Publications by authors named "Sara L Powers"

In mammals, histone H3.3 is a critical regulator of transcription state change and heritability at both euchromatin and heterochromatin. The H3.

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Unlike the core histones, which are incorporated into nucleosomes concomitant with DNA replication, histone H3.3 is synthesized throughout the cell cycle and utilized for replication-independent (RI) chromatin assembly. The RI incorporation of H3.

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Objective: Face transplantation replaces substantial defects with anatomically identical donor tissues; preoperative vascular assessment relies on noninvasive imaging to separate and characterize the external carotid vessels and branches. The objective is to describe and illustrate vascular considerations for face transplantation candidates.

Methods: Novel noninvasive imaging using computed tomography and magnetic resonance imaging over 3 spatial dimensions plus time was developed and tested in 4 face transplant candidates.

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Background: Facial allotransplantation requires a detailed arterial and venous assessment for surgical planning. Target vessels are often depleted by multiple reconstructive attempts or the severe facial injury itself. The purpose of this study was to retrospectively compare the diagnostic performance of computed tomography and magnetic resonance angiography in the preoperative assessment.

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The purpose of this study was to estimate dose reduction after implementation of asymmetrical cone beam processing using exposure differences measured in a water phantom and a small cohort of clinical coronary CTA patients. Two separate 320 × 0.5 mm detector row scans of a water phantom used identical cardiac acquisition parameters before and after software modifications from symmetric to asymmetric cone beam acquisition and processing.

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We report initial surgical planning computed tomographic protocols for composite tissue allotransplantation of the face. This complex procedure replaces missing facial structures with anatomically identical tissues, restoring form and function. Achieved results are superior to those accomplished with conventional techniques.

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Background: Gene activation is thought to occur through a series of temporally defined regulatory steps. However, this process has not been completely evaluated in single living mammalian cells.

Methodology/principal Findings: To investigate the timing and coordination of gene activation events, we tracked the recruitment of GCN5 (histone acetyltransferase), RNA polymerase II, Brd2 and Brd4 (acetyl-lysine binding proteins), in relation to a VP16-transcriptional activator, to a transcription site that can be visualized in single living cells.

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Intramural hematoma (IMH) is defined as localized hemorrhage within the aortic wall and is included in the acute aortic syndrome spectrum with aortic dissection and penetrating aortic ulcer. The mortality from IMH is similar to classic aortic dissection (21%). 16% of patients with IMH will evolve to classic aortic dissection over time.

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Although manipulation of the endoplasmic reticulum (ER) folding environment in the yeast Saccharomyces cerevisiae has been shown to increase the secretory productivity of recombinant proteins, the cellular interactions and processes of native enzymes and chaperones such as protein disulfide isomerase (PDI) are still unclear. Previously, we reported that overexpression of the ER chaperone PDI enabled up to a 3-fold increase in secretion levels of the Pyrococcus furiosus beta-glucosidase in the yeast S. cerevisiae.

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To elucidate determinants of thermostability and folding pathways of the intrinsically stable proteins from extremophilic organisms, we are studying beta-glucosidase from Pyrococcus furiosus. Using fluorescence and circular dichroism spectroscopy, we have characterized the thermostability of beta-glucosidase at 90 degrees C, the lowest temperature where full unfolding is achieved with urea. The chemical denaturation profile reveals that this homotetrameric protein unfolds at 90 degrees C with an overall DeltaG degrees of approximately 20 kcal mol(-1).

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