Voir la thématique générale.

Voir un cours sur les protéines de stress LEA et HSP.

Base de données LEAPdb (Jaspard & Hunault)

Base de données sHSPdb (Jaspard & Hunault)

Baneyx, F. (1999) " Recombinant protein expression in Escherichia coli " Curr. Opin. Struct. Biol. 10, 411 - 421

Blattner, F. R., Burland, V., Plunkett, G. III, Sofia, H. J., & Daniels, D. L. (1993) " Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes " Nucleic Acids Res. 21, 5408 - 5417

Blattner, F. R., Plunkett, G. III, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., & Shao, Y. (1997) "  The complete genome sequence of Escherichia coli K-12 " Science 277, 1453 - 1474

Bradford, M. M. (1976) " A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding " Anal. Biochem. 72, 248 - 254

Braig, K . (1998) " Chaperonins " Curr. Opin. Struct. Biol. 8, 159 - 165

Carrio, M. M., Corchero, J. L., & Villaverde, A. (1998) " Dynamic of in vivo protein aggregation : building inclusion bodies in recombinant bacteria " FEMS Microbiol. Lett. 169, 9 - 15

Carrio, M. M., Corchero, J. L., & Villaverde, A. (1999) " Proteolytic digestion of bacterial inclusion body proteins during dynamic transition between soluble and insoluble forms " Bioch. Biophys. Acta. 1434, 170 - 176

Clarke, A. R. (1996) " Molecular chaperones in protein folding and translocation " Curr. Opin. Struct. Biol. 6, 43 - 50

De Bernardez Clark, E. (1998) " Refolding of recombinant proteins " Curr. Opin. Struct. Biol. 9, 157 - 163

Ellis, R. J . (1987) " Protein as molecular chaperones " Nature 328, 378 - 379

Ellis, R. J. (1994) " Roles of molecular chaperones in protein folding " Curr. Opin. Struct. Biol. 4, 117 - 122

Ellis, R. J., & Hartl, F. U. (1999) " Principles of protein folding in the cellular environment " Curr. Opin. Struct. Biol. 9, 102 - 110

Gething, M. J., & Sambrook, J. (1992) " Protein folding in the cell " Nature 355, 33 - 45

Gunasekera, D., & Kemp, R. G. (1999) " Cloning, sequencing, expression, and purification of the C isozyme of mouse phosphofructokinase " Prot. Expr. and Purif. 16, 448 - 453

Härndahl, U., Tufvesson, E., & Sundby, C. (1998) " The chloroplast small heat shock protein - purification and characterization of pea recombinant protein " " Prot. Expr. and Purif. 14, 87 - 96

Horton, H. R., Moran, L. A., Ochs, R. S., Rawn, J. D., & Scrimgeour, K. G. (1994) " Principes de Biochimie " De Boeck Université, Bruxelles

Hunault, G., & Jaspard, E. (2010) "LEAPdb: a database for the late embryogenesis abundant proteins" BMC Genomics 11, 221

Jaspard, E., & Hunault, G. (2016) "sHSPdb: a database for the analysis of small Heat Shock Proteins" BMC Plant Biol. 16, 135

Lamb, A. L., Wernimont, A. K., Pufahl, R. A., O’Halloran, T. V., & Rosenzweig, A. C. (2000) " Crystal structure of the second domain of the human copper chaperone for superoxide dismutase " Biochemistry 39, 1589 - 1595

Laemmli, U. K. (1970) " Cleavage of structural proteins during the assembly of the head of bacteriophage T4 " Nature 227, 680 - 685

Lee, G. J., Pokala, N., & Vierling, E. (1995) " Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea " J. Biol. Chem. 270, 10432 - 10438

Lenne, C., & Douce, R. (1994) " A low molecular mass heat-shock protein is localized to higher plant mitochondria " Plant Physiol. 105, 1255 - 1261 

Lenne, C., Block, M. A., Garin, J., & Douce, R. (1995) " Sequence and expression of the mRNA encoding HSP22, the mitochondrial small heat-shock protein in pea leaves " Biochem. J. 311, 805 - 813

Lilie, H., Schwarz, E., & Rudolph, R. (1998) " Advances in refolding of proteins produced in E. coli " Curr. Opin. Struct. Biol. 9, 497 - 501

Lund, A. A., Blum, P. H., Bhattramakki, D., & Elthon, T. E. (1998) " Heat-stress response of maize mitocondria " Plant Physiol. 116, 1097 - 1110

Missiakas, D., & Raina, S. (1997) " Protein folding in the bacterial periplasm " J. Bacteriol. 179, 2465 - 2471

Patra, A. K., Mukhopadhyay, R., Mukhija, R., Krishnan, A., Garg, L. C., & Panda, A. K. (2000) " Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli " Prot. Expr. and Purif. 18, 182 - 192

Rogl, H., Kosemund, K., Kühlbrandt, W., & Collinson, I. (1998) " Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography " FEBS Lett. 432, 21 - 26

Shearstone, J. R., & Baneyx, F. (1999) "  Biochemical characterization of the small heat shock protein IbpB from Escherichia coli " J. Biol. Chem. 274, 9937 - 9945

Umakoshi, H., Yano, K., Kuboi, R., & Komasawa, I. (1996) " Extractive cultivation of recombinant Escherichia coli using aqueous two-phase system for production and separation of intracellular heat shock proteins " Biotechnol. Prog. 12, 51 - 56

Vierling, E. (1991) " The roles of heat shock proteins in plants " Ann. Rev. Plant Physiol. Plant Mol. Biol. 42, 579 - 620

Waters, E. R., Lee, G. J., & Vierling, E. (1996) " Evolution structure and function of the small heat-shock protein in plants " J. Exp. Bot. 47, 325 -338

Wilharm, E., Parry, M. A. A., Friebel, R., Tschesche, H., Matschiner, G., Sommerhoff, C. P., & Jenne, D. E. (1999) " Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma " J. Biol. Chem. 274, 27331 - 27337

Wood, C. K., Pratt, J. R., & Moore, A. L. (1998) " Identification and characterisation of cultivar-specific 22-kDa heat-shock proteins from mitochondria of Pisum sativum " Physiol. Plant. 103, 369 - 376

Zavialov, A., Benndorf, R., Ehrnsperger, M., Zav’yalov, V., Dudich, I., Buchner, J., & Gaestel, M. (1998) " The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25 " Int. J. Biol. Macromolec. 22, 163 - 173