeiichi... | lld:pubmed |
| pubmed-article:12074582 | pubmed:author | pubmed-author:TadaHirokoH | lld:pubmed |
| pubmed-article:12074582 | pubmed:author | pubmed-author:YamadaHidenor... | lld:pubmed |
| pubmed-article:12074582 | pubmed:author | pubmed-author:SenoMasaharuM | lld:pubmed |
| pubmed-article:12074582 | pubmed:author | pubmed-author:MiuraKazunori... | lld:pubmed |
| pubmed-article:12074582 | pubmed:author | pubmed-author:DouraHidekiH | lld:pubmed |
| pubmed-article:12074582 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12074582 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:12074582 | pubmed:volume | 294 | lld:pubmed |
| pubmed-article:12074582 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12074582 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12074582 | pubmed:pagination | 1040-6 | lld:pubmed |
| pubmed-article:12074582 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:meshHeading | pubmed-meshheading:12074582... | lld:pubmed |
| pubmed-article:12074582 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12074582 | pubmed:articleTitle | Solution structure of betacellulin, a new member of EGF-family ligands. | lld:pubmed |
| pubmed-article:12074582 | pubmed:affiliation | Bio-oriented Technology Research Advancement Institution, 1-40-2 Nisshin, Saitama, Saitama 331-8537, Japan. | lld:pubmed |
| pubmed-article:12074582 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12074582 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:685 | entrezgene:pubmed | pubmed-article:12074582 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:12074582 | lld:entrezgene |
