De Madres a Madres: Women building community coalitions for health

How one group of Hispanic women in Houston, Texas, built community coalitions for primary health care is chronicled from the perspectives of the women. We describe how they formed partnerships with community businesses, health and social service agencies, schools, and churches to develop an outreach network that enables pregnant women to obtain early prenatal care. These women's steps in coalition building are related to feminist theory, with an emphasis on group decision making, shared power for the empowerment of all, and the creation of an environment in which individual worth and dignity are enhanced and risk taking is encouraged and supported.     

Protein Folding Activity of the Ribosome (PFAR) –– A Target for Antiprion Compounds

Prion diseases are fatal neurodegenerative diseases affecting mammals. Prions are misfolded amyloid aggregates of the prion protein (PrP), which form when the alpha helical, soluble form of PrP converts to an aggregation-prone, beta sheet form. Thus, prions originate as protein folding problems. The discovery of yeast prion(s) and the development of a red-/white-colony based assay facilitated safe and high-throughput screening of antiprion compounds. With this assay three antiprion compounds; 6-aminophenanthridine (6AP), guanabenz acetate (GA), and imiquimod (IQ) have been identified. Biochemical and genetic studies reveal that these compounds target ribosomal RNA (rRNA) and inhibit specifically the protein folding activity of the ribosome (PFAR). The domain V of the 23S/25S/28S rRNA of the large ribosomal subunit constitutes the active site for PFAR. 6AP and GA inhibit PFAR by competition with the protein substrates for the common binding sites on the domain V rRNA. PFAR inhibition by these antiprion compounds opens up new possibilities for understanding prion formation, propagation and the role of the ribosome therein. In this review, we summarize and analyze the correlation between PFAR and prion processes using the antiprion compounds as tools.