Supporting better adherence among patients engaged in intermittent self-catherisation.

Coloplast has conducted a qualitative study among health professionals working in the field of continence care. Interviews with health professionals working in urology and rehabilitation provided insights into the barriers to, and supporters of, adherent behaviour-suggesting ways in which health professionals can work with patients performing intermittent self-catheterisation (ISC) to support better adherence. This includes individualised training that addresses individual fears, ensures correct understanding of the body and the treatment, and eliminates misconceptions.

Interaction with RPA is necessary for Rad52 repair center formation and for its mediator activity.

Homologous recombination (HR) is a major DNA repair pathway and therefore essential for maintaining the integrity of the genome. HR is catalyzed by proteins encoded by genes of the RAD52 epistasis group, including the recombinase Rad51 and its mediator Rad52. HR proteins fused with green fluorescent protein form foci at damaged DNA reflecting the assembly of repair centers that harbor a high concentration of repair proteins.

Molecular anatomy of the recombination mediator function of Saccharomyces cerevisiae Rad52.

A helical filament of Rad51 on single-strand DNA (ssDNA), called the presynaptic filament, catalyzes DNA joint formation during homologous recombination. Rad52 facilitates presynaptic filament assembly, and this recombination mediator activity is thought to rely on the interactions of Rad52 with Rad51, the ssDNA-binding protein RPA, and ssDNA. The N-terminal region of Rad52, which has DNA binding activity and an oligomeric structure, is thought to be crucial for mediator activity and recombination.

Rad52 multimerization is important for its nuclear localization in Saccharomyces cerevisiae.

Rad52 is essential for all homologous recombination and DNA double strand break repair events in Saccharomyces cerevisiae. This protein is multifunctional and contains several domains that allow it to interact with DNA as well as with different repair proteins. However, it has been unclear how Rad52 enters the nucleus.