Andreu, J.M., Gorbunoff, M.J., Medrano, F.J., Rossi, M. and Timasheff, S.N.  [1991]. Mechanism of colchicine binding to tubulin; tolerance of substituents in ring C´ of biphenyl analogues. Biochemistry, 30, 3777-3786.

Medrano, F.J., Andreu, J.M., Gorbunoff, M.J. and Timasheff, S.N.  [1991]. Roles of the ring C oxygens in the binding of colchicine to tubulin. Biochemistry, 30, 3770-3777.

Mozo-Villarias, A., Morros, A. and Andreu, J.M.  [1991]. Thermal transitions in the structure of tubulin. Environments of aromatic aminoacids. Eur. Biophys. J., 19, 295-300.

Andreu, J.M., Garcia de Ancos, J., Medrano, F.J., Gil, R., Diaz, J.F., Nogales, E., Towns-Andrews, E., Pantos, E. and Bordas, J  [1991]. Twelve protofilament taxol-induced microtubules assembled from purified tubulin. A synchrotron X-ray scattering study in comparison with glycerol- and MAP-induced microtubules, in The living cell in four dimensions. Amer. Inst. of Physics Conf. Proc.

Peyrot, V., Briand, C. and Andreu, J.M.  [1991]. Limited proteolysis of tubulin by subtilisin induces ring formation, in The living cell in four dimensions. Amer. Inst. of Physics Conf. Proc. 226, 181-186.

Diaz, J.F. and Andreu, J.M.  [1991]. Kinetics of dissociation of the tubulin-colchicine complex. Complete reaction scheme and comparison to thermodynamic measurements. J. Biol. Chem., 26, 2890-2896.

Arévalo, M.A., Nieto, J.M., Andreu, D. and Andreu, J.M.  [1990]. Tubulin assembly probed with antibodies to synthetic peptides. J. Mol. Biol., 214, 105-12048.

Peyrot, V., Briand, C. and Andreu, J.M.  [1990]. C-Terminal cleavage of tubulin by subtilisin enhances ring formation. Arch. Biochem. Biophys. 279, 328-337.

Peyrot, V., Leynadier, D. Sarrazin, M., Briand, C., Rodriguez, A., Nieto, J.M. and Andreu, J.M.  [1989]. Interaction of tubulin and cellular microtubules with the new antitumour drug MDL 27048, a powerful reversible microtubule inhibitor. J. Biol. Chem. 264, 21296-21301.

Menendez, M., Laynez, J., Medrano, F.J. and Andreu, J.M.  [1989]. A thermodynamic study of the interaction of tubulin with colchicine site ligands.

Mollinedo, F. Nieto, J.M. and Andreu, J.M.  [1989]. Cytoplasmic microtubules in human neutrophil degranulation.Reversible inhibition by the colchicineanalog MTC. Molecular Pharmacol. 36, 547-555.

Vivo, A., Andreu, J.M., De la Viña, J. and De Felipe, M.C.  [1989]. Leghemoglobin in lupin plants. Plant Physiol., 90, 452-457.

Medrano, F.J., Andreu, J.M., Gorbunoff, M.J. & Timasheff, S.N.  [1989]. The roles of colchicine rings B and C in the binding process to tubulin. Biochemistry 28, 5589-5599.

Andreu, J.M., Garcia de Ancos, J. Starling, D. Hodgkinson, J. and Bordas, J.  [1989]. A Synchrotron X-Ray scattering study of purified calf brain tubulin and of its expansion induced by mild detergent binding. Biochemistry 28, 4036-4040.

De la Viña, S., Andreu, D., Medrano, F.J., Nieto, J.M. and Andreu, J.M.  [1988]. Tubulin structure probed with antibodies to synthetic peptides. Mapping of three major types of limited proteolysis fragments. Biochemistry 27, 5352 5365.

Andreu, D., De la Viña, S. and Andreu, J.M.  [1988]. Chemical synthesis of five tubulin antigenic sequences : production and characterization of their corresponding anti-tubulin monospecific antibodies. Intl. J. Peptide Protein Res. 31, 555-566.

. Andreu, D., De la Viña, S. and Andreu, J.M.  [1988]. Tubulin domains examined by antibodies from synthetic peptides. Peptides: Chemistry and Biology (G.R. Marshall ed.), pp. 534-536.

Diez, J.C., Avila, J., Nieto, J.M. and Andreu, J.M.  [1987]. Reversible inhibition of microtubules and cell growth by the bicyclic colchicine analogue MTC. Cell Motil. Cytosk., 7, 178-186.

Andreu, J.M., De la Torre, J. and Carrascosa, J.L.  [1986]. Interaction of tubulin with octylglucoside and deoxycholate II.Protein conformation, binding of colchicine site ligands and microtubule assembly. Biochemistry 25, 5230-5239.

Andreu, J.M. and Muñoz, J.A.  [1986]. Interaction of tubulin with octylglucoside and deoxycholate. I. Binding and hydrodynamic studies. Biochemistry 25, 5220-5229.