A versatile plasmid system for reconstitution and analysis of mammalian ubiquitination cascades in yeast

Autor: Rossella Avagliano Trezza, Janny van den Burg, Nico van den Oever, Ben Distel

Publikováno v: Microbial Cell, Vol 5, Iss 3, Pp 150-157 (2017)

Ubiquitination is a posttranslational protein modification that regulates most aspects of cellular life. The sheer number of ubiquitination enzymes that are present in a mammalian cell, over 700 in total, has thus far hampered the analysis of distinc

Externí odkaz: https://doaj.org/article/483030b98fe54a73b9092dc1a22fe8c9

Early adipogenesis is repressed through the newly identified FHL2-NFAT5 signaling complex

Autor: Maria P, Clemente-Olivo, Miguel, Hernández-Quiles, Rinske, Sparrius, Miesje M, van der Stoel, Vera, Janssen, Jayron, Habibe, Janny, van den Burg, Aldo, Jongejan, Paula Sobrevals, Alcaraz, Robert, van Es, Harmjan, Vos, Eric, Kalkhoven, Carlie J M, de Vries

Publikováno v: Cellular Signalling. 104:110587

The LIM-domain-only protein FHL2 is a modulator of signal transduction and has been shown to direct the differentiation of mesenchymal stem cells towards osteoblast and myocyte phenotypes. We hypothesized that FHL2 may simultaneously interfere with t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f596e279469ae781694e1dc398a5e107
https://doi.org/10.1016/j.cellsig.2023.110587

Binding of a proline-independent hydrophobic motif by the Candida albicans Rvs167-3 SH3 domain

Autor: Areti Gkourtsa, Teja Avula, Frans Hochstenbach, Janny van den Burg, Ben Distel

Publikováno v: Microbiological research, 190, 27-36. Urban und Fischer Verlag Jena

Src-homology 3 (SH3) domains are small protein-protein interaction modules. While most SH3 domains bind to proline-x-x-proline (PxxP) containing motifs in their binding partners, some SH3 domains recognize motifs other than proline-based sequences. R

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1d08074a11f27e8a772244b5aa77bfa

Carnitine-dependent transport of acetyl coenzyme A in Candida albicans is essential for growth on nonfermentable carbon sources and contributes to biofilm formation

Autor: Karin Strijbis, Ekaterina Paramonova, Wouter F. Visser, Carlo W.T. van Roermund, Ben Distel, Janny van den Burg, Frank C. Odds, Els Mol, Donna M. MacCallum, Bastiaan P. Krom

Publikováno v: Strijbis, K, van Roermund, C W T, Visser, W F, Mol, E C, van den Burg, J, MacCallum, D M, Odds, F C, Paramonova, E, Krom, B P & Distel, B 2008, ' Carnitine-dependent transport of acetyl coenzyme A in Candida albicans is essential for growth on nonfermentable carbon sources and contributes to biofilm formation ', Eukaryotic Cell, vol. 7, no. 4, pp. 610-8 . https://doi.org/10.1128/EC.00017-08
Eukaryotic Cell, 7(4), 610-8. American Society for Microbiology
Eukaryotic Cell, 7(4), 610-618
Eukaryotic cell, 7(4), 610-618. American Society for Microbiology

In eukaryotes, acetyl coenzyme A (acetyl-CoA) produced during peroxisomal fatty acid β-oxidation needs to be transported to mitochondria for further metabolism. Two parallel pathways for acetyl-CoA transport have been identified in Saccharomyces cer

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94a96af4b80f7f4535f36f2a982a2442
https://doi.org/10.1128/ec.00017-08

RNA binding proteins MRP1 (gBP21) and MRP2 (gBP25) are essential for editing and stability of a subset of mitochondrial mRNAs in procyclic Trypanosoma brucei

Autor: Kenneth Stuart, Rob Benne, Nancy Lewis Ernst, E. Vondrusková, Alena Zíková, Janny van den Burg, Julius Lukeš

Publikováno v: The Journal of Eukaryotic Microbiology. 52:35S-38S

In trypanosomes, MRP1 and MRP2 (previously called gBPx and gBPy, in which x and y indicate the MW of these proteins in a particular species) are guide (g)RNA binding proteins that are part of a large heteromeric complex that may play a role in U-inse

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9887a5051b60d581aecf35f668defeab
https://doi.org/10.1111/j.1550-7408.2005.05202003_5_6.x