69 research outputs found

    Adaptive Mixture Methods Based on Bregman Divergences

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    We investigate adaptive mixture methods that linearly combine outputs of mm constituent filters running in parallel to model a desired signal. We use "Bregman divergences" and obtain certain multiplicative updates to train the linear combination weights under an affine constraint or without any constraints. We use unnormalized relative entropy and relative entropy to define two different Bregman divergences that produce an unnormalized exponentiated gradient update and a normalized exponentiated gradient update on the mixture weights, respectively. We then carry out the mean and the mean-square transient analysis of these adaptive algorithms when they are used to combine outputs of mm constituent filters. We illustrate the accuracy of our results and demonstrate the effectiveness of these updates for sparse mixture systems.Comment: Submitted to Digital Signal Processing, Elsevier; IEEE.or

    hnRNP A1 and hnRNP F Modulate the Alternative Splicing of Exon 11 of the Insulin Receptor Gene

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    Exon 11 of the insulin receptor gene (INSR) is alternatively spliced in a developmentally and tissue-specific manner. Linker scanning mutations in a 5′ GA-rich enhancer in intron 10 identified AGGGA sequences that are important for enhancer function. Using RNA-affinity purification and mass spectrometry, we identified hnRNP F and hnRNP A1 binding to these AGGGA sites and also to similar motifs at the 3′ end of the intron. The hnRNPs have opposite functional effects with hnRNP F promoting and hnRNP A1 inhibiting exon 11 inclusion, and deletion of the GA-rich elements eliminates both effects. We also observed specific binding of hnRNP A1 to the 5′ splice site of intron 11. The SR protein SRSF1 (SF2/ASF) co-purified on the GA-rich enhancer and, interestingly, also competes with hnRNP A1 for binding to the splice site. A point mutation -3U→C decreases hnRNP A1 binding, increases SRSF1 binding and renders the exon constitutive. Lastly, our data point to a functional interaction between hnRNP F and SRSF1 as a mutant that eliminates SRSF1 binding to exon 11, or a SRSF1 knockdown, which prevents the stimulatory effect of hnRNP F over expression
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