This COBRE Phase III proposal aims to further develop the Center for Molecular Medicine at the University of Kentucky. This Center focuses on research aimed at understanding the molecular mechanisms associated with human disease with emphases on cancer, neurodegenerative diseases, diabetes, and cardiovascular diseases. We propose to transition to independence the research infrastructure developed during previous COBRE funding. Our COBRE funded Center for Molecular Medicine has had a number of successes. During the previous funding period 30 junior faculty from 12 different departments and centers were funded as COBRE project or pilot grant PIs. These mentored faculty received 27 NIH ROI grants, 11 other NIH grants, and 41 other peer-reviewed extramural grants. The COBRE-supported junior faculty published more than 400 research papers. These and other successes can in large part be attributed to a strong mentoring program, excellent institutional support, and the availability of the scientific cores associated with the Center. For this application, we propose to transition the Center for Molecular Medicine and its three scientific cores to independence of NIH/NIGMS support and to enhance and upgrade core technologies. It is worth noting that two of our original cores have or soon will transition to independence;the Proteomics core developed by this COBRE is now a University fee-for-service core, and the COBRE supported Imaging core is soon to become a department supported core. During the proposed five-year transition period we will increase the critical mass of faculty associated with the Center and continue to enhace its Cores. The use of vouchers will promote core usage and pilot grants will develop research collaborations and competitive grant submissions. The Administrative Core will serve as the focal point of the grant and in conjunction with the Program Coordinator and Internal Advisory Committee will serve as the operational arm of the Center. An External Advisory Committee, consisting of world-renown scientists will provide ongoing assessment and evaluation of the Center. Continuing Institutional commitments will ensure programmatic growth, and long-term sustainability.
This COBRE funded Center for Molecular Medicine has as a focus the molecular basis of human disease. The COBRE scientific cores have supported and will continue to support and enhance translational research at the University of Kentucky and other regional institutions.
|Wachter, Erin; MoyÃ¡, Diego; Parkin, Sean et al. (2016) Ruthenium Complex "Light Switches" that are Selective for Different G-Quadruplex Structures. Chemistry 22:550-9|
|Meier, Shelby; Bell, Michelle; Lyons, Danielle N et al. (2016) Pathological Tau Promotes Neuronal Damage by Impairing Ribosomal Function and Decreasing Protein Synthesis. J Neurosci 36:1001-7|
|Xu, Xuehe; Watt, David S; Liu, Chunming (2016) Multifaceted roles for thymine DNA glycosylase in embryonic development and human carcinogenesis. Acta Biochim Biophys Sin (Shanghai) 48:82-9|
|Wagner, Jonathan M; Chan, Sum; Evans, Timothy J et al. (2016) Structures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system. BMC Struct Biol 16:5|
|Sviripa, Vitaliy M; Burikhanov, Ravshan; Obiero, Josiah M et al. (2016) Par-4 secretion: stoichiometry of 3-arylquinoline binding to vimentin. Org Biomol Chem 14:74-84|
|Frasinyuk, Mykhaylo S; Mrug, Galyna P; Bondarenko, Svitlana P et al. (2016) Antineoplastic Isoflavonoids Derived from Intermediate ortho-Quinone Methides Generated from Mannich Bases. ChemMedChem 11:600-11|
|Kwiatkowski, Stefan; Sviripa, Vitaliy M; Zhang, Zhaiyi et al. (2016) Synthesis of a norcantharidin-tethered guanosine: Protein phosphatase-1 inhibitors that change alternative splicing. Bioorg Med Chem Lett 26:965-8|
|Riedmann, Caitlyn; Fondufe-Mittendorf, Yvonne N (2016) Comparative analysis of linker histone H1, MeCP2, and HMGD1 on nucleosome stability and target site accessibility. Sci Rep 6:33186|
|Falaleeva, Marina; Surface, Justin; Shen, Manli et al. (2015) SNORD116 and SNORD115 change expression of multiple genes and modify each other's activity. Gene 572:266-73|
|Kril, Liliia M; Vilchez, Valery; Jiang, Jieyun et al. (2015) N-Aryl benzenesulfonamide inhibitors of [3H]-thymidine incorporation and Î²-catenin signaling in human hepatocyte-derived Huh-7 carcinoma cells. Bioorg Med Chem Lett 25:3897-9|
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