| pubmed-article:21536014 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21536014 | lifeskim:mentions | umls-concept:C1333543 | lld:lifeskim |
| pubmed-article:21536014 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:21536014 | lifeskim:mentions | umls-concept:C0332197 | lld:lifeskim |
| pubmed-article:21536014 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:21536014 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:21536014 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:21536014 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:21536014 | pubmed:dateCreated | 2011-6-7 | lld:pubmed |
| pubmed-article:21536014 | pubmed:abstractText | The A391E mutation in the transmembrane domain of fibroblast growth factor receptor 3 leads to aberrant development of the cranium. It has been hypothesized that the mutant glutamic acid stabilizes the dimeric receptor due to hydrogen bonding and enhances its ligand-independent activation. We previously tested this hypothesis in lipid bilayers and showed that the mutation stabilizes the isolated transmembrane domain dimer by -1.3°kcal/mol. Here we further test the hypothesis, by investigating the effect of the A391E mutation on the activation of full-length fibroblast growth factor receptor 3 in human embryonic kidney 293T cells in the absence of ligand. We find that the mutation enhances the ligand-independent activation propensity of the receptor by -1.7°kcal/mol. This value is consistent with the observed strength of hydrogen bonds in membranes, and supports the above hypothesis. | lld:pubmed |
| pubmed-article:21536014 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21536014 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21536014 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21536014 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21536014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21536014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21536014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21536014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21536014 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21536014 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:21536014 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:21536014 | pubmed:author | pubmed-author:HortonWilliam... | lld:pubmed |
| pubmed-article:21536014 | pubmed:author | pubmed-author:DegninCatheri... | lld:pubmed |
| pubmed-article:21536014 | pubmed:author | pubmed-author:HristovaKalin... | lld:pubmed |
| pubmed-article:21536014 | pubmed:author | pubmed-author:LaederichMela... | lld:pubmed |
| pubmed-article:21536014 | pubmed:author | pubmed-author:ChenFenghaoF | lld:pubmed |
| pubmed-article:21536014 | pubmed:copyrightInfo | Copyright © 2011 Elsevier B.V. All rights reserved. | lld:pubmed |
| pubmed-article:21536014 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:21536014 | pubmed:volume | 1808 | lld:pubmed |
| pubmed-article:21536014 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21536014 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21536014 | pubmed:pagination | 2045-50 | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:meshHeading | pubmed-meshheading:21536014... | lld:pubmed |
| pubmed-article:21536014 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21536014 | pubmed:articleTitle | The A391E mutation enhances FGFR3 activation in the absence of ligand. | lld:pubmed |
| pubmed-article:21536014 | pubmed:affiliation | Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD 21218, USA. | lld:pubmed |
| pubmed-article:21536014 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21536014 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:21536014 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21536014 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:2261 | entrezgene:pubmed | pubmed-article:21536014 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21536014 | lld:entrezgene |
