Mathematical modeling of the refractive effect of SMILE surgery in high degree myopia correction

The aim of the study. To develop a mathematical model of changes in corneal refraction during femtosecond laser-assisted lenticule extraction through a small surgical incision and, on this basis, to propose a technology for modified calculation of surgical parameters and to prove its effectiveness. Material and methods. The study included 191 patients with high myopia. They were divided into two groups: group  1 consisted of 55  patients who  were  had  SMILE (SMall Incision Lenticule Extraction) surgery with standard calculations; group  2 included 136 patients who had SMILE surgery with a modified calculation of surgical parameters based on the developed mathematical model of the refractive effect of the surgery. Results. When assessing the refractive effect of patients who were operated using standard technology, it was found that it was possible to achieve a refraction different from emmetropia for ± 0.5 D only in 51 % of cases; in the remaining patients, the planned residual refractive effect was obtained and averaged –1.96 ± 0.29 D. In patients operated using the modified technology, a statistically significantly better refractive result was achieved already on the first day. A refractive error of more than ± 1.0 D was obtained in only 1 % of cases; a deviation from the calculated refraction of ± 0.5 D was achieved in 82 % of cases, with the average values by 1 year –0.24 ± 0.57 D. Conclusions. The developed technology of a modified calculation of the parameters of the SMILE surgery for high myopia correction makes it possible to obtain an optimal refractive effect in compliance with safety rules when the structural and functional parameters of the eye are initially unfavorable for refractive surgery

Circadian oscillator proteins across the kingdoms of life : Structural aspects 06 Biological Sciences 0601 Biochemistry and Cell Biology

Circadian oscillators are networks of biochemical feedback loops that generate 24-hour rhythms and control numerous biological processes in a range of organisms. These periodic rhythms are the result of a complex interplay of interactions among clock components. These components are specific to the organism but share molecular mechanisms that are similar across kingdoms. The elucidation of clock mechanisms in different kingdoms has recently started to attain the level of structural interpretation. A full understanding of these molecular processes requires detailed knowledge, not only of the biochemical and biophysical properties of clock proteins and their interactions, but also the three-dimensional structure of clockwork components. Posttranslational modifications (such as phosphorylation) and protein-protein interactions, have become a central focus of recent research, in particular the complex interactions mediated by the phosphorylation of clock proteins and the formation of multimeric protein complexes that regulate clock genes at transcriptional and translational levels. The three-dimensional structures for the cyanobacterial clock components are well understood, and progress is underway to comprehend the mechanistic details. However, structural recognition of the eukaryotic clock has just begun. This review serves as a primer as the clock communities move towards the exciting realm of structural biology