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                                                                             References      261
                        B. Topley (1949). Condensed phosphates. Q. Rev. Chem. Soc., 3, 345–370.
                        A. Torriani-Gorini (1994). Introduction of Pho regulon of E. coli. In A. Torriani-Gorini, S. Silver and
                          E. Yagil (Eds), Phosphate in Microorganisms, American Society of Microbiology, Washington,
                          DC, USA, pp. 1–4.
                        D. Tranqui, M. Laugt and J. C. Guitel (1969). Structure cristalline du polyphosphate de cuirve-
                          ammonium: Cu(NH 4 )(PO 3 ) 3 . Bull. Soc. Fr. Mineral. Cristallogr., 92, 329–334.
                        P. L. Trelstad, P. Purdhani, W. Geisdorfer, W. Hillen and J. D. Keasling (1999). Polyphosphate kinase
                          of Acinetobacter sp. strain ADP1: purification and characterization of the enzyme and its role
                          during changes in extracellular phosphate level. Appl. Environ. Microbiol., 65, 3780–3786.
                        L. V. Trilisenko, V. M. Vagabov and I. S. Kulaev (1980). The isolation and some peculiarities of
                          Neurospora crassa mutant with deficiency in polyphosphate phosphohydrolase (in Russian).
                          Mikrobiologiya, 49, 82–87.
                        L. V. Trilisenko, V. M. Vagabov and I. S. Kulaev (1982a). Comparative study of some properties of
                          polyphosphate phosphohydrolase in Neurospora crassa strain ad-6 (28610) and a leaky derivative.
                          Neurospora Lett., 29, 19–20.
                        L. V. Trilisenko, V. M. Vagabov and I. S. Kulaev (1982b). The study of some properties of
                          polyphosphate phosphohydrolase in leaky mutant of Neurospora crassa. Biokhimiya (Moscow),
                          47, 1963–1969.
                        L. V. Trilisenko, O. N. Il’inskaya, V. M. Vagabov and I. S. Kulaev (1985a). Inorganic polyphosphates
                          and polyphosphate phosphohydrolase in mycelial strains and slime-variants of Neurospora crassa.
                          Biokhimiya (Moscow), 50, 1120–1126.
                        L. V. Trilisenko, V. M. Vagabov and I. S. Kulaev (1985b). Intracellular localization of two polyphos-
                          phate phosphohydrolases with different substrate specificity in a ‘slime’ variant of Neurospora
                          crassa (in Russian). Dokl. Akad. Nauk SSSR, 280, 763–765.
                        L. V. Trilisenko, V. M. Vagabov and I. S. Kulaev (2002). The content and chain length of polyphosphate
                          from vacuoles of Saccharomyces cerevisiae VKM Y-1173. Biochemistry (Moscow), 67, 592–596.
                        L. V. Trilisenko, N. A. Andreeva, T. V. Kulakovskaya, V. M. Vagabov and I. S. Kulaev (2003).
                          Effect of inhibitors on polyphosphate metabolism in the yeast Saccharomyces cerevisiae under
                          hypercompensation conditions. Biochemistry (Moscow), 68, 577–581.
                        Y. A. Trotsenko and V. N. Shishkina (1990). Studies of phosphate metabolism in obligate
                          methanotrophs. FEMS Microbiol. Lett., 87, 267–272.
                        A. B. Tsiomenko, I. Augustin, V. M. Vagabov and I. S. Kulaev (1974). The interrelationship of the
                          metabolism of inorganic polyphosphates and mannan in yeasts (in Russian). Dokl. Akad. Nauk
                          SSSR, 215, 478–482.
                        K. Tsutsui (1986). Tripolyphosphate as an alternative phosphate donor in selective protein
                          phosphorylation in liver microsomes. J. Biol. Chem., 261, 2645–2653.
                        K. Tsutsumi, M. Munekata and T. Shiba (2000). Involvement of inorganic polyphosphate in
                          expression of SOS genes. Biochim. Biophys. Acta, 1493, 73–81.
                        C. M. Tzeng and A. Kornberg (1998). Polyphosphate kinase is highly conserved in many bacterial
                          pathogenes. Mol. Microbiol., 29, 381–382.
                        C. M. Tzeng and A. Kornberg (2000). The multiple activities of polyphosphate kinase of Escherichia
                          coli and their subunit structure determined by radiation target analysis. J. Biol. Chem., 275,
                          3977–3983.
                        L. Ugurbil, H. Rottenberg, R. Glynn and G. Schulman (1978).  31 P nuclear magnetic resonance
                          studies of bioenergetics and glycolysis in anaerobic Escherichia coli cells. Proc. Natl. Acad. Sci.
                          USA, 75, 2224–2228.
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