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. 2011 May 2;108(20):8233–8238. doi: 10.1073/pnas.1017700108

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Fig. 1. — Phosphorylation states of SRSF1 affect ESE binding affinity. (A) Cartoon representation of SRSF1 domain organization (upper) and coomassie stained SDS/PAGE showing unphosphorylated, hypo-phosphorylated (p-SRSF1), and hyper-phosphorylated SRSF1 (pp-SRSF1). (B and C) Filter binding assay showing the binding of SRSF1 (RRM1/2), SRSF1 (FL), p-SRSF1 (FL), and pp-SRSF1 (FL) to Ron ESE (AGGCGGAGGAAGC) and to mut Ron ESE (mRon ESE; AGGCGGUUGUUGC), respectively. The means and standard deviation (SD) of the results from three independent experiments are shown. (D) Estimated equilibrium dissociation constants (K_d) of SRSF1∶ESE complexes were measured based on FB assay (Ron^a) and EMSA (Ron^b) (see Fig. S1 A–C). K_d was estimated as 50% of bound RNA fraction. ND denotes not determined. SD was determined from three independent experiments.