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<ol><li> <p><a></a>Makarchikov AF, Lakaye B, Gulyai IE, Czerniecki J, Coumans B, Wins P, Grisar T, Bettendorff L: <strong>Thiamine triphosphate and thiamine triphosphatase activities: from bacteria to mammals.</strong> </p> <p><em>Cell Mol Life Sci</em> 2003, <strong>60</strong><strong>:</strong>1477-1488. </p> </li> <li> <p><a></a><strong>Enzyme Nomenclature</strong> [http://www.expasy.ch/enzyme/] </p> </li> <li> <p><a></a>Lakaye B, Wirtzfeld B, Wins P, Grisar T, Bettendorff L: <strong>Thiamine triphosphate, a new signal required for optimal growth of Escherichia coli during amino acid starvation.</strong> </p> <p><em>J Biol Chem</em> 2004, <strong>279</strong><strong>:</strong>17142-17147. </p> </li> <li> <p><a></a>Bettendorff L, Wirtzfeld B, Makarchikov AF, Mazzucchelli G, Frederich M, Gigliobianco T, Gangolf M, De Pauw E, Angenot L, Wins P: <strong>Discovery of a natural thiamine adenine nucleotide.</strong> </p> <p><em>Nat Chem Biol</em> 2007, <strong>3</strong><strong>:</strong>211-212. </p> </li> <li> <p><a></a>Dawson EMC, Elliott DC, Elliott WH, Jones KM: <em>Data for Biochemical Research</em>. 3rd edition. Oxford: Oxford Science Publications; 1986. </p> </li> <li> <p><a></a>Yuan J, Fowler WU, Kimball E, Lu W, Rabinowitz JD: <strong>Kinetic flux profiling of nitrogen assimilation in Escherichia coli.</strong> </p> <p><em>Nat Chem Biol</em> 2006, <strong>2</strong><strong>:</strong>529-530. </p> </li> <li> <p><a></a>Kurganov BI: <em>Allosteric enzymes</em>. Moscow: Nauka; 1978. </p> </li> <li> <p><a></a>Nelson DL, Cox MM: <em>Lehninger Principles of Biochemistry</em>. New York: Worth Publishers; 2000.</p> </li> <li> <p><a></a>Barchi RL, Viale RO: <strong>Membrane-associated thiamin triphosphatase. II. Activation by divalent cations.</strong> </p> <p><em>J Biol Chem</em> 1976, <strong>251</strong><strong>:</strong>193-197. </p> </li> <li> <p><a></a>Shikata H, Egi Y, Koyama S, Yamada K, Kawasaki T: <strong>Properties of the thiamin triphosphate-synthesizing activity catalyzed by adenylate kinase (isoenzyme 1).</strong> </p> <p><em>Biochem Int</em> 1989, <strong>18</strong><strong>:</strong>943-949. </p> </li> <li> <p><a></a>Lakaye B, Makarchikov AF, Antunes AF, Zorzi W, Coumans B, De Pauw E, Wins P, Grisar T, Bettendorff L: <strong>Molecular characterization of a specific thiamine triphosphatase widely expressed in mammalian tissues.</strong> </p> <p><em>J Biol Chem</em> 2002, <strong>277</strong><strong>:</strong>13771-13777. </p> </li> <li> <p><a></a>Winkler W, Nahvi A, Breaker RR: <strong>Thiamine derivatives bind messenger RNAs directly to regulate bacterial gene expression.</strong> </p> <p><em>Nature</em> 2002, <strong>419</strong><strong>:</strong>952-956. </p> </li> <li> <p><a></a>Mironov AS, Gusarov I, Rafikov R, Lopez LE, Shatalin K, Kreneva RA, Perumov DA, Nudler E: <strong>Sensing small molecules by nascent RNA. A mechanism to control transcription in bacteria.</strong> </p> <p><em>Cell</em> 2002, <strong>111</strong><strong>:</strong>747-756. </p> </li> <li> <p><a></a>Bradford MM: <strong>A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.</strong> </p> <p><em>Anal Biochem</em> 1976, <strong>72</strong><strong>:</strong>248-254. </p> </li> <li> <p><a></a>Bettendorff L, Peeters M, Jouan C, Wins P, Schoffeniels E: <strong>Determination of thiamin and its phosphate esters in cultured neurons and astrocytes using an ion-pair reversed-phase high-performance liquid chromatographic method.</strong> </p> <p><em>Anal Biochem</em> 1991, <strong>198</strong><strong>:</strong>52-59. </p> </li> </ol>
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