pubmed-article:18289114 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18289114 | lifeskim:mentions | umls-concept:C0016026 | lld:lifeskim |
pubmed-article:18289114 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
pubmed-article:18289114 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
pubmed-article:18289114 | lifeskim:mentions | umls-concept:C0037506 | lld:lifeskim |
pubmed-article:18289114 | lifeskim:mentions | umls-concept:C0005553 | lld:lifeskim |
pubmed-article:18289114 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
pubmed-article:18289114 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:18289114 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
pubmed-article:18289114 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:18289114 | pubmed:dateCreated | 2008-2-21 | lld:pubmed |
pubmed-article:18289114 | pubmed:abstractText | The current article describes the biophysical characterization and folding studies of fibroblast growth factor homologous factor-1b (FHF-1b) in comparison with acidic fibroblast growth factor (FGF-1). Our data indicates that FHF-1 is significantly more stable than FGF-1. The folding mechanism of these two proteins seems to be different although they share high degree of sequence and structural similarity. FHF-1 unfolds through stable intermediate state while unfolding of FGF-1 is two-state. Interestingly, low concentration of sodium dodecyl sulfate (SDS) drives the folding pathway of FHF-1b to two-state. | lld:pubmed |
pubmed-article:18289114 | pubmed:language | eng | lld:pubmed |
pubmed-article:18289114 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18289114 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18289114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18289114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18289114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18289114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18289114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18289114 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18289114 | pubmed:issn | 0929-8665 | lld:pubmed |
pubmed-article:18289114 | pubmed:author | pubmed-author:DubeyVikash... | lld:pubmed |
pubmed-article:18289114 | pubmed:author | pubmed-author:PandeMonuM | lld:pubmed |
pubmed-article:18289114 | pubmed:author | pubmed-author:JagannadhamMe... | lld:pubmed |
pubmed-article:18289114 | pubmed:author | pubmed-author:SinghBishal... | lld:pubmed |
pubmed-article:18289114 | pubmed:author | pubmed-author:SarkarNandini... | lld:pubmed |
pubmed-article:18289114 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18289114 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:18289114 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18289114 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18289114 | pubmed:pagination | 215-8 | lld:pubmed |
pubmed-article:18289114 | pubmed:meshHeading | pubmed-meshheading:18289114... | lld:pubmed |
pubmed-article:18289114 | pubmed:meshHeading | pubmed-meshheading:18289114... | lld:pubmed |
pubmed-article:18289114 | pubmed:meshHeading | pubmed-meshheading:18289114... | lld:pubmed |
pubmed-article:18289114 | pubmed:meshHeading | pubmed-meshheading:18289114... | lld:pubmed |
pubmed-article:18289114 | pubmed:meshHeading | pubmed-meshheading:18289114... | lld:pubmed |
pubmed-article:18289114 | pubmed:meshHeading | pubmed-meshheading:18289114... | lld:pubmed |
pubmed-article:18289114 | pubmed:meshHeading | pubmed-meshheading:18289114... | lld:pubmed |
pubmed-article:18289114 | pubmed:meshHeading | pubmed-meshheading:18289114... | lld:pubmed |
pubmed-article:18289114 | pubmed:meshHeading | pubmed-meshheading:18289114... | lld:pubmed |
pubmed-article:18289114 | pubmed:meshHeading | pubmed-meshheading:18289114... | lld:pubmed |
pubmed-article:18289114 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18289114 | pubmed:articleTitle | Biophysical characterization of fibroblast growth factor homologous factor-1b (FHF-1b): sodium dodecyl sulfate promotes two state folding. | lld:pubmed |
pubmed-article:18289114 | pubmed:affiliation | Department of Biotechnology, Indian Institute of Technology, Guwahati-781039, Assam, India. vdubey@iitg.ernet.in | lld:pubmed |
pubmed-article:18289114 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18289114 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:2257 | entrezgene:pubmed | pubmed-article:18289114 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18289114 | lld:entrezgene |