CedarCommons Logo Variations 2024

A fresh logo for the newly named CedarCommons, the institutional repository and digital archives of Cedarville University was designed by Creative Services and released in 2024. Important elements of the logo include: Computer monitor - digital nature of the repository items and access to those items. Columned building - Cedarville Univeristy history and Bliblical heritage of the digital archives and special collections. Unlocked padlock - commitment to open access to items contained in the repository. CedarCommons - a combination of Cedarville and a definition of Commons which is a gathering place and resources common to a community. Gold and Navy - Cedarville University color palett

Cedrus Press Author Roadmap Brochure (trifold)

Author\u27s Roadmap CedrusPress\u27 trifold brochure promoting faculty book and textbook open-access publishing services offered by Digital Services

CedarCommons Mousepad

A navy, gold, and white mousepad promoting CedarCommons reposity. Includes an inspirational quote by Thomas Fuller (1608-1661) - an English churchman and historian - All things are difficult before they become easy. A small gift to the Digital Services staff in anticipation of the repository platform and data conversion in 2025

Digital Commons Promotional Stickers

DigitalCommons@Cedarville repository and Centennial Library stickers distributed as promotional pieces in 2023-2024

Globe Stress Balls for New Faculty

Squeezable stress ball shaped like a globe imprinted with the DigitalCommons@Cedarville logo and tagline we share your work with the world. A gift for the 2023 class of new faculty

H3K27Ac Levels are Affected by Heat Stress and Anti-Mitotic Drugs in Tetrahymena Thermophila

Gene regulation is one of the most complex tasks to be undertaken by any eukaryotic cell, and a prime contributor to gene regulation is the post-translational modification of histone tails. Diffuse Intrinsic Pontine Glioma (DIPG) is an example of a cancer that occurs when one lysine, H3K27 on the tail of histone H3, is mutated to a methionine, making the usual post-translational modifications (methylation and acetylation) that occur at position 27 impossible. We believe that this lysine residue is critical for the regulation of cell division. Our hypothesis was that perturbations of cell division, as well as stress, will affect acetylation at H3K27. We also sought to find some of the binding partners that interact with H3K27ac by doing whole cell CO-IP. Our results show that stress and mitotic inhibitors affect acetylation levels of H3K27, and that proteins associated with DNA repair, transcription, RNA processing, and nuclear proteostasis associate with H3K7ac