This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The Bosch lab is interested in malarial proteins involved in invasion and egress of the parasite into or from various cell types in the human liver, red blood cells as well as in the Mosquito vector.
We aim at impairing the parasite's proliferation through small molecule inhibitors for key proteins through structure based drug design in conjunction with x-ray crystallography. The Prigge lab is interested in the structural biology of key proteins from malaria and tuberculosis. Current protein crystals include proteins involved in pathogen persistence in tuberculosis and sexual differentiation in malaria. The Bailey lab performs structure function studies of a newly characterized acquired immune system in prokaryotes, which shares some of the basic principles of eukaryotic RNAi. Through the analysis of crystal structures and functional data we hope to discern the molecular mechanisms underpinning this immunity. To this end we have obtained crystals of several of the proteins involved.
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|Tolbert, William D; Gohain, Neelakshi; Alsahafi, Nirmin et al. (2017) Targeting the Late Stage of HIV-1 Entry for Antibody-Dependent Cellular Cytotoxicity: Structural Basis for Env Epitopes in the C11 Region. Structure 25:1719-1731.e4|
|Yoon, Chun Hong; DeMirci, Hasan; Sierra, Raymond G et al. (2017) Se-SAD serial femtosecond crystallography datasets from selenobiotinyl-streptavidin. Sci Data 4:170055|
|Warelow, Thomas P; Pushie, M Jake; Cotelesage, Julien J H et al. (2017) The active site structure and catalytic mechanism of arsenite oxidase. Sci Rep 7:1757|
|Tzarum, Netanel; de Vries, Robert P; Peng, Wenjie et al. (2017) The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus. Cell Rep 19:235-245|
|Hettle, Andrew; Fillo, Alexander; Abe, Kento et al. (2017) Properties of a family 56 carbohydrate-binding module and its role in the recognition and hydrolysis of ?-1,3-glucan. J Biol Chem 292:16955-16968|
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