1. Banks, B.E.C., Doonan, S., Lawrence, A.J. & Vernon, C.A. (1968). The molecular weight and other properties of aspartate aminotransferase from pig heart muscle. Eur. J. Biochem. 5, 528-539.
2. Banks, B.E.C., Doonan, S., Gauldie, J., Lawrence, A.J. & Vernon, C.A. (1968). The dissociation into subunits of aspartate aminotransferase from pig heart muscle. Eur. J. Biochem. 6, 507-513.
3. Banks, B.E.C., Banthorpe, D.V., Berry, A.R., Davies, H.ff.S., Doonan, S., Lamont, D.M., Shipolini, R. & Vernon, C.A. (1968). The preparation of nerve growth factors from snake venoms. Biochem. J. 108, 157-158.
4. Shipolini, R.A., Callewaert, G.L., Cottrell, R.C., Doonan, S., Banks, B.E.C. & Vernon, C.A. (1971). Phospholipase A from bee venom. Eur. J. Biochem. 20, 459-468.
5. Doonan, S., Doonan, H.J., Riva, F., Vernon, C.A., Walker, J.M., Bossa, F., Barra, D., Carloni, M. & Fasella, P. (1972). The primary structure of aspartate aminotransferase from pig heart muscle: partial sequences determined by digestion with pepsin and trypsin. Biochem. J. 130, 443-452.
6. Bossa, F., Barra, D., Carloni, M., Fasella, P., Riva, F., Doonan, S., Doonan, H.J., Hanford, R., Vernon, C.A. & Walker, J.M., (1973). The primary structure of aspartate aminotransferase from pig heart muscle: partial sequences determined by digestion with thermolysin and elastase. Biochem. J. 133, 805-819.
7. Doonan, S., Doonan, H.J., Hanford, R., Vernon, C.A., Walker, J.M., Bossa, F., Barra, D., Carloni, M., Fasella, P., Riva, F. & Walton, P.L. (1974). The primary structure of aspartate aminotransferase from pig heart muscle determined in part using a protease with specificity for lysine. FEBS Lett. 38, 229-233.
8. Hanford, R., Doonan, H.J., Doonan, S., Vernon, C.A., Walker, J.M., Bossa, F., Barra, D., Carloni, M., Fasella, P. & Riva, F. (1974). The primary structure of aspartate aminotransferase from pig heart muscle: peptides produced by cleavage with cyanogen bromide and with dilute acid. Atti Accad. Naz. Lincei Rend. 56, 73-83.
9. Riva, F., Barra, D., Bossa, F., Carloni, M., Fasella, P., Doonan, S., Doonan, H.J., Hanford, R., & Walker, J.M. (1974). The primary structure of aspartate aminotransferase from pig heart muscle: limited peptic digestion. Atti Accad. Naz. Lincei Rend. 56, 581-588.
10. Barra, D., Bossa, F., Carloni, M., Fasella, P., Martini, F., Petruzzelli, R., Riva, F., Doonan, S., Doonan, H.J., Hanford, R., & Walker, J.M. (1974). The primary structure of aspartate aminotransferase from pig heart muscle: chymotryptic peptides. Atti Accad. Naz. Lincei Rend. 56, 589-598.
11. Doonan, S., Hughes, G.J., Barra, D., Bossa, F., Martini, F. & Petruzzelli, R. (1974). Homology of the primary structures of cytoplasmic and mitochondrial aspartate aminotransferases from pig heart. FEBS Lett. 49, 25-28.
12. Shipolini, R.A., Doonan, S. & Vernon, C.A. (1974). The disulphide bridges of phospholipase A2 from bee venom. Eur. J. Biochem. 48, 477-483.
13. Doonan, S., Koerner, D.H., Schmutzler, W. & Vernon, C.A. (1974). Inducibility and some properties of the threonine dehydratase of sheep liver. Biochem. J. 144, 533-541.
14. Airoldi, L.P.da S. & Doonan, S. (1975). A method of distinguishing between aspartic acid and asparagine and between glutamic acid and glutamine during sequence analysis by the dansyl-Edman method. FEBS Lett. 50, 155-158.
15. Doonan, S. & Fahmy, H.M.A. (1975). Specific enzymic cleavage of polypeptides at cysteine residues. Eur. J. Biochem. 56, 421-426.
16. Banthorpe, D.V., Chaudhry, A.R. & Doonan, S. (1975). Specificity and inhibition of phosphatases in Tanacetum vulgare. Z. Pflanzenphysiol. 76, 143-154.
17. Doonan, S., Doonan, H.J., Hanford, R., Vernon, C.A., Walker, J.M., Airoldi, L.P.da S., Bossa, F., Barra, D., Carloni, M., Fasella, P. & Riva, F. (1975). The primary structure of aspartate aminotransferase from pig heart muscle: digestion with a proteinase having specificity for lysine residues. Biochem. J. 149, 497-506.
18. Barra, D., Bossa, F., Doonan, S., Fahmy, H.M.A., Martini, F. & Hughes, G.J. (1976). Large scale purification and some properties of mitochondrial aspartate aminotransferase from pig heart. Eur. J. Biochem. 64, 519-526.
19. Baumber, M.E. & Doonan, S. (1976). A quantitative study of the subcellular distribution of aspartate aminotransferase isozymes in rat liver. Int. J. Biochem. 7, 119-124.
20. Doonan, S. & Stanway, G. (1976). Identification of the reactive sulphydryl group of mitochondrial aspartate aminotransferase from pig heart. FEBS Lett. 69, 261-264.
21. Banks, B.E.C., Doonan, S., Flogel, M., Porter, P.B., Vernon, C.A., Walker, J.M., Crouch, T.H., Halsey, J.F., Chiancone, E. & Fasella, P. (1976). An assessment of some of the methods available for the determination of molecular weights of proteins as applied to aspartate aminotransferase from pig heart. Eur. J. Biochem. 71, 469-473.
22. Banthorpe, D.V., Bucknall, G.A., Doonan, H.J., Doonan, S. & Rowan, M.G. (1976). Biosynthesis of geraniol and nerol in cell-free extracts of Tanacetum vulgare. Phytochem. 15, 91-100.
23. Banthorpe, D.V., Doonan, S. & Gutowski, J.A. (1977). Biosynthesis of irregular monoterpenes in cell-free extracts from higher plants. Phytochem. 16, 85-92.
24. Marra, E., Doonan, S., Saccone, C. & Quagliariello, E. (1977). Selective permeability of rat liver mitochondria to purified aspartate aminotransferases in vitro. Biochem. J. 164, 685-691.
25. Banthorpe, D.V., Doonan, S. & Gutowski, J.A. (1977). Isopentenyl pyrophosphate isomerase from pig liver. Arch. Biochem. Biophys. 184, 381-390.
26. Barra, D., Bossa, F., Doonan, S., Fahmy, H.M.A., Hughes, G.J., Kakoz, K.Y., Martini, F. & Petruzzelli, R. (1977). The structure of mitochondrial aspartate aminotransferase from pig heart and comparison with that of the cytoplasmic isozyme. FEBS Lett. 83, 241-244.
27. Doonan, S., Loudon, A.G., Barra, D., Bossa. F. & Brunori, M. (1978). Identification of the N-terminal blocking groups of trout hemoglobins by mass spectrometry. FEBS Lett. 85, 141-144.
28. Doonan, S., Ho, T.K.W., Pearce, F.L. & Slaughter, C.A. (1978). Glycosidases in the submaxillary gland of the mouse: sexual dimorphism and the effects of testosterone. Int. J. Biochem. 9. 235-238.
29. Doonan, S., Garman, A.J., Hanson, J.M., Loudon, A.G. & Vernon, C.A. (1978). Identification by mass spectrometry of Ne -formyl-lysine residues in a peptide from bee venom. J. Chem. Soc. Perk. 1, 1156-1160.
30. Marra, E., Doonan, S., Saccone, C. & Quagliariello, E. (1978). Studies of the selective permeation of radioactively labelled aspartate aminotransferase isozymes into mitochondria in vitro. Eur. J. Biochem. 83, 427-435.
31. Doonan, S. & Fahmy, H.M.A. (1978). Evidence for the existence of an extended region of structural heterogeneity in the mitochondrial aspartate aminotransferase from pig heart. Bull. Molec. Biol. Med. 3, 121-129.
32. Sutor, D.J., Percival, J.M. & Doonan, S. (1978). Isolation and identification of some urinary inhibitors of calcium phosphate formation. Clin. Chem. Acta, 89, 273-278.
33. Sutor, D.J., Percival, J.M. & Doonan, S. (1979). Urinary inhibitors of the formation of calcium oxalate. Brit. J. Urol. 51, 253-255.
34. Marra, E., Passarella, S., Doonan, S., Saccone, C. & Quagliariello, E. (1979). The effect of sulfhydryl group reagents on the permeation of mitochondrial aspartate aminotransferase into mitochondria in vitro. Arch. Biochem. Biophys. 195, 269-279.
35. Barra, D., Martini, F., Montarani, G., Doonan, S. & Bossa, F. (1979). Primary structure of mitochondrial aspartate aminotransferase from turkey liver: cysteine-containing peptides. FEBS Lett. 108, 103-106.
36. Doonan, S., Fahmy, H.M.A., Hughes, G.J., Barra, D. & Bossa, F. (1979). The primary structure of mitochondrial aspartate aminotransferase from pig heart: peptides obtained by cleavage at basic residues. Ital. J. Biochem. 28, 441-455.
37. Barra, D., Petruzzelli, R., Martini, F., Bossa, F. & Doonan, S. (1979). The primary structure of mitochondrial aspartate aminotransferase from pig heart: peptides obtained by cleavage with thermolysin and chymotrypsin. Ital. J. Biochem. 28, 456-477.
38. Barra, D., Savi, M.R., Petruzzelli, R., Bossa, F. & Doonan, S. (1979). The primary structure of mitochondrial aspartate aminotransferase from pig heart: peptides obtained by cleavage with pepsin and with Staphylococcus aureus protease. Ital. J. Biochem. 28, 478-490.
39. Barra, D., Bossa, F., Doonan, S., Fahmy, H.M.A., Hughes, G.J., Martini, F., Petruzzelli, R. & Wittmann-Liebold, B. (1980). The cytosolic and mitochondrial aspartate aminotransferases from pig heart: a comparison of their primary structures, predicted secondary structures and some physical properties. Eur. J. Biochem. 108, 405-414.
40. Passarella, S., Marra, E., Doonan, S. & Quagliariello, E (1980). Selective permeability of rat liver mitochondria to purified malate dehydrogenase isoenzymes in vitro. Biochem. J. 192, 649-658.
41. Marra, E., Passarella, S., Doonan, S., Quagliariello, E. & Saccone, C. (1980). Protease resistance of aspartate aminotransferase imported in mitochondria. FEBS Lett. 122, 33-36.
42. Barry, F.P., Doonan, S. & Ross, C.A. (1981). Cleavage by trypsin and by the proteinase from Armillaria mellea at e -N-formyl-lysine residues. Biochem. J. 193, 737-742.
43. Porter, P.B., Barra, D., Bossa, F., Cantalupo, G., Doonan, S., Martini, F., Sheehan, D. & Wilkinson, S.M. (1981). Purification and basic properties of the aspartate aminotransferases from a variety of sources. Comp. Biochem. Physiol. 69B, 737-746.
44. Doonan, S., Barra, D., Bossa, F., Porter, P.B. & Wilkinson, S.M. (1981). Interspecies comparisons of aspartate aminotransferases based on amino acid compositions. Comp. Biochem. Physiol. 69B, 747-752.
45. Bossa, F., Barra, D., Martini, F., Schinina, E.,
Doonan, S. & O’Donovan, K.M.C. (1981). Interspecies comparisons of aspartate aminotransferases based on terminal and active site sequences. Comp. Biochem. Physiol. 69B, 753-760.
46. Porter, P.B.,
Doonan, S. & Pearce, F.L. (1981). Interspecies comparisons of aspartate aminotransferases based on immunochemical methods. Comp. Biochem. Physiol. 69B, 761-767.
47. Passarella, S., Marra, E., Doonan, S., Languino, L.R., Saccone, C. & Quagliariello, E. (1982). Uptake of aspartate aminotransferase into mitochondria in vitro depends on the transmembrane pH gradient. Biochem. J. 202, 353-362.
48. Marra, E., Passarella, S., Doonan, S., Serafino, M.R., Saccone, C. & Quagliariello, E. (1982). Uptake of mitochondrial isozymes into mitoplasts. Bull. Mol. Biol. Med. 7, 97-104.
49. Passarella, S., Marra, E., Doonan, S. & Quagliariello, E. (1983). Uptake of malate dehydrogenase into mitochondria in vitro: some characteristics of the process. Biochem. J. 210, 207-214.
50. Martini, F., Angelaccio, S., Barra, D., Doonan, S. & Bossa, F. (1983). Primary structure of aspartate aminotransferase from horse heart and comparison with that of other homotopic and heterotopic isoenzymes. Comp. Biochem. Physiol. 76B, 483-487.
51. Martini, F., Angelaccio, S., Barra, D., Doonan, S. & Bossa, F. (1984). Partial amino-acid sequence and cysteine reactivities of cytosolic aspartate aminotransferase from horse heart. Biochim. Biophys. Acta, 789, 51-56.
52. Cogan, T.M., Fitzgerald, R.J. & Doonan, S. (1984). Acetolactate synthase of Leuconostoc lactis and its regulation of acteoin production. J. Dairy Res. 51, 597-604.
53. O’Hare, M.C. & Doonan, S. (1985). Purification and structural comparisons of the cytosolic and mitochondrial isoenzymes of fumarase from pig liver. Biochim. Biophys. Acta, 827, 127-134.
54. Donnelly, D.F., O’Hare, M.C. & Doonan, S. (1985). Subcellular distribution of fumarase isoenzymes in rat liver. Int. J Biochem, 17, 279-282.
55. Marra, E., Passarella, S., Casamassima, E., Perlino, E., Doonan, S. & Quagliariello, E. (1985). Kinetic studies of the uptake of aspartate aminotransferase and malate dehydrogenase into mitochondria in vitro. Biochem. J. 228, 493-503.
56. O’Donovan, K.M.C., Doonan, S., Marra, E., Passarella, S. & Quagliariello, E. (1985). Removal of an N-terminal peptide from mitochondrial aspartate aminotransferase abolishes its interactions with mitochondria in vitro. Biochem. J. 228, 609-614.
57. Passarella, S., Marra, E., Atlante, A., Doonan, S. & Quagliariello, E. (1985). The role of metal ions in the uptake of aspartate aminotransferase and malate dehydrogenase into isolated rat liver mitochondria in vitro. FEBS Lett. 189, 235-240.
58. Martini, F., Angelaccio, S., Barra, D., Pascarella, S., Maras, B., Doonan, S. & Bossa, F. (1985). The primary structure of mitochondrial aspartate aminotransferase from human heart. Biochim. Biophys. Acta, 832, 46-51.
59. Fitzgerald, R.J., Doonan, S. & Cogan, T.M. (1986). Purification and characterisation of the D-lactate dehydrogenase from Leuconostoc lactis. Int. J. Biochem. 18, 31-38.
60. Doonan, S., Martini, F., Angelaccio, S., Pascarella, S., Barra, D. & Bossa, F. (1986). The complete amino acid sequences of cytosolic and mitochondrial aspartate aminotransferases from horse heart, and inferences on evolution of the isoenzymes. J. Mol Evol. 23, 328-335.
61. Kinsella, B.T. & Doonan, S. (1986). Nucleotide sequence of a cDNA coding for mitochondrial fumarase from human liver. Biosci Reports, 6, 921-929.
62. Barry, F. & Doonan, S. (1987). Stability to sodium dodecyl sulphate of the proteinase from Armillaria mellea: use for fragmentation of insoluble proteins. Int. J. Biochem. 19, 625-632.
63. Boonyarat, D. & Doonan, S. (1988). Purification and structural comparisons of the cytosolic and mitochondrial fumarases from baker’s yeast. Int. J. Biochem. 20, 1125-1132.
64. Falahee, M.B., Weiss, R.B., O’Connor, M., Doonan, S., Gesteland, R.F. & Atkins, J.F. (1988). Mutants of translational components that alter reading frame by two steps forward or one step back. J. Biol. Chem. 263, 18099-18103.
65. Passarella, S., Marra, E., Atlante, A., Barile, M., Doonan, S. & Quagliariello, E. (1990). Uptake of aspartate aminotransferase into mitochondria in vitro causes efflux of malate dehydrogenase and vice versa. Biochim. Biophys. Acta, 1022, 273-282.
66. Doyle, J.M., Schinina, M.E., Bossa, F. & Doonan, S. (1990). The amino acid sequence of cytosolic aspartate aminotransferase from human liver. Biochem. J. 270, 651-657.
67. Cronin, V.B., Maras, B., Barra, D. & Doonan, S. (1991). The amino acid sequence of aspartate aminotransferase from baker’s yeast (Saccharomyces cerevisiae). Biochem J. 277, 335-340.
68. Fitzgerald, R.J., Doonan, S., McKay, L.L. & Cogan, T.M. (1992). Intracellular pH and the role of D-lactate dehydrogenase in the production of metabolic end products by Leuconostoc lactis. J. Dairy Res. 59, 359-367.
69. O’Connell, J., Sheehan H.M. & Doonan, S. (1993). Construction of cDNA libraries from cultures of Armillaria mellea. Int. J. Biochem. 25, 201-207.
70. Bougeron, T., Chretien, D., Poggi-Bach, J., Doonan, S., Rabier, D., Letouze, P., Munnich, A., Rotig, A., Landrieu, P. & Rustin, P. (1994). Mutation of the fumarase gene in two siblings with progressive encephalopathy and fumarase defficiency. J. Clin. Invest. 93, 2514-2518.
71. Abruzzese, F., Greco, M., Perlino E., Doonan, S. & Marra, E. (1995). Lack of correlation between mRNA expression and enzymatic activity of the aspartate aminotransferase isoenzymes in various tissues of the rat. FEBS Lett. 366, 170-172.
72. Marra, E., Azzariti, A., Giannattasio, S., Doonan, S. & Quagliariello, E. (1995). Cummulative effects of mutations in newly-synthesised aspartate aminotransferase on uptake into mitochondria. Biochem. Biophys. Res. Commun. 214, 511-517.
73. Azzariti, A., Giannattasio, S., Doonan, S., Merafina, R.S., Marra, E. & Quagliariello, E. (1995). Use of protease sensitivity to probe the conformations of newly-synthesised mutant forms of mitochondrial aspartate aminotransferase. Biochem. Biophys. Res. Commun. 215, 800-807.
74. Atlante, A., Abruzzese, F., Seccia, T.M., Vulpis, V., Doonan, S., Pirelli, A. & Marra, E. (1995). Changes in enzyme levels in hypertensive heart tissue. Biochem. Mol. Biol. Int. 37, 983-990.
75. Twomey, C.M. & Doonan, S. (1997). Comparative study of the thermal inactivation of cytosolic and mitochondrial aspartate aminotransferases. Biochim. Biophys. Acta, 1342, 37-44.
76. O’Farrell, P.A., Sannia, G., Walker, J.M. & Doonan, S. (1997). Cloning and sequencing of aspartate aminotransferase from Thermus aquaticus YT1. Biochem. Biophys. Res. Commun. 239, 810-815.
77. Jeffery, C.J., Barry, T.M., Doonan, S., Petsko, G.A. & Ringe, D. (1998). Crystallization and preliminary X-ray diffraction analysis of aspartate aminotransferase from Saccharomyces cerevisiae. Acta Cryst. D54, 659-661.
78. Jeffery, C.J., Barry, T.M., Doonan, S., Petsko, G.A. & Ringe, D. (1998). Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase. Prot. Sci. 7, 1380-1387.
79. Azzariti, A., Vacca, R.A., Giannattasio, S., Merafina, R.S., Marra, E. & Doonan, S. (1998). Kinetic properties and thermal stabilities of mutant forms of mitochondrial aspartate aminotransferase. Biochim. Biophys. Acta, in the press.
80. Lawton, J.M. & Doonan, S. (1998). Thermal inactivation and chaperonin-mediated renaturation of mitochondrial aspartate aminotransferase Biochem. J. 334, 219-224.
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