This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The Center for Protease Research was established in 2001 with funds from the COBRE program. The previous grant application had a strong focus on chemistry, while this continuation will have a strong biology component with cancer and asthma as the primary disease targets. Understanding the biological role played by matrix metalloproteinases and histone deacetylases in cancer and other diseases such as asthma will be a major scientific goal. The Center will coordinate the expertise of 4 new investigators: Glenn Dorsam and Gregory Cook, Department of Chemistry and Molecular Biology;Bin Guo, Department of Pharmaceutical Sciences;and Jane Schuh, Department of Veterinary and Microbiological Sciences. Core Facilities in biology and synthetic chemistry will play a key role in assisting the research programs of the new PI's, other NDSU researchers, and North Dakota INBRE researchers. The Center will continue to build infrastructure, initiate new activities, and continue previously successful programs to foster growth of biomedical research in North Dakota. Combating cancer, one of the leading causes of mortality in humans, is a major goal for biomedical scientists. The NDSU COBRE center will conduct research to provide fundamental information on how proteases, a key biological player in several diseases, impacts cancer. These studies have the potential to provide novel therapeutics that can treat this deadly disease.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Exploratory Grants (P20)
Project #
5P20RR015566-09
Application #
8167859
Study Section
Special Emphasis Panel (ZRR1-RI-5 (01))
Project Start
2010-07-01
Project End
2011-06-30
Budget Start
2010-07-01
Budget End
2011-06-30
Support Year
9
Fiscal Year
2010
Total Cost
$1,018,097
Indirect Cost
Name
North Dakota State University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
803882299
City
Fargo
State
ND
Country
United States
Zip Code
58108
Lundquist, Taylor A; Kittilson, Jeffrey D; Ahsan, Rubina et al. (2018) The effect of within-instar development on tracheal diameter and hypoxia-inducible factors ? and ? in the tobacco hornworm, Manduca sexta. J Insect Physiol 106:199-208
Jensen, Jaime L; Wu, Qiong; Colbert, Christopher L (2018) NMR assignments of the N-terminal signaling domain of the TonB-dependent outer membrane transducer PupB. Biomol NMR Assign 12:91-94
Edwinson, Adam; Widmer, Giovanni; McEvoy, John (2016) Glycoproteins and Gal-GalNAc cause Cryptosporidium to switch from an invasive sporozoite to a replicative trophozoite. Int J Parasitol 46:67-74
Holubová, Nikola; Sak, Bohumil; Hor?i?ková, Michaela et al. (2016) Cryptosporidium avium n. sp. (Apicomplexa: Cryptosporidiidae) in birds. Parasitol Res 115:2243-51
Linder, Douglas P; Rodgers, Kenton R (2015) Methanethiol Binding Strengths and Deprotonation Energies in Zn(II)-Imidazole Complexes from M05-2X and MP2 Theories: Coordination Number and Geometry Influences Relevant to Zinc Enzymes. J Phys Chem B 119:12182-92
Jensen, Jaime L; Balbo, Andrea; Neau, David B et al. (2015) Mechanistic Implications of the Unique Structural Features and Dimerization of the Cytoplasmic Domain of the Pseudomonas Sigma Regulator, PupR. Biochemistry 54:5867-77
Ghospurkar, Padmaja L; Wilson, Timothy M; Liu, Shengqin et al. (2015) Phosphorylation and cellular function of the human Rpa2 N-terminus in the budding yeast Saccharomyces cerevisiae. Exp Cell Res 331:183-99
Piya, Gunjan; Mueller, Erica N; Haas, Heather K et al. (2015) Characterization of the interaction between Rfa1 and Rad24 in Saccharomyces cerevisiae. PLoS One 10:e0116512
Jensen, Jaime L; Indurthi, Venkata S K; Neau, David B et al. (2015) Structural insights into the binding of the human receptor for advanced glycation end products (RAGE) by S100B, as revealed by an S100B-RAGE-derived peptide complex. Acta Crystallogr D Biol Crystallogr 71:1176-83
Singh, Raushan K; Cho, Kyongshin; Padi, Satish K R et al. (2015) Mechanism of N-Acylthiourea-mediated activation of human histone deacetylase 8 (HDAC8) at molecular and cellular levels. J Biol Chem 290:6607-19

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