| pubmed-article:1311202 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1311202 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:1311202 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:1311202 | lifeskim:mentions | umls-concept:C0016055 | lld:lifeskim |
| pubmed-article:1311202 | lifeskim:mentions | umls-concept:C0007577 | lld:lifeskim |
| pubmed-article:1311202 | lifeskim:mentions | umls-concept:C0162807 | lld:lifeskim |
| pubmed-article:1311202 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:1311202 | lifeskim:mentions | umls-concept:C1516050 | lld:lifeskim |
| pubmed-article:1311202 | lifeskim:mentions | umls-concept:C1709061 | lld:lifeskim |
| pubmed-article:1311202 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:1311202 | pubmed:dateCreated | 1992-3-30 | lld:pubmed |
| pubmed-article:1311202 | pubmed:abstractText | The secondary structure of the tenth type III module from human fibronectin has been determined using NMR. This type of module appears many times in a wide variety of proteins. The type III module described here contains an Arg-Gly-Asp sequence known to be involved in cell-cell adhesion. The module was expressed in yeast and characterized by amino acid sequencing and mass spectrometry. 2D and 3D NMR spectroscopy of 15N-labeled protein was used to perform sequence-specific assignment of the spectrum. The secondary structure was defined by patterns of nuclear Overhauser effects, 3JNH-alpha CH spin-spin coupling constants, and amide proton solvent exchange rates. The molecule consists of seven beta-strands in two antiparallel beta-sheets with an immunoglobulin-like fold similar to that predicted for homologous modules in the cytokine receptor super family [Bazan, J. F. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 6934-6938]. The Arg-Gly-Asp sequence is located on a loop between the beta-strands F and G. | lld:pubmed |
| pubmed-article:1311202 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1311202 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1311202 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1311202 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1311202 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1311202 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1311202 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1311202 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1311202 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:1311202 | pubmed:author | pubmed-author:CampbellI DID | lld:pubmed |
| pubmed-article:1311202 | pubmed:author | pubmed-author:BaronMM | lld:pubmed |
| pubmed-article:1311202 | pubmed:author | pubmed-author:BoydJJ | lld:pubmed |
| pubmed-article:1311202 | pubmed:author | pubmed-author:MardonH JHJ | lld:pubmed |
| pubmed-article:1311202 | pubmed:author | pubmed-author:DriscollP CPC | lld:pubmed |
| pubmed-article:1311202 | pubmed:author | pubmed-author:MainA LAL | lld:pubmed |
| pubmed-article:1311202 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1311202 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:1311202 | pubmed:volume | 31 | lld:pubmed |
| pubmed-article:1311202 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1311202 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1311202 | pubmed:pagination | 2068-73 | lld:pubmed |
| pubmed-article:1311202 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1311202 | pubmed:meshHeading | pubmed-meshheading:1311202-... | lld:pubmed |
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| pubmed-article:1311202 | pubmed:meshHeading | pubmed-meshheading:1311202-... | lld:pubmed |
| pubmed-article:1311202 | pubmed:meshHeading | pubmed-meshheading:1311202-... | lld:pubmed |
| pubmed-article:1311202 | pubmed:meshHeading | pubmed-meshheading:1311202-... | lld:pubmed |
| pubmed-article:1311202 | pubmed:meshHeading | pubmed-meshheading:1311202-... | lld:pubmed |
| pubmed-article:1311202 | pubmed:meshHeading | pubmed-meshheading:1311202-... | lld:pubmed |
| pubmed-article:1311202 | pubmed:meshHeading | pubmed-meshheading:1311202-... | lld:pubmed |
| pubmed-article:1311202 | pubmed:meshHeading | pubmed-meshheading:1311202-... | lld:pubmed |
| pubmed-article:1311202 | pubmed:meshHeading | pubmed-meshheading:1311202-... | lld:pubmed |
| pubmed-article:1311202 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1311202 | pubmed:articleTitle | 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin. | lld:pubmed |
| pubmed-article:1311202 | pubmed:affiliation | Department of Biochemistry, University of Oxford, U.K. | lld:pubmed |
| pubmed-article:1311202 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1311202 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:2335 | entrezgene:pubmed | pubmed-article:1311202 | lld:entrezgene |
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