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Referencias:

• Eklund, H., Gleason, F.K., Holmgren, A., Structural and functional relations among thioredoxins of different species (1991) Proteins Struct. Funct. Genet., 11, pp. 13-28
• Martin, J., Thioredoxin, a fold for all reasons (1995) Structure, 3, pp. 245-250
• Katti, S.K., LeMaster, D.M., Eklund, H., Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution (1990) J. Mol. Biol., 212, pp. 167-184
• Wolosiuk, R.A., Ballicora, M.A., Hagelin, K., The reductive pentose phosphate cycle for photosynthetic CO2 assimilation: Enzyme modulation (1993) FASEB J., 7, pp. 622-637
• Jacquot, J.P., Lancelin, J.M., Meyer, Y., Thioredoxins: Structure and function in plant cells (1997) New Phytol., 136, pp. 543-570
• Geck, M.K., Hartman, F.C., Kinetic and mutational analysis on the regulation of phosphoribulokinase by thioredoxins (2000) J. Biol. Chem., 275, pp. 18034-18039
• Stumpp, M.T., Motohashi, K., Hisabori, T., Chloroplast thioredoxin mutants without active-site cysteines facilitate the reduction of the regulatory disulfide bridge on the γ-subunit of chloroplast ATP synthase (1999) Biochem. J., 341, pp. 157-163
• Muller, E.D.G., Buchanan, B.B., Thioredoxin is essential for photosynthetic growth (1989) J. Biol. Chem., 264, pp. 4008-4014
• Navarro, F., Florencio, J., The cyanobacterial thioredoxin gene is required for both photoautotrophic and heterotrophic growth (1996) Plant Physiol., 111, pp. 1067-1075
• Huppe, H.C., Buchanan, B.B., Activation of a chloroplast type fructose bisphosphatase from Chlamydomonas reinhardtii by light-mediated agents (1989) Z. Naturforsch., 44 c, pp. 487-494
• Ballicora, M.A., Wolosiuk, R.A., Enhancement of the reductive activation of chloroplast fructose 1,6-phosphate by modulators and protein perturbants (1994) Eur. J. Biochem., 222, pp. 467-474
• Rodriguez-Suarez, R.J., Mora-Garcia, S., Wolosiuk, R.A., Characterization of cysteine residues involved in the reductive activation and the structural stability of rapeseed (Brassica napus) chloroplast fructose 1,6-phosphate (1997) Biochem. Biophys. Res. Commun., 232, pp. 388-393
• Jacquot, J.P., Lopez-Jaramillo, J., Miginiac-Maslow, M., Lemaire, S., Cherfils, J., Chueca, A., Lopez-Gorge, J., Cysteine-153 is required for regulation of pea chloroplast fructose 1,6-phosphate (1997) FEBS Lett., 401, pp. 143-146
• Villeret, V., Huang, S., Zhang, Y., Xue, Y., Lipscomb, W.N., Crystal structure of chloroplast fructose 1,6-phosphate at 2.8 Å resolution (1995) Biochemistry, 34, pp. 4299-4306
• Geck, M.K., Larimer, F.W., Hartman, F.C., Identification of residues of spinach thioredoxin f that influence interactions with target enzymes (1996) J. Biol. Chem., 271, pp. 24736-24740
• Lopez-Jaramillo, J., Chueca, A., Jacquot, J.P., Hermoso, R., Lázaro, J.J., Sahrawy, M., Lopez-Gorge, J., High yield expression of pea thioredoxin m and assessment of its efficiency in chloroplast fructose 1,6-phosphate activation (1997) Plant Physiol., 114, pp. 1169-1175
• Mora-Garcia, S., Rodriguez-Suarez, R.J., Wolosiuk, R.A., Role of electrostatic interactions on the affinity of thioredoxin for target proteins (1998) J. Biol. Chem., 273, pp. 16273-16280
• Sambrook, J., Fritsch, E., Maniatis, T., (1989) Molecular Cloning. A Laboratory Manual, 2nd edn., , Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
• Ausubel, F.M., Brent, R., Kingston, R., Moore, E.W., Seidman, J.G., Smith, J.A., Struhl, K., (1995) Current Protocols in Molecular Biology, , John Wiley and Sons, New York
• Heuck, A.P., Wolosiuk, R.A., Fluoresceinthiocarbamyl-insulin: A potential analytical tool for the assay of disulfide bond reduction (1997) J. Biochem. Biophys. Methods, 34, pp. 213-225
• Rodriguez-Suarez, R.J., Wolosiuk, R.A., High level expression in Escherichia coli, purification and properties of chloroplast fructose 1,6-phosphate from rapeseed (Brassica napus) leaves (1995) Photosynth. Res., 46, pp. 313-322
• Jacquot, J.P., Keryer, E., Issakidis, E., Decottignies, P., Miginiac-Maslow, M., Schmitter, J.M., Cretin, C., Properties of recombinant NADP-malate dehydrogenases from Sorghum vulgare leaves expressed in Escherichia coli cells (1991) Eur. J. Biochem., 199, pp. 47-59
• Rodriguez-Suarez, R.J., Wolosiuk, R.A., Sequence of a cDNA encoding chloroplast fructose 1,6-phosphate from rapeseed (1993) Plant Physiol., 103, pp. 1453-1454
• Pace, C.N., Determination and analysis of urea and guanidine hydrochloride denaturation curves (1986) Methods Enzymol., 131, pp. 266-280
• Heuck, A.P., Wolosiuk, R.A., Di-fluoresceinthiocarbamyl-insulin: A fluorescent substrate for the assay of protein disulfide oxidoreductase activity (1997) Anal. Biochem., 248, pp. 94-101
• Hertig, C.M., Wolosiuk, R.A., Studies on the hysteretic properties of chloroplast fructose 1,6-phosphate (1983) J. Biol. Chem., 258, pp. 984-989
• Chen, P.S., Toribara, T.I., Warner, H., Microdetermination of phosphorus (1956) Anal. Chem., 239, pp. 1756-1758
• Gill, S.C., Von Hippel, P.H., Calculation of protein extinction coefficients from amino acid sequence data (1989) Anal. Biochem., 182, pp. 319-326
• Chiadmi, M., Navaza, A., Miginiac-Maslow, M., Jacquot, J.P., Cherfils, J., Redox signalling in the chloroplast: Structure of oxidized pea fructose-1,6-bisphosphate phosphatase (1999) EMBO J., 18, pp. 6809-6815
• Capitani, G., Markovic-Housley, Z., DelVal, G., Morris, M., Jansonius, J.N., Schurmann, P., Crystal structures of two functionally different thioredoxins in spinach chloroplasts (2000) J. Mol. Biol., 302, pp. 135-154
• Peitsch, M.C., Protein modeling by e-mail (1995) Biotechnology, 13, pp. 658-660
• Nicholls, A., Sharp, K., Honig, B., Protein folding and association: Insights from the interfacial and thermodynamics properties of hydrocarbons (1991) Proteins Struct. Funct. Genet., 11, pp. 281-296
• Jeng, M.F., Campbell, A.P., Begley, T., Holmgren, A., Case, D.A., Wright, P.A., Dyson, H.J., High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin (1994) Structure, 2, pp. 853-868
• Eklund, H., Gleason, F.K., Holmgren, A., Structural and functional relations among thioredoxins of different species (1991) Proteins Struct. Funct. Genet., 11, pp. 13-28
• Mora-Garcia, S., Ballicora, M.A., Wolosiuk, R.A., Chloroplast fructose 1,6-phosphate: Modification of non-covalent interactions promote the activation by chimeric Escherichia coli thioredoxins (1996) FEBS Lett., 380, pp. 123-126
• Hertig, C., Wolosiuk, R.A., A dual effect of Ca2+ on chloroplast fructose 1,6-phosphate (1980) Biochem. Biophys. Res. Commun., 97, pp. 325-333
• Schurmann, P., Roux, J., Salvi, L., Modification of thioredoxin specificity of chloroplast fructose 1,6-phosphate by substrate and Ca2+ (1985) Physiol. Veg., 23, pp. 813-818
• DeLamotte-Guery, F., Miginiac-Maslow, M., Decottignies, P., Stein, M., Minard, P., Jacquot, J.P., Mutation of a negatively charged amino acid in thioredoxin modifies its reactivity with chloroplastic enzymes (1991) Eur. J. Biochem., 196, pp. 287-294
• Prado, F.E., Lázaro, J.J., Hermoso, R., Chueca, A., Lopez-Gorge, J., Purification and properties of pea (Pisum sativum L.) thioredoxin f, a plant thioredoxin with unique features in the activation of chloroplast fructose 1,6-phosphate (1992) Planta, 188, pp. 345-353
• Schreiber, G., Fersht, A.R., Rapid electrostatically assisted association of proteins (1996) Nat. Struct. Biol., 3, pp. 427-431
• Stein, M., Wolosiuk, R.A., The effect of chaotropic anions on the activation and the activity of chloroplast fructose 1,6-phosphate (1987) J. Biol. Chem., 262, pp. 16171-16179
• Ballicora, M.A., D'Alessio, A.C., Mora-Garcia, S., Rodriguez-Suarez, R.J., Wolosiuk, R.A., The reductive modulation of chloroplast fructose 1,6-phosphate by tributylphosphine and sodium borohydride (1998) Cell. Mol. Biol., 42, pp. 673-682
• Corley, E., Wolosiuk, R.A., Hertig, C.M., Regulation of the activation of chloroplast fructose 1,6-phosphate: Inhibition by spermidine and spermine (1983) Biochem. Biophys. Res. Commun., 115, pp. 707-714
• Hu, C.-H., Tsou, C.-L., Formation of enzyme-substrate disulfide linkage during catalysis by protein disulfide isomerase (1991) FEBS Lett., 290, pp. 87-89
• Park, J., Churchich, J.E., Interaction of thioredoxin with oxidized aminobutyrate aminotransferase. Evidence for the formation of a covalent intermediate (1992) FEBS Lett., 310, pp. 1-4
• Quin, J., Clore, G.M., Kennedy, W.M.P., Huth, J.R., Gronenborn, A.M., Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NFκB (1995) Structure, 3, pp. 289-297
• Brandes, H.K., Larimer, F.W., Hartman, F.C., The molecular pathway for the regulation of phosphoribulokinase by thioredoxin f (1996) J. Biol. Chem., 271, pp. 3333-3336
• Hirasawa, M., Schurmann, P., Jacquot, J.P., Manieri, W., Jacquot, P., Keryer, E., Hartman, F.C., Knaff, D.B., Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin: Thioredoxin reductase and thioredoxin f-regulated enzymes (1999) Biochemistry, 38, pp. 5200-5205
• Schwarz, O., Schurmann, P., Strotmann, H., Kinetics and thioredoxin specificity of thiol modulation of the chloroplast H+-ATPase (1997) J. Biol. Chem., 272, pp. 16924-16927
• Haberlein, I., Wurfel, M., Follmann, H., Non-redox protein interactions in the thioredoxin activation of chloroplast enzymes (1992) Biochim. Biophys. Acta, 1121, pp. 293-296

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