Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Michael C. Justice"'
Autor:
Fernando Pelaez, Angela Basilio, José R. Tormo, Michael C. Justice, Jennifer Nielsen Kahn, Guy H. Harris, Francisca Vicente, Jesús Martín, Antonio González del Val, Gonzalo Platas, Deborah L. Zink, Javier Collado, Gerald F. Bills
Publikováno v:
Mycological Research. 113:754-770
Sordarins are a class of natural antifungal agents which act by specifically inhibiting fungal protein synthesis through their interaction with the elongation factor 2, EF2. A number of natural sordarins produced by diverse fungi of different classes
Autor:
Jonathan D. Dinman, Anne Carr-Schmid, Jason W. Harger, Mythili S. Shastry, Michael C. Justice, Terri Goss Kinzy, Jane Kwon
Publikováno v:
Virology. 300(1):60-70
Many viruses use programmed −1 ribosomal frameshifting to ensure the correct ratio of viral structural to enzymatic proteins. Alteration of frameshift efficiencies changes these ratios, in turn inhibiting viral particle assembly and virus propagati
Autor:
Michael C. Justice, Karen Carniol, Jennifer Nielsen, Dennis M. Schmatz, Theresa Ku, Ming-Jo Hsu
Publikováno v:
Journal of Biological Chemistry. 274:4869-4875
The natural product sordarin, a tetracyclic diterpene glycoside, selectively inhibits fungal protein synthesis by impairing the function of eukaryotic elongation factor 2 (eEF2). Sordarin and its derivatives bind to the eEF2-ribosome-nucleotide compl
Autor:
Theresa Ku, Jennifer Nielsen, Michael C. Justice, Ming-Jo Hsu, Dennis M. Schmatz, James M. Balkovec, Bruno Tse
Publikováno v:
Journal of Biological Chemistry. 273:3148-3151
Elongation factor 2 (EF2) is an essential protein catalyzing ribosomal translocation during protein synthesis and is highly conserved in all eukaryotes. It is largely interchangeable in translation systems reconstituted from such divergent organisms
Autor:
Michael C. Justice, Arturas Meskauskas, Jennifer Nielsen, Jonathan D. Dinman, Jason W. Harger
Publikováno v:
Virology. 286(1)
Programmed ribosomal frameshifting is utilized by a number of RNA viruses to ensure the correct ratio of viral structural to enzymatic proteins for viral particle assembly. Altering frameshifting efficiencies upsets this ratio, inhibiting virus propa
Autor:
Mythili, Shastry, Jennifer, Nielsen, Theresa, Ku, Ming-Jo, Hsu, Paul, Liberator, Jennifer, Anderson, Dennis, Schmatz, Michael C, Justice
Publikováno v:
Microbiology (Reading, England). 147(Pt 2)
The sordarin class of natural products selectively inhibits fungal protein synthesis by impairing the function of eukaryotic elongation factor 2 (eEF2). Mutations in Saccharomyces cerevisiae eEF2 or the ribosomal stalk protein rpP0 can confer resista
Publikováno v:
Nucleic acids research. 25(23)
The homeodomain (HD) is a conserved sequence-specific DNA-binding motif found in many eukaryotic transcriptional regulatory proteins. Despite the wealth of in vitro data on the mechanism HD proteins use to bind DNA, comparatively little is known abou
Autor:
Mythili S. Shastry, A. Rod Merrill, Michael C. Justice, Rikke Søe, Gregers R. Andersen, Ralph T. Mosley, Jennifer Nielsen-Kahn
Publikováno v:
Aarhus University
Søe, R, Mosley, R T, Justice, M, Nielsen-Kahn, J, Shastry, M, Merrill, A R & Andersen, G R 2007, ' Sordarin derivatives induce a novel conformation of the yeast ribosome translocation factor eEF2 ', Journal of Biological Chemistry, vol. 282, pp. 657-666 .
Søe, R, Mosley, R T, Justice, M, Nielsen-Kahn, J, Shastry, M, Merrill, A R & Andersen, G R 2007, ' Sordarin derivatives induce a novel conformation of the yeast ribosome translocation factor eEF2 ', Journal of Biological Chemistry, vol. 282, pp. 657-666 .
The sordarins are fungal specific inhibitors of the translation factor eEF2, which catalyzes the translocation of tRNA and mRNA after peptide bond formation. We have determined the crystal structures of eEF2 in complex with two novel sordarin derivat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::512b9ae825a41110c3ff38bb648932e3
https://pure.au.dk/portal/en/publications/sordarin-derivatives-induce-a-novel-conformation-of-the-yeast-ribosome-translocation-factor-eef2(3b962080-c88d-11db-bee9-02004c4f4f50).html
https://pure.au.dk/portal/en/publications/sordarin-derivatives-induce-a-novel-conformation-of-the-yeast-ribosome-translocation-factor-eef2(3b962080-c88d-11db-bee9-02004c4f4f50).html