pubmed-article:19238248 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19238248 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
pubmed-article:19238248 | lifeskim:mentions | umls-concept:C1826944 | lld:lifeskim |
pubmed-article:19238248 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:19238248 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:19238248 | lifeskim:mentions | umls-concept:C1325249 | lld:lifeskim |
pubmed-article:19238248 | lifeskim:mentions | umls-concept:C0814199 | lld:lifeskim |
pubmed-article:19238248 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:19238248 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:19238248 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:19238248 | pubmed:dateCreated | 2009-2-24 | lld:pubmed |
pubmed-article:19238248 | pubmed:abstractText | R-spondin 4 is a secreted protein mainly associated with embryonic nail development. R-spondins have been recently identified as heparin-binding proteins with high affinity. Proteoglycan binding has been associated with both the TSR and the C terminal basic amino acid rich domains. In this paper, molecular modelling techniques were used to construct the model of R-spondin 4 TSR domain based on the structure of the F-spondin TSR domain 4 (30-40 cent sequence identity). Beside a positively charged surface in the TSR domain, presence of the basic amino acid rich domain which could forms a continuous heparin binding surface may explain the high affinity of R-spondins for heparin. Our results provide a framework for understanding the possible regulatory role of heparin in R-spondins signalling. | lld:pubmed |
pubmed-article:19238248 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:19238248 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19238248 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19238248 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:19238248 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19238248 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19238248 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19238248 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19238248 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19238248 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19238248 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19238248 | pubmed:language | eng | lld:pubmed |
pubmed-article:19238248 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19238248 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
pubmed-article:19238248 | pubmed:issn | 0973-2063 | lld:pubmed |
pubmed-article:19238248 | pubmed:author | pubmed-author:AyadiLeilaL | lld:pubmed |
pubmed-article:19238248 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19238248 | pubmed:volume | 3 | lld:pubmed |
pubmed-article:19238248 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19238248 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19238248 | pubmed:pagination | 119-23 | lld:pubmed |
pubmed-article:19238248 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:19238248 | pubmed:articleTitle | Molecular modelling of the TSR domain of R-spondin 4. | lld:pubmed |
pubmed-article:19238248 | pubmed:affiliation | Targets for Diagnosis and Therapy Centre of Biotechnology of Sfax, Sfax, Tunisia 3038. leila.ayadi@ipeis.rnu.tn | lld:pubmed |
pubmed-article:19238248 | pubmed:publicationType | Journal Article | lld:pubmed |