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. 2009 Sep 10;4(9):e6998. doi: 10.1371/journal.pone.0006998

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Quack et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Comparative β-Gal liquid assays were performed to determine the relative binding strength of the identified interaction partners (n = 6). A representative member of each clone group was re-transformed in yeast cells (AH109) together with TK3-SH3 (light grey) or TK3-US-SH3 (dark grey). The tested clones were (from left to right): diaphanous (SmDia), the eukaryotic translation initiation factor (eIF4γ2b), the BAF60 subunit of the SWI/SNF complex (SWI/SNF-BAF60), the YME1-like metalloprotease (YME1-homologue), the mRNA (guanine-7) methyl transferase (RNA methyl TF), the quinolinate phosphoribosyl-transferase (phosphoribosyl TF), the SH3 binding protein (SH3 domain BP), the Smad protein (Smad2/3), and pericentrin B. As negative control, yeast cells were transformed with TK3-US-SH3 only (bait only).