To describe the hysteresis nonlinearities in smart actuators, numerous models have been presented in the literature, among which the Preisach operator would be the most effective one due to its capability in capturing multi-loop or sophisticated hysteresis curves. When such an operator is coupled with uncertain nonlinear dynamics, especially in noncanonical form, it is a challenging problem to develop techniques to cancel out the hysteresis effects, and at the same time achieve asymptotic tracking performance. To resolve this problem, in this paper, we investigate the problem of iterative inverse-based adaptive control for an uncertain noncanonical nonlinear systems with unknown input Preiasch hysteresis, and a new adaptive version of the closest match algorithm is proposed to compensate for the Preisach hysteresis. With our scheme, the stability and convergence of the closed-loop system can be established. The effectiveness of the proposed control scheme is illustrated by simulation and experiment results.

Ribosome profiling and mass spectroscopy have identified canonical and noncanonical translation initiation codons (TICs) that are upstream of the main translation initiation site and used to translate oncogenic proteins. Here, we use a Kozak Similarity Score algorithm to find that nearly all of these TICs have flanking nucleotides closely matching the Kozak sequence. Remarkably, the nucleotides flanking alternative noncanonical TICs are frequently closer to the Kozak sequence than the nucleotides flanking TICs used to translate the gene’s main protein. Of note, the 5’ untranslated region (5‘UTR) of cancer-associated genes with an upstream TIC tend to be significantly longer than the same region in genes not associated with cancer. The presence of a longer than typical 5’UTR increases the likelihood of ribosome binding to upstream noncanonical TICs, and may be a distinguishing feature of a number of genes overexpressed in cancer. Noncanonical TICs that are located in the 5’UTR, although thought disadvantageous and suppressed by evolution, may translate oncogenic proteins because of their flanking nucleotides