Women Leaders as Change Agents: Mary Campbell’s Story of Academic and Community Leadership

Through this ethnographic study, I had the pleasure of being introduced to Mary Campbell. Mary was born and raised in Pittsburgh, Pennsylvania and grew up in a household made up of her mom, her father, and three older brothers. Unlike families that held their daughters and sons to different gendered standards, Mary always received encouragement from her family that she could do whatever her brothers did (see Figure 1). Mary attributes her Catholic upbringing with instilling many of the values that she maintains today, such as giving back to her community. During a service project in which she participated during her senior year of high school, Mary was introduced to two nuns who had devoted their lives to helping inner-city children. From this interaction with those two influential women, Mary was inspired to pursue both a bachelor’s and a master’s degree in social work with concentrations in marriage and family studies

A Mammalian Homolog of Drosophila melanogaster Transcriptional Coactivator Intersex Is a Subunit of the Mammalian Mediator Complex

The multiprotein Mediator complex is a coactivator required for transcriptional activation of RNA polymerase II transcribed genes by DNA binding transcription factors. We previously partially purified a Med8-containing Mediator complex from rat liver nuclei (Brower, C. S., Sato, S., Tomomori-Sato, C., Kamura, T., Pause, A., Stearman, R., Klausner, R. D., Malik, S., Lane, W. S., Sorokina, I., Roeder, R. G., Conaway, J. W., and Conaway, R. C. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 10353–10358). Analysis of proteins present in the most highly enriched Mediator fractions by tandem mass spectrometry led to the identification of several new mammalian Mediator subunits, as well as several potential Mediator subunits. Here we identify one of these proteins, encoded by the previously uncharacterized AK000411 open reading frame, as a new subunit of the mammalian Mediator complex. The AK000411 protein, which we designate hIntersex (human Intersex), shares significant sequence similarity with the Drosophila melanogaster intersex protein, which has functional properties expected of a transcriptional coactivator specific for the Drosophila doublesex transactivator. In addition, we show that hIntersex assembles into a subcomplex with Mediator subunits p28b and TRFP. Taken together, our findings identify a new subunit of the mammalian Mediator and shed new light on the architecture of the mammalian Mediator complex

A Mammalian Mediator Subunit that Shares Properties with Saccharomyces cerevisiae Mediator Subunit Cse2

The multiprotein Mediator complex is a coactivator required for activation of RNA polymerase II transcription by DNA bound transcription factors. We previously identified and partially purified a mammalian Mediator complex from rat liver nuclei (Brower, C.S., Sato, S., Tomomori-Sato, C., Kamura, T., Pause, A., Stearman, R., Klausner, R.D., Malik, S., Lane, W.S., Sorokina, I., Roeder, R.G., Conaway, J.W., and Conaway, R.C. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 10353-10358). Analysis by tandem mass spectrometry of proteins present in the most highly purified rat Mediator fractions led to the identification of a collection of new mammalian Mediator subunits, as well as several potential Mediator subunits including a previously uncharacterized protein encoded by the FLJ10193open reading frame. In this study, we present direct biochemical evidence that the FLJ10193protein, which we designate Med25, is a bona fide subunit of the mammalian Mediator complex. In addition, we present evidence that Med25 shares structural and functional properties with Saccharomyces cerevisiae Mediator subunit Cse2 and may be a mammalian Cse2 ortholog. Taken together, our findings identify a novel mammalian Mediator subunit and shed new light on the architecture of the mammalian Mediator complex

Accessibility to Food Intolerance and Food Allergy Resources in McLean County, Illinois: An Interdisciplinary Pilot Study

Food intolerances and food allergies are evolving and diagnoses of such conditions are rapidly increasing. Yet our ancient bodies and social resources are not adapting to this dynamic environment. Accessing healthcare and allergen-free foods is necessary for all people with food allergies and intolerances, but gaps in social resources complicate acquiring these resources, especially for low-income individuals. This interdisciplinary pilot study utilizes a mixed method approach, including sociologically and anthropologically-based surveys and participant observation, respectively, and is guided by the action research approach. Data analysis illustrates major gaps in access to healthcare, specifically to dietitians, and in food acquisition from government agencies and food pantries. All grocery stores included in this study have some amount of allergen-free foods, but knowledge of these products varies drastically. The paper is concluded with a resource-neutral plan of action that aims to enhance the lives of people who suffer from food intolerances in McLean County, Illinois

Identification of Mammalian Mediator Subunits with Similarities to Yeast Mediator Subunits Srb5, Srb6, Med11, and Rox3

The Mediator is a multiprotein coactivator required for activation of RNA polymerase II transcription by DNA binding transactivators. We recently identified a mammalian homologue of yeast Mediator subunit Med8 and partially purified a Med8-containing Mediator complex from rat liver nuclei (Brower, C. S., Sato, S., Tomomori-Sato, C., Kamura, T., Pause, A., Stearman, R., Klausner, R. D., Malik, S., Lane, W. S., Sorokina, I., Roeder, R. G., Conaway, J. W., and Conaway, R. C. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 10353-10358). Analysis of proteins present in the most highly purified Med8-containing fractions by tandem mass spectrometry led to the identification of many known mammalian Mediator subunits, as well as four potential Mediator subunits exhibiting sequence similarity to yeast Mediator subunits Srb5, Srb6, Med11, and Rox3. Here we present direct biochemical evidence that these four proteins are bona fide mammalian Mediator subunits. In addition, we identify direct pairwise binding partners of these proteins among the known mammalian Mediator subunits. Taken together, our findings identify a collection of novel mammalian Mediator subunits and shed new light on the underlying architecture of the mammalian Mediator complex

Impact of Secondary-Level CTE Credentials on Carpentry Students and Field Employment

A capstone submitted in partial fulfillment of the requirements for the degree of Doctor of Education in the Ernst and Sara Lane Volgenau College of Education at Morehead State University by Joshua A. Parmley on April 5, 2024

Stabilization of DNA i-motif structures by 7-aminoactinomycin D, an anti-tumor drug

Alternative DNA structures are likely to form from Watson-Crick B-form DNA when antitumor drug known to bind DNA loops -- can affect the iM structure. Our results demonstrate as an i-motif (iM). While both structures are known to exist in vivo they are energetically uphill can utilize intercalating cytosine-cytosine base pairing to form a four-stranded structure known controlled by alternative DNA structures like G4s and iMs. especially during processes that involve superhelical duress. A guanosine rich strand can form a facilitate their stabilization. In this report we present data on how 7-aminoactinomycin D -- an formation. Earlier it was believed that iMs required slightly acidic conditions (pH ≤ 6) for four-stranded structure known as a G-quadruplex (G4). The complimentary cytosine rich strand from double strand DNA (dsDNA) meaning that additional factors are needed to facilitate their of ~7. Additionally loop regions of iMs have been implicated in their thermal and pH-dependent shift the pKa of the iM (the pH at which 50% of the iM is folded) nearer to the physiological pH small molecules may be a promising way to therapeutically regulate expression of genes stability. Small molecules such as polyamines and larger molecules like proteins can interact structure stabilization. However crowding agents like polyethylene glycols and dextrans can that a small molecule antitumor drug can stabilize or destabilize iMs by simultaneously changing there is an asymmetric distribution of guanosine and cytosine on opposite DNA strands thermodynamic properties including Tm pKa and ΔG°37 °C. Our results suggest that the use of with iMs by binding to their loops suggesting that additional biochemical factors may also facilitate their stabilization. In this report, we present data on how 7-aminoactinomycin D -- an antitumor drug known to bind DNA loops -- can affect the iM structure. Our results demonstrate that a small molecule antitumor drug can stabilize or destabilize iMs by simultaneously changing thermodynamic properties including Tm, pKa, and ΔG°37 °C. Our results suggest that the use of small molecules may be a promising way to therapeutically regulate expression of genes controlled by alternative DNA structures like G4s and iMs

Fairy Tale Transformation Through The Visual Media of Animation Displayed By Walt Disney and Studio Ghibli

This Senior Project takes the first films and most popular animated fairy tale like stories from both Disney and Studio Ghibli and compares them with their source material and inspirations in order to see how they have differed. By doing this we can see how natural changes to fit with the time of its release and how as the public's opinion changes on subjects the stories themselves change. But with each change do the crucial lessons from the originals change or are they simply ingrained within each telling of the story? Here is where we see what each story is meant to exhibit and reenforce in order to teach the audience the lessons the stories put on display.Purchase College SUNYCinema StudiesBachelor of ArtsAnderson, Joel N