946 resultados para Preston family (John Preston, d. 1753)


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Appendixes: A. Abridged genealogy, or pedigree of the ancient noble family of Peyton: p. [311]-336; Isleham Hall, the priory and church, co. Cambridge, England: p. 337-354.--B. Memoranda of the Preston family, by O. Brown: p. [355]-374.--C. Abridged pedigree of the Lewis family: p. 375-379.--D. Extract from the Washington pedigree ... by John Washington: p. [380]-383.

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Mammalian heparanase is an endo-β-glucuronidase associated with cell invasion in cancer metastasis, angiogenesis and inflammation. Heparanase cleaves heparan sulfate proteoglycans in the extracellular matrix and basement membrane, releasing heparin/heparan sulfate oligosaccharides of appreciable size. This in turn causes the release of growth factors, which accelerate tumor growth and metastasis. Heparanase has two glycosaminoglycan-binding domains; however, no three-dimensional structure information is available for human heparanase that can provide insights into how the two domains interact to degrade heparin fragments. We have constructed a new homology model of heparanase that takes into account the most recent structural and bioinformatics data available. Heparin analogs and glycosaminoglycan mimetics were computationally docked into the active site with energetically stable ring conformations and their interaction energies were compared. The resulting docked structures were used to propose a model for substrates and conformer selectivity based on the dimensions of the active site. The docking of substrates and inhibitors indicates the existence of a large binding site extending at least two saccharide units beyond the cleavage site (toward the nonreducing end) and at least three saccharides toward the reducing end (toward heparin-binding site 2). The docking of substrates suggests that heparanase recognizes the N-sulfated and O-sulfated glucosamines at subsite +1 and glucuronic acid at the cleavage site, whereas in the absence of 6-O-sulfation in glucosamine, glucuronic acid is docked at subsite +2. These findings will help us to focus on the rational design of heparanase-inhibiting molecules for anticancer drug development by targeting the two heparin/heparan sulfate recognition domains.

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Small black and white photograph mounted on black card of an unidentified Bell family relative, possibly a sibling of Irene Bell, whose photo is similarly featured. This undated photograph was in the possession of the Rick Bell family, whose relatives include former Black slaves from the United States.According to the 1911 Census of Canada, Irene Bell had the following siblings: Ernest Bell, born 1889 Archie Bell, born 1895 Allen Bell, born 1901 Kenneth Bell, born 1910

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This black and white photograph is believed to be of Albert Sloman (back left), Josephine Sloman (centre) and an unidentified man (right). Iris Sloman, daughter of Albert and Josephine, is thought to be in the front row, centre. The location and date of the photo is unknown, however, it could be in the early 1920s. This photograph was in the possession of Rick Bell, of St. Catharines, son of Iris and Richard Bell. Relatives of the Sloman - Bell family are former Black slaves from the United States.

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Mode of access: Internet.

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Contains selected sermons, letters and poems.

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Mode of access: Internet.

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Appendix: Sermon at the opening of Greenbrier Presbytery.--Semicentenary sermon.--Dr. M. L. Lacy's funeral discourse.