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pro vyhledávání: '"Christine B. Kofoed"'
Autor:
Birte Vester, Christine B. Kofoed
Publikováno v:
Antimicrobial Agents and Chemotherapy. 46:3339-3342
The antibiotic growth promoter avilamycin inhibits protein synthesis by binding to bacterial ribosomes. Here the binding site is further characterized on Escherichia coli ribosomes. The drug interacts with domain V of 23S rRNA, giving a chemical foot
Publikováno v:
Poulsen, S M, Kofoed, C & Vester, B 2000, ' Inhibition of the ribosomal peptidyl transferase reaction by the mycarose moiety of the antibiotics carbomycin, spiramycin and tylosin. ', Journal of Molecular Biology, vol. 304, no. 3, pp. 471-81 . https://doi.org/10.1006/jmbi.2000.4229
Udgivelsesdato: 2000-Dec-1 Many antibiotics, including the macrolides, inhibit protein synthesis by binding to ribosomes. Only some of the macrolides affect the peptidyl transferase reaction. The 16-member ring macrolide antibiotics carbomycin, spira
Autor:
Ole N. Jensen, Thomas E. Rasmussen, Allan Stensballe, Martin R. Larsen, Steen Gammeltoft, Christine B Kofoed, Majbrit Hjerrild, Nikolaj Blom, Thomas Sicheritz-Pontén, Søren Brunak
Publikováno v:
Technical University of Denmark Orbit
Protein phosphorylation plays a key role in cell regulation and identification of phosphorylation sites is important for understanding their functional significance. Here, we present an artificial neural network algorithm: NetPhosK (http://www.cbs.dt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::549d6ba10dcd2ef382bf14c2521cb1af
https://orbit.dtu.dk/en/publications/e72f22e1-0fe9-4d8a-b9b7-83550c1d22ea
https://orbit.dtu.dk/en/publications/e72f22e1-0fe9-4d8a-b9b7-83550c1d22ea