pubmed-article:10503247 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10503247 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
pubmed-article:10503247 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
pubmed-article:10503247 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
pubmed-article:10503247 | lifeskim:mentions | umls-concept:C0015914 | lld:lifeskim |
pubmed-article:10503247 | lifeskim:mentions | umls-concept:C0599455 | lld:lifeskim |
pubmed-article:10503247 | lifeskim:mentions | umls-concept:C1180347 | lld:lifeskim |
pubmed-article:10503247 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:10503247 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:10503247 | lifeskim:mentions | umls-concept:C0332466 | lld:lifeskim |
pubmed-article:10503247 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
pubmed-article:10503247 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:10503247 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:10503247 | pubmed:dateCreated | 1999-11-2 | lld:pubmed |
pubmed-article:10503247 | pubmed:abstractText | Mammalian fertilization depends upon successful binding and fusion between the membranes of the spermatozoon and the oocyte. These processes are thought to be mediated by a series of protein-protein interactions in which sperm antigens known as fertilins are thought to play a key role. Using a recently developed fluorescence technique, the interactions of the oligopeptide sequence corresponding to the fusogenic domain of mouse fertilin-alpha (MF alpha P) and phospholipid vesicles have been investigated. Following stopped-flow mixing, MF alpha P bound rapidly to phospholipid membranes in a co-operative manner with a Hill coefficient of 2.4 and binding rate constants in excess of 1000 s-1. The co-operative nature of the binding process is suggested to represent evidence of a structural mechanism to prevent egg fertilization by immature spermatozoa. The subsequent membrane insertion was found to take place over a longer time period (with rate constants of up to 6.3 s-1), and was linear with respect to peptide concentration. Comparison of these processes with similar time-resolved circular dichroism measurements revealed that changes in peptide secondary structure were very rapid. Fourier transform infrared spectroscopy measurements confirmed changes in the secondary structure of MF alpha P during interaction with PC phospholipid membranes, indicating that the peptide is mainly present in a beta-structure with a small proportion of alpha-helix. These results are consistent with the hypothesis that fertilin-alpha is the fusogenic species with an important role in fertilization. | lld:pubmed |
pubmed-article:10503247 | pubmed:language | eng | lld:pubmed |
pubmed-article:10503247 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10503247 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10503247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10503247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10503247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10503247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10503247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10503247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10503247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10503247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10503247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10503247 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10503247 | pubmed:issn | 0968-7688 | lld:pubmed |
pubmed-article:10503247 | pubmed:author | pubmed-author:JonesRR | lld:pubmed |
pubmed-article:10503247 | pubmed:author | pubmed-author:O'SheaPP | lld:pubmed |
pubmed-article:10503247 | pubmed:author | pubmed-author:CladeraJJ | lld:pubmed |
pubmed-article:10503247 | pubmed:author | pubmed-author:SeniorSS | lld:pubmed |
pubmed-article:10503247 | pubmed:author | pubmed-author:WolfeC ACA | lld:pubmed |
pubmed-article:10503247 | pubmed:author | pubmed-author:LadhaSS | lld:pubmed |
pubmed-article:10503247 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10503247 | pubmed:volume | 16 | lld:pubmed |
pubmed-article:10503247 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10503247 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10503247 | pubmed:pagination | 257-63 | lld:pubmed |
pubmed-article:10503247 | pubmed:dateRevised | 2009-9-2 | lld:pubmed |
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pubmed-article:10503247 | pubmed:articleTitle | Membrane interactions of the putative fusion peptide (MF alpha P) from fertilin-alpha, the mouse sperm protein complex involved in fertilization. | lld:pubmed |
pubmed-article:10503247 | pubmed:affiliation | Institute of Food Research, Norwich Research Park, Colney, UK. | lld:pubmed |
pubmed-article:10503247 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10503247 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10503247 | lld:pubmed |