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Arnold, K., Bordoli, L., Kopp, J. and Schwede, T. (2006). The SWISS-MODEL Workspace: A web-based
environment for protein structure homology modeling, Bioinformatics. 222, 195-201.
Company, P., Gonzalez-Bosch, C. (2003). Identification of a copper chaperone from tomato fruits infacted with
Botrytis cinerea by differential display. Biochemical and Biophysical Research Communications.
304, 825-830.
Hall, T.A. (1999). BioEdit : a user-griendly biological sequence alignment editor and analysis program for
Window 95/98/NT. Nucleic Acids Symposium Series. 41, 95-98.
Lin, S.J. and Culotta, V.C. (1995). The Atx1 gene of Saccharomyces cerevisiae endoces a small metal
homeostasis factor that protects cell against reactive oxygen toxicity. Proceedings of the National
Academy of Science of United states of America. 92, 3784-3788.
Mira, H., Vilar, M., Perez-Paya, E. and Penarrubia, L. (2001b). Functional and conformational properties of the
exclusive C-domain from the Arabidopsis copper chaperone (CCH). Biochemical Jourmal. 357, 545-
549.
Pufahl, R., Singer, C. and Peariso, K. (1997). Metal ion chaperone function of the solution Cu(I) receptor Atx1.
Science. 278, 858-856.
Wernimont, A.K., Huffman, D.L., Lamb. A.L., O’Halloran, T.V. and Rosenzweig, A.C. (2000). Structure basis
for copper transfer by the metallochaperone for the Menkes/Wilson disease protein. Nature Structural
Biology. 7, 766-771.