Radiologic anatomy of the round window relevant to cochlear implantation and inner ear drug delivery.

Objective: To determine anatomic relationships and variation of the round window membrane to bony surgical landmarks on computed tomography.

Study Design: Retrospective imaging review.

Methods: 100 temporal bone images were evaluated.

Heat shock protein 104 (Hsp104)-mediated curing of [] yeast prions depends on both [] conformation and the properties of the Hsp104 homologs.

Prions arise from proteins that have two possible conformations: properly folded and non-infectious or misfolded and infectious. The [] yeast prion, which is the misfolded and self-propagating form of the translation termination factor eRF3 (Sup35), can be cured of its infectious conformation by overexpression of Hsp104, which helps dissolve the prion seeds. This dissolution depends on the trimming activity of Hsp104, which reduces the size of the prion seeds without increasing their number.