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4. Disentangling the Roles of Parental Monitoring and Family Conflict in Adolescents' Management of Type 1 Diabetes.

Author

Hilliard, Marisa E., Holmes, Clarissa S., Chen, Rusan, Maher, Kathryn, Robinson, Elizabeth, and Streisand, Randi

Abstract

Objective: Less parental monitoring of adolescents' diabetes self-care and more family conflict are each associated with poorer diabetes outcomes. However, little is known about how these two family factors relate with one another in the context of self-care and glycemic control. Diabetes self-care was evaluated as a mediator of the associations among parental monitoring, family conflict, and glycemic control in early adolescents with type 1 diabetes. Methods: Adolescent-parent dyads (n = 257) reported on the frequency of parental monitoring, family conflict, and diabetes self-care. Hemoglobin Ale was abstracted from medical charts. Structural equation modeling was used for mediation analysis. Results: A mediation model linking parental involvement and family conflict with Ale through diabetes self-care fit the data well. Monitoring and conflict were inversely correlated (ß = -0.23, p < .05) and each demonstrated indirect associations with Ale (standardized indirect effects -0.13 and 0.07, respectively) through their direct associations with self-care (ß = 0.39, p < .001 and ß = -0.19, p < .05, respectively). Conflict also was positively associated with higher Ale (ß = 0.31, p < .01). Conclusions: Elevated family conflict and less parental monitoring are risk factors for poorer glycemic control, and diabetes self-care is one mediator linking these variables. Interventions to promote parental monitoring of diabetes management during early adolescence may benefit from emphasizing strategies to prevent or reduce family conflict. [ABSTRACT FROM AUTHOR]

Published
2013
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5. Structural integrity of α-helix H12 in translation initiation factor eIF5B is critical for 80S complex stability

Author

Shin, Byung-Sik, Acker, Michael G., Kim, Joo-Ran, Maher, Kathryn N., Arefin, Shamsul M., Lorsch, Jon R., and Dever, Thomas E.

Abstract

Translation initiation factor eIF5B promotes GTP-dependent ribosomal subunit joining in the final step of the translation initiation pathway. The protein resembles a chalice with the α-helix H12 forming the stem connecting the GTP-binding domain cup to the domain IV base. Helix H12 has been proposed to function as a rigid lever arm governing domain IV movements in response to nucleotide binding and as a molecular ruler fixing the distance between domain IV and the G domain of the factor. To investigate its function, helix H12 was lengthened or shortened by one or two turns. In addition, six consecutive residues in the helix were substituted by Gly to alter the helical rigidity. Whereas the mutations had minimal impacts on the factor's binding to the ribosome and its GTP binding and hydrolysis activities, shortening the helix by six residues impaired the rate of subunit joining in vitro and both this mutation and the Gly substitution mutation lowered the yield of Met-tRNAiMetbound to 80S complexes formed in the presence of nonhydrolyzable GTP. Thus, these two mutations, which impair yeast cell growth and enhance ribosome leaky scanning in vivo, impair the rate of formation and stability of the 80S product of subunit joining. These data support the notion that helix H12 functions as a ruler connecting the GTPase center of the ribosome to the P site where Met-tRNAiMetis bound and that helix H12 rigidity is required to stabilize Met-tRNAiMetbinding.

Published
2011

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