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Citations Search

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Int J Biol Macromol. 97, 460–7. The non-canonical NOTCH1 ligand Delta-like 1 homolog (DLK1) self interacts in mammals. 2017

Traustadóttir, G.Á., Jensen, C.H., Garcia Ramirez, J.J., Beck, H.C., Sheikh, S.P., Andersen, D.C.

Notes: Delta-like 1 homolog (DLK1) functions in cell differentiation during development in both a Notch-dependent and -independent manner. Here, the CheckMate™/Flexi® Mammalian Two-Hybrid System and Dual-Luciferase® Reporter Assay System are used to monitor DLK1-DLK1, DLK1-fibronectin, and DLK1-cysteine-rich FGF receptor interactions. This further illustrates the function of the Notch-independent mechanism in development. (5104)

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J. Virol. doi:10.1128/JVI.01509-08, Epub (ahead of print). Classical swine fever virus can remain virulent after specific elimination of the interferon regulatory factor 3 degrading function of Npro. 2008

Ruggli, N., Summerfield, A., Fiebach, A.R., Guzylack-Piriou, L., Bauhofer, O., Lamm, C.G., Waltersperger, S., Matsuno, K., Liu, L., Gerber, M., Choi, K.H., Hofmann, M.A., Sakoda, Y., Tratschin, J.D.

Notes: These authors studied the effect of specific amino acid substitutions in the Npro gene of swine fever virus. The Npro gene encodes a non-strucutral protein that prevents interferon production by promoting proteasomal degradation of interferon regulatory factor 3 (IRF3). Npro also has an autoprotease function. Deletion of the entire Npro region attenuates virulence. In this study, the authors showed that degradation of IRF3 and autoprotease activity are independent, structurally overlapping functions. In particular, they investigated the effect of specific amino acid substitutions that eliminated IRF3 interaction and degradation, but did not affect autoprotease activity. They showed that removal of IRF3 degradation activity of Npro had only minimal effect on virulence in swine. The pGEM-T Vector was used to clone the amplified Npro gene, and the CheckMate™ Flexi Vector Mammalian Two-Hybrid System was used for protein interaction studies. (3944)

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