Zobrazeno 1 - 10 of 16 pro vyhledávání: '"M. R. Kanost"'
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Akademický článek
Exchangeable apolipoproteins of insects share a common structural motif.
Autor: A.F Smith, L.M Owen, L M Strobel, H Chen, M R Kanost, E Hanneman, M A Wells
Publikováno v: Journal of Lipid Research, Vol 35, Iss 11, Pp 1976-1984 (1994)
Elucidation of the secondary structure of the exchangeable apolipoproteins has been hindered by the difficulty in producing crystals suitable for X-ray spectrographic analyses. Consequently, in order to analyze potential structure-function relationsh
Externí odkaz: https://doaj.org/article/875011022ecf4ae5979701e47cacd60e
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3
The structure of a Michaelis serpin-protease complex
Autor: S, Ye, A L, Cech, R, Belmares, R C, Bergstrom, Y, Tong, D R, Corey, M R, Kanost, E J, Goldsmith
Publikováno v: Nature structural biology. 8(11)
Serine protease inhibitors (serpins) regulate the activities of circulating proteases. Serpins inhibit proteases by acylating the serine hydroxyl at their active sites. Before deacylation and complete proteolysis of the serpin can occur, massive conf
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c20ab18c9a31ccd75cf15a0a13f692f0
https://pubmed.ncbi.nlm.nih.gov/11685246
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9
Isolation and characterization of novel inducible serine protease inhibitors from larval hemolymph of the greater wax moth Galleria mellonella
Autor: A C, Fröbius, M R, Kanost, P, Götz, A, Vilcinskas
Publikováno v: European journal of biochemistry. 267(7)
Three inducible serine protease inhibitors (ISPI-1, 2, 3) have been purified from larval hemolymph of greater wax moth larvae, Galleria mellonella, and characterized at a molecular level. These inhibitors were synthesized after larvae were injected w
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::387a55e732e06a889839bf85a63dbe6d
https://pubmed.ncbi.nlm.nih.gov/10727944
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10
Developmental expression of Manduca sexta hemolin
Autor: X Q, Yu, M R, Kanost
Publikováno v: Archives of insect biochemistry and physiology. 42(3)
Hemolin is hemolymph protein that is a member of the immunoglobulin superfamily. Its induced expression after bacterial infection suggests that it functions in the immune response. In this paper, we describe the expression of the Manduca sexta hemoli
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::465bde24ef1d2c17607c9369daed6a10
https://pubmed.ncbi.nlm.nih.gov/10536048
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