Exploring Health Literacy, Transition Readiness, and Healthcare Utilization in Medicaid Chronically Ill Youth.

Purpose: Youths with special healthcare needs face challenges transitioning from pediatric to adult health care. Understanding possible mechanisms contributing to poor healthcare transition could improve care. This study explores associations between health literacy (HL), transition readiness, and healthcare utilization.

Do health literacy disparities explain racial disparities in family-centered care for youths with special health care needs?

Objective: To explore the relationship among youth health literacy, parental health literacy, and family-centered care (FCC) for youth with special health care needs (YSHCN) and assess potential racial disparities.

Methods: HL and FCC were assessed in 486 Medicaid-enrolled YSHCN (ages 12-18) and their healthcare-responsible parent/caregiver. Analyses assessed racial differences in HL and FCC for parents and youth using logistic regression.

Insights into the base-pairing preferences of 8-oxoguanosine on the ribosome.

Of the four bases, guanine is the most susceptible to oxidation, which results in the formation of 8-oxoguanine (8-oxoG). In protein-free DNA, 8-oxodG adopts the syn conformation more frequently than the anti one. In the syn conformation, 8-oxodG base pairs with dA.

Decoding on the ribosome depends on the structure of the mRNA phosphodiester backbone.

During translation, the ribosome plays an active role in ensuring that mRNA is decoded accurately and rapidly. Recently, biochemical studies have also implicated certain accessory factors in maintaining decoding accuracy. However, it is currently unclear whether the mRNA itself plays an active role in the process beyond its ability to base pair with the tRNA.

Uniformity of Peptide Release Is Maintained by Methylation of Release Factors.

Termination of protein synthesis on the ribosome is catalyzed by release factors (RFs), which share a conserved glycine-glycine-glutamine (GGQ) motif. The glutamine residue is methylated in vivo, but a mechanistic understanding of its contribution to hydrolysis is lacking. Here, we show that the modification, apart from increasing the overall rate of termination on all dipeptides, substantially increases the rate of peptide release on a subset of amino acids.