| pubmed-article:16316452 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16316452 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:16316452 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:16316452 | lifeskim:mentions | umls-concept:C1442757 | lld:lifeskim |
| pubmed-article:16316452 | lifeskim:mentions | umls-concept:C0018882 | lld:lifeskim |
| pubmed-article:16316452 | lifeskim:mentions | umls-concept:C1706211 | lld:lifeskim |
| pubmed-article:16316452 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16316452 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:16316452 | pubmed:dateCreated | 2005-11-30 | lld:pubmed |
| pubmed-article:16316452 | pubmed:abstractText | Surfactant protein B (SP-B) is essential for normal lung surfactant function. Theoretical models predict that the disulfide cross-linked, N- and C-terminal domains of SP-B fold as charged amphipathic helices, and suggest that these adjacent helices participate in critical surfactant activities. This hypothesis is tested using a disulfide-linked construct (Mini-B) based on the primary sequences of the N- and C-terminal domains. Consistent with theoretical predictions of the full-length protein, both isotope-enhanced Fourier transform infrared (FTIR) spectroscopy and molecular modeling confirm the presence of charged amphipathic alpha-helices in Mini-B. Similar to that observed with native SP-B, Mini-B in model surfactant lipid mixtures exhibits marked in vitro activity, with spread films showing near-zero minimum surface tensions during cycling using captive bubble surfactometry. In vivo, Mini-B shows oxygenation and dynamic compliance that compare favorably with that of full-length SP-B. Mini-B variants (i.e. reduced disulfides or cationic residues replaced by uncharged residues) or Mini-B fragments (i.e. unlinked N- and C-terminal domains) produced greatly attenuated in vivo and in vitro surfactant properties. Hence, the combination of structure and charge for the amphipathic alpha-helical N- and C-terminal domains are key to SP-B function. | lld:pubmed |
| pubmed-article:16316452 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16316452 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16316452 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16316452 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16316452 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:16316452 | pubmed:issn | 1397-002X | lld:pubmed |
| pubmed-article:16316452 | pubmed:author | pubmed-author:BraunAA | lld:pubmed |
| pubmed-article:16316452 | pubmed:author | pubmed-author:AlonsoCC | lld:pubmed |
| pubmed-article:16316452 | pubmed:author | pubmed-author:BaconDD | lld:pubmed |
| pubmed-article:16316452 | pubmed:author | pubmed-author:GordonL MLM | lld:pubmed |
| pubmed-article:16316452 | pubmed:author | pubmed-author:WaringA JAJ | lld:pubmed |
| pubmed-article:16316452 | pubmed:author | pubmed-author:ShermanM AMA | lld:pubmed |
| pubmed-article:16316452 | pubmed:author | pubmed-author:WaltherF JFJ | lld:pubmed |
| pubmed-article:16316452 | pubmed:author | pubmed-author:AlioLL | lld:pubmed |
| pubmed-article:16316452 | pubmed:author | pubmed-author:HoodHH | lld:pubmed |
| pubmed-article:16316452 | pubmed:author | pubmed-author:ZasadzinskiJ... | lld:pubmed |
| pubmed-article:16316452 | pubmed:author | pubmed-author:Hernandez-Juv... | lld:pubmed |
| pubmed-article:16316452 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16316452 | pubmed:volume | 66 | lld:pubmed |
| pubmed-article:16316452 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16316452 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16316452 | pubmed:pagination | 364-74 | lld:pubmed |
| pubmed-article:16316452 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
| pubmed-article:16316452 | pubmed:meshHeading | pubmed-meshheading:16316452... | lld:pubmed |
| pubmed-article:16316452 | pubmed:meshHeading | pubmed-meshheading:16316452... | lld:pubmed |
| pubmed-article:16316452 | pubmed:meshHeading | pubmed-meshheading:16316452... | lld:pubmed |
| pubmed-article:16316452 | pubmed:meshHeading | pubmed-meshheading:16316452... | lld:pubmed |
| pubmed-article:16316452 | pubmed:meshHeading | pubmed-meshheading:16316452... | lld:pubmed |
| pubmed-article:16316452 | pubmed:meshHeading | pubmed-meshheading:16316452... | lld:pubmed |
| pubmed-article:16316452 | pubmed:meshHeading | pubmed-meshheading:16316452... | lld:pubmed |
| pubmed-article:16316452 | pubmed:meshHeading | pubmed-meshheading:16316452... | lld:pubmed |
| pubmed-article:16316452 | pubmed:meshHeading | pubmed-meshheading:16316452... | lld:pubmed |
| pubmed-article:16316452 | pubmed:meshHeading | pubmed-meshheading:16316452... | lld:pubmed |
| pubmed-article:16316452 | pubmed:meshHeading | pubmed-meshheading:16316452... | lld:pubmed |
| pubmed-article:16316452 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16316452 | pubmed:articleTitle | The role of charged amphipathic helices in the structure and function of surfactant protein B. | lld:pubmed |
| pubmed-article:16316452 | pubmed:affiliation | Department of Medicine, Division of Infectious Diseases, UCLA School of Medicine, Center for Health Sciences, Los Angeles, CA 90095, USA. awaring@ucla.edu | lld:pubmed |
| pubmed-article:16316452 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16316452 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16316452 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16316452 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16316452 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16316452 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16316452 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16316452 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16316452 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16316452 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16316452 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16316452 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16316452 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16316452 | lld:pubmed |
