Grace Notes: feasibility of a manualized intervention to advance spiritual well-being for clients with acquired brain injury.

Spiritual well-being appears to contribute to mental health and adaptation in adults with acquired brain injury (ABI). ABI-related interventions, including those associated with spirituality, must be specifically designed with learning-related impairments in mind. We conducted a feasibility study of a manualized intervention to support spiritual well-being after ABI called Grace Notes. The goal is to provide clients with time tested, easily accessible spiritual practices that help them experience deeper feelings of being in relationship with their Higher Power as they understand it. Findings suggest that Grace Notes can be implemented by both its developer with the context of an interdisciplinary outpatient rehabilitation program and a rehabilitation clinician as a stand-alone group. People with ABI appear to be interested in a spiritually intervention that draws from a variety of spiritual practices and traditions. Further study related to the efficacy of spiritual well-being intervention after ABI is warranted.

Structure and function of the molecular chaperone Hsp104 from yeast.

The molecular chaperone Hsp104 plays a central role in the clearance of aggregates after heat shock and the propagation of yeast prions. Hsp104's disaggregation activity and prion propagation have been linked to its ability to resolubilize or remodel protein aggregates. However, Hsp104 has also the capacity to catalyze protein aggregation of some substrates at specific conditions. Hence, it is a molecular chaperone with two opposing activities with respect to protein aggregation. In yeast models of Huntington's disease, Hsp104 is required for the aggregation and toxicity of polyglutamine (polyQ), but the expression of Hsp104 in cellular and animal models of Huntington's and Parkinson's disease protects against polyQ and alpha-synuclein toxicity. Therefore, elucidating the molecular determinants and mechanisms underlying the ability of Hsp104 to switch between these two activities is of critical importance for understanding its function and could provide insight into novel strategies aimed at preventing or reversing the formation of toxic protein aggregation in systemic and neurodegenerative protein misfolding diseases. Here, we present an overview of the current molecular models and hypotheses that have been proposed to explain the role of Hsp104 in modulating protein aggregation and prion propagation. The experimental approaches and the evidences presented so far in relation to these models are examined. Our primary objective is to offer a critical review that will inspire the use of novel techniques and the design of new experiments to proceed towards a qualitative and quantitative understanding of the molecular mechanisms underlying the multifunctional properties of Hsp104 in vivo.