Ian M. Armitage

Ian M. Armitage is involved, through his laboratory, 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.

Biography Updated on 5 November 2007

Personal Home Page

http://www.cbs.umn.edu/bmbb/faculty/Armitage.I.M.shtml

Articles in Scholarly Journals [Incomplete List]

  1. Metallothionein-3 and neuronal nitric oxide synthase levels in brains from the Tg2576 mouse model of Alzheimer's disease
    Molecular and Cellular Biochemistry, vol. 283, no. 1-2, pp. 129–137, 2006
  2. Antiserum specific for the intact isoform-3 of metallothionein
    Journal of Biochemical and Biophysical Methods, vol. 63, no. 1, pp. 43–52, 2005
  3. Identification of mouse brain proteins associated with isoform 3 of metallothionein
    Protein Science, vol. 14, no. 5, pp. 1151–1157, 2005
  4. Solution structure of Cu6 metallothionein from the fungus Neurospora crassa
    European Journal of Biochemistry, vol. 271, no. 21, pp. 4213–4221, 2004
  5. Dynamics of interdomain and intermolecular interactions in mammalian metallothioneins
    Journal of Inorganic Biochemistry, vol. 88, no. 2, pp. 135–143, 2002
  6. Biochemistry, vol. 40, no. 38, pp. 11433–11441, 2001
  7. Oxidative dimerization in metallothionein is a result of intermolecular disulphide bonds between cysteines in the a-domain
    Biochemical Journal, vol. 359, no. 2, p. 353, 2001
  8. Re-evaluation of the Binding of ATP to Metallothionein
    Journal of Biological Chemistry, vol. 275, no. 11, pp. 7534–7538, 2000
  9. The accordion-HMQC: heteronuclear correlations for a range of coupling constants
    Magnetic Resonance in Chemistry, vol. 38, no. 6, pp. 452–458, 2000
  10. Biochemistry, vol. 38, no. 14, pp. 4471–4479, 1999
  11. Silver and Gold NMR
    Metal-Based Drugs, vol. 6, no. 4-5, pp. 239–245, 1999
  12. NMR spectroscopic studies of I = 1/2 metal ions in biological systems
    Biochemistry and Cell Biology, vol. 76, no. 2-3, pp. 223–234, 1998
  13. Critical Role of Phosphagens in the Energy Cascade of Cutaneous Ischemia and Protective Action of Phosphocreatine Analogues in Skin Flap Survival
    Plastic & Reconstructive Surgery, vol. 101, no. 6, pp. 1597–1603, 1998
  14. Sensitivity-Enhanced Detection of Fast Exchanging Protons by an Exchange-Edited Gradient HEHAHA-HSQC Experiment
    Journal of Magnetic Resonance, vol. 135, no. 1, pp. 70–75, 1998
  15. HIV protease substrate conformation: modulation by cyclophilin A
    FEBS Letters, vol. 414, no. 1, pp. 84–88, 1997
  16. 3D solution structure of copper and silver-substituted yeast metallothioneins
    FEBS Letters, vol. 379, no. 1, pp. 85–93, 1996
  17. Inorganic Chemistry, vol. 34, no. 14, pp. 3833–3834, 1995
  18. Biochemistry, vol. 34, no. 2, pp. 620–631, 1995
  19. Characterization of the calcium-binding sites of calcineurin B
    FEBS Letters, vol. 362, no. 1, pp. 55–58, 1995
  20. Expression of Human Cyclophilin-40 and the Effect of the His141Trp Mutation on Catalysis and Cyclosporin A Binding
    European Journal of Biochemistry, vol. 229, no. 1, pp. 188–193, 1995
  21. Biochemistry, vol. 33, no. 6, pp. 1495–1501, 1994
  22. Biochemistry, vol. 32, no. 26, pp. 6773–6787, 1993
  23. Biochemistry, vol. 31, no. 51, pp. 12778–12784, 1992
  24. Journal of the American Chemical Society, vol. 113, no. 24, pp. 9354–9358, 1991
  25. Journal of the American Chemical Society, vol. 112, no. 18, pp. 6745–6747, 1990
  26. Biochemistry, vol. 29, no. 18, pp. 4466–4478, 1990
  27. An overview of recent progress in ligand-receptor research based on nuclear magnetic resonance spectroscopy
    Biochemical Pharmacology, vol. 40, no. 1, pp. 3–5, 1990
  28. A binding site peptide fragment of the nicotinic acetylcholine receptor. Sequence- specific assignment of IH-NMR resonances in the dodecamer a 185–196
    Biochemical Pharmacology, vol. 40, no. 1, pp. 63–65, 1990
  29. Structural elements pertinent to the interaction of cyclosporin a with its specific receptor protein, cyclophilin
    Biochemical Pharmacology, vol. 40, no. 1, pp. 131–140, 1990
  30. Quantitative studies of hydrodynamic effects and cross-relaxation in protein solutions and tissues with proton and deuteron longitudinal relaxation times
    Magnetic Resonance in Medicine, vol. 13, no. 2, pp. 192–203, 1990
  31. An analysis of magnetic cross-relaxation between water and methylene protons in a model system
    Magnetic Resonance in Medicine, vol. 9, no. 3, pp. 333–342, 1989
  32. Relative contributions of chemical exchange and other relaxation mechanisms in protein solutions and tissues
    Magnetic Resonance in Medicine, vol. 11, no. 3, pp. 295–308, 1989
  33. Biochemistry, vol. 28, no. 6, pp. 2410–2418, 1989
  34. Biochemistry, vol. 28, no. 7, pp. 2991–2995, 1989
  35. Magnetic Resonance, Pathology and Physiology of the BA1112 Rhabdomyosarcoma In Vivo
    Investigative Radiology, vol. 23, no. 4, pp. 277–288, 1988
  36. Inorganic Chemistry, vol. 26, no. 19, pp. 3139–3144, 1987
  37. Journal of the American Chemical Society, vol. 108, no. 14, pp. 4242–4244, 1986
  38. Influence of glycogen on water proton relaxation times
    Magnetic Resonance in Medicine, vol. 3, no. 3, pp. 463–466, 1986
  39. Biochemistry, vol. 25, no. 22, pp. 6778–6784, 1986
  40. Inorganic Chemistry, vol. 24, no. 8, pp. 1170–1174, 1985
  41. Inorganic Chemistry, vol. 24, no. 21, pp. 3439–3444, 1985
  42. m-Fluorotyrosine substitution in ?-galactosidase; Evidence for the existence of a catalytically active tyrosine
    Biochemical and Biophysical Research Communications, vol. 131, no. 2, pp. 675–680, 1985
  43. Journal of the American Chemical Society, vol. 107, no. 6, pp. 1775–1777, 1985
  44. NMR in cancer I. High resolution spectroscopy of tumors
    Magnetic Resonance Imaging, vol. 2, no. 4, pp. 265–278, 1984
  45. Studies of factors affecting the design of NMR contrast agents: manganese in blood as a model system
    Magnetic Resonance in Medicine, vol. 1, no. 3, pp. 396–409, 1984
  46. Biochemistry, vol. 22, no. 5, pp. 1046–1054, 1983
  47. Model for Mammalian Metallothionein Structure
    Proceedings of the National Academy of Sciences, vol. 80, no. 6, pp. 1501–1505, 1983
  48. 113Cd nmr study of the metal cluster structure of human liver metallothionein
    Journal of Inorganic Biochemistry, vol. 17, no. 2, pp. 147–153, 1982
  49. Journal of the American Chemical Society, vol. 103, no. 21, pp. 6522–6524, 1981
  50. Structure of the Metal Clusters in Rabbit Liver Metallothionein
    Proceedings of the National Academy of Sciences, vol. 77, no. 12, pp. 7094–7098, 1980
  51. Reversible trifluoroacetic acid-induced conformational changes in glycophorin as detected by proton nuclear magnetic resonance spectroscopy
    Biochimica et Biophysica Acta (BBA) - Biomembranes, vol. 595, no. 2, pp. 235–243, 1980
  52. Biochemistry, vol. 19, no. 17, pp. 4021–4030, 1980
  53. Biochemistry, vol. 19, no. 17, pp. 4031–4043, 1980
  54. Journal of the American Chemical Society, vol. 101, no. 26, pp. 7734–7736, 1979
  55. Biochemistry, vol. 16, no. 7, pp. 1317–1320, 1977
  56. Biochemistry, vol. 15, no. 25, pp. 5419–5430, 1976
  57. Journal of the American Chemical Society, vol. 98, no. 8, pp. 2371–2371, 1976
  58. Journal of the American Chemical Society, vol. 98, no. 10, pp. 2723–2726, 1976
  59. Journal of the American Chemical Society, vol. 98, no. 13, pp. 3749–3755, 1976
  60. Journal of the American Chemical Society, vol. 98, no. 18, pp. 5710–5712, 1976
  61. Journal of Organic Chemistry, vol. 41, no. 11, pp. 1926–1930, 1976
  62. Nuclear Magnetic Resonance Spectroscopy: Reinvestigation of Carbon-13 Spin-Lattice Relaxation Time Measurements of Amino Acids
    Proceedings of the National Academy of Sciences, vol. 72, no. 4, pp. 1599–1601, 1975
  63. [13C]Valine Metabolism in Methylmalonicacidemia Using Nuclear Magnetic Resonance: Propionate as an Obligate Intermediate
    Proceedings of the National Academy of Sciences, vol. 72, no. 9, pp. 3692–3696, 1975
  64. Journal of the American Chemical Society, vol. 97, no. 9, pp. 2548–2550, 1975
  65. Journal of the American Chemical Society, vol. 97, no. 12, pp. 3416–3419, 1975
  66. Nuclear Magnetic Resonance Spectroscopy. Carbon-13 Spin-Lattice Relaxation Time Measurements of Amino Acids
    Proceedings of the National Academy of Sciences, vol. 71, no. 5, pp. 2096–2097, 1974
  67. Journal of the American Chemical Society, vol. 95, no. 5, pp. 1437–1443, 1973
  68. Journal of the American Chemical Society, vol. 94, no. 25, pp. 8919–8921, 1972