461 research outputs found
Cody Autrey
No full textCody Autrey was raised in Freeport, Florida. He is pursuing a bachelor’s degree in Biomedical Sciences. His passion for serving under-served populations has led him to volunteer with the American Red Cross, Crisis Text Line, and Shepherd\u27s Hope Health Clinic. Cody is currently researching ion-selective electrodes for the monitoring of ionic deficiencies in patient blood samples under the guidance of Dr. Karin Chumbimuni-Torres. He plans to obtain his M.D. and become a Trauma Surgeon.https://stars.library.ucf.edu/ramp_gallery/1092/thumbnail.jp
Statue of Buffalo bill (William F. Cody), Cody, Wyo.
No full textStatue of Buffalo bill (William F. Cody), Cody, Wyo
sj-pdf-1-asu-10.1177_00031348211067993 – Supplemental Material for Evaluation of Citation Inaccuracies in Surgical Literature by Journal Type, Study Design, and Level of Evidence: Towards Safeguarding the Peer-Review Process
No full textSupplemental Material, sj-pdf-1-asu-10.1177_00031348211067993 for Evaluation of Citation Inaccuracies in Surgical Literature by Journal Type, Study Design, and Level of Evidence: Towards Safeguarding the Peer-Review Process by Matthew Sauder, Kevin Newsome, Israel Zagales, Cody Autrey, Snigdha Das, Darwin Ang and Adel Elkbuli in The American Surgeon</p
Reservoir Site above Shoshone River Dam, Cody, WY
No full textReservoir Site above Shoshone River Dam, Cody, W
Canon Walls overhang the road, Shoshone Canon, Cody, Wy., The
No full textCanon Walls overhang the road, Shoshone Canon, Cody, Wy., Th
River from way north of Shoshone Canon, Cody, WY, The
No full textRiver from way north of Shoshone Canon, Cody, WY, Th
Bulletin No. 301 - Cody - A New Oat for Wyoming
No full textBulletin No. 301 - Cody - A New Oat for Wyomin
Horace Kephart preferred life in a mountain camp
No full textThis article on Horace Kephart’s life, written by Paul Cody, was published in 1992 in Cornell University’s Alumni News. Horace Kephart (1862-1931) was a noted naturalist, woodsman, journalist, and author and promoter of the Great Smoky Mountains National Park
Design and synthesis of novel FtsZ-targeting antibacterial agents
No full textBacterial infections pose a major health concern worldwide, and the emergence of multi-drug resistant strains of bacteria has intensified the search for new antibiotic treatments with novel mechanisms of action. Bacterial cell division remains a new, currently untargeted pathway making it highly desirable research area for discovering new ways to kill bacteria. FtsZ is a highly conserved, essential bacterial cell division protein that forms the dynamic Z-ring involved in recruitment of other essential proteins and serving as the constricting force for cell division. Inhibiting the function of this key protein disrupts proper cell division, and has therefore become a key target in the search for new antibiotics. There are many known FtsZ inhibitors spanning from natural products such as sanguinarine and berberine, to synthetic derivatives such as GTP analogs and PC190723. The majority of these known inhibitors, however, lack the proper potency, safety profiles, and physiochemical properties required for clinical development. Initial studies involved modifying the structures of two known FtsZ inhibitors, sanguinarine and berberine, to increase potency and explore the structure-activity relationships. Unfortunately, although successfully obtaining analogs with good antibacterial activity, these compounds lacked desired solubility properties for further advancement. This led to the second generation of compounds that lacked a constitutive cationic charge while retaining the antibacterial activity seen with the previous analogs. While these compounds had much better solubility, they possessed a new drawback. Compounds from the second generation were found to be highly protein bound resulting in a significant loss of antibacterial activity when administered in the presence of protein. Studies began to design and synthesize analogs that either exhibited much higher potency or much less protein binding. Although initial attempts at this were unsuccessful, continued efforts are being made to find a FtsZ inhibitor with improved potency, physiochemical properties, and a broader spectrum of antibacterial activity.Ph. D.Includes bibliographical referencesby Cody Kelle
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