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Research Interests
Multinuclear Magnetic Resonance, Metal Homeostasis, Zinc-Finger Transcription Factor Activation, Alzheimer's Disease and Immunophilins
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Research Description
My laboratory is involved with the development and application of state-of-the-art multinuclear, multidimensional magnetic resonance methods to elucidate the structure, dynamics and mechanism of action of biological macromolecules. The strategy that is frequently used to focus on a particular aspect of a complex biological system such as an enzyme's active site or intermediates in the reaction profile, is the selective observation of less abundant nuclei present naturally or incorporated by specific biosynthetic or chemical labeling procedures. Specific systems under current investigation include: metalloproteins involved in metal homeostasis, metallothioneins, which includes studies of their role in the activation of zinc-finger containing transcription factors and the physiological role of the brain specific metallothionein, MT3, in Alzheimer's disease; and molecules involved in the immune response, the immunosuppressive drug cyclosporin A (CsA), and its cytosolic receptor protein, cyclophilin (CyP) and the penultimate interaction of the CsA:CyP complex with calcineurin.
Another area of past active research involved fundamental studies of factors affecting the relaxation (MRI) of protons in tissue with applications to clinical magnetic resonance imaging techniques.
High Field Nuclear Magnetic Resonance Facility at the University of Minnesota
Recent Publications
El Ghazi, I., Martin, B. L., and Armitage, I. M., Metallothionein-3 is a Component of a Multiprotein Complex in the Mouse Brain", Exp Biol Med, 231, 1500-1506 (2006). PubMed
Martin, B.L. , Tokheim, A.M., McCarthy, P.T., Doms, B.S., Davis, A.A. and Armitage, I.M. "Metallothionein-3 and neuronal nitric oxide synthase levels in brains from the Tg2576 mouse model of Alzheimer's disease." Molecular and Cellular Biochemistry, 286, 129-136. (2006) E-Journal
Lahti, D. W., Hoekman, J. D., Tokheim, A. M., Martin, B. L., and Armitage, I. M., "Identification of Mouse Brain Proteins Associated with Isoform 3 of Metallothionein", Protein Science, 14, 1151-1157 (2005). PubMed
Tokheim, A. M., Armitage, I. M., and Martin, B. L., "Antiserum Specific for the Intact Isoform-3 of Metallothionein", J. Biochem. Biophys. Methods, 63, 43-52 (2005). PubMed
Zangger, K. and Armitage, I. M., "Metallothionein" in Handbook of Metalloproteins , Volume 3, W. Bode, M. Cygler and A. Messerschmidt (eds) John Wiley & Sons, 351-364, (2004).
Cobine, P. A., McKay, R. T., Zangger, K., Dameron, C. T., and Armitage, I. M., "Solution Structure of Cu6 Metallothionein from the fungus Neurospora crass a," Eur. J. Biochem. (now FEBS J. ) 271 , 4213-4221 (2004). PubMed
Zangger, K. and Armitage, I. M. (2002) "Dynamics of Interdomain Interactions in Mammalian Metallothioneins," J. Inorg. Biochem., 88 ,(2), 135-143. PubMed
Zangger, K., Shen, G., Oz, G., Otvos, J.D. and Armitage, I.M., (2001) "Oxidative Dimerization in Metallothionein is a Result of Intermolecular Disulfide Bonds between Cysteines in the a-Domain," Biochem. J., 359, 353-360. PubMed
Oz, G., Zangger, K., and Armitage, I.M., (2001) "Three-dimensional Structure and Dynamics of a Brain Specific Growth Inhibitory Factor: Metallothionein-3," Biochemistry, 40, 11433-11441. PubMed
Zangger, K., Oz, G., Haslinger, E., Kunert, O. and Armitage, I.M., (2001) "Nitric Oxide Selectively Releases Metals from the N-terminal Domain of Metallothioneins: Potential Role at Inflammatory Sites," FASEB J., 15 (7): 1303-5. FASEB J
Zangger, K. Oz, G., and Armitage, I.M., (2000) "Re-evaluation of the Binding of ATP to Metallothioneins", J. Biol. Chem. 275:7534-8. PubMed.
Zangger, K. and Armitage, I.M. (2000) "The Accordian-HMQC:Heteronuclear Correlations Over a range of Coupling Constants," Magn. Reson. Chem. 38: 452-458.
Zangger, K., Oz, G., Otvos, J.D., Armitage, I.M. (1999) Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy. Protein Sci. 8(12):2630-8. PubMed
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