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Referencias:

• Arikan, S., Lozano-Chiu, M., Paetznick, V., Rex, J.H., In vitro susceptibility testing methods for caspofungin against Aspergillus and Fusarium isolates (2001) Antimicrob Agents Chemother, 45, pp. 327-330
• Barth, G., Gaillardin, C., Physiology and genetics of the dimorphic fungus Yarrowia lipolytica (1997) FEMS Microbiol Rev, 19, pp. 219-237
• Bartnicki-Garcia, S., Reyes, E., Polyuronides in the cell wails of Mucor rouxii (1968) Biochim Biophys Acta, 170, pp. 54-62
• Bartnicki-García, S., Nickerson, W.K., Nutrition, growth and morphogenesis of Mucor rouxii (1962) J Bacteriol, 83, pp. 841-858
• Cabib, E., Drgonova, J., Drgon, T., Role of small G proteins in yeast cell polarization and wall biosynthesis (1998) Annu Rev Biochem, 67, pp. 307-333
• Corbett, K.D., Alber, T., The many faces of Ras: Recognition of small GTP-binding proteins (2001) Trends Biochem Sci, 26, pp. 710-716
• DeMali, K.A., Wennerberg, K., Burridge, K., Integrin signaling to the actin cytoskeleton. Comparison of morphogenetic networks of filamentous fungi and yeast (2003) Curr Opin Cell Biol, 15, pp. 572-582
• Dow, J.M., Rubery, P.H., Chemical fractionation of the cell walls of mycelial and yeast-like forms of Mucor rouxii: A comparative study of the polysaccharide and glycoprotein components (1977) J Gen Microbiol, 99, pp. 29-41
• Ellerbroek, S.M., Wennerberg, K., Burridge, K., Serine phosphorylation negatively regulates RhoA in vivo (2003) J Biol Chem, 278, pp. 19023-19031
• Forget, M.A., Desrosiers, R.R., Gingras, D., Beliveau, R., Phosphorylation states of Cdc42 and RhoA regulate their interactions with Rho GDP dissociation inhibitor and their extraction from biological membranes (2002) Biochem J, 361, pp. 243-254
• Gancedo, J.M., Control of pseudohyphae formation in Saccharomyces cerevisiae (2001) FEMS Microbiol Rev, 25, pp. 107-123
• Guest, M.G., Lin, X., Momany, M., Aspergillus nidulans RhoA is involved in polar growth, branching and cell wall synthesis (2004) Fungal Genet Biol, 41, pp. 13-22
• Haidle, C.W., Storck, R., Control of dimorphism in Mucor rouxii (1966) J Bacteriol, 92, pp. 1236-1244
• Hancock, J.F., Cadwallader, K., Paterson, H., Marshall, C.J., A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins (1991) EMBO J, 10, pp. 4033-4039
• Harris, S.D., Momany, M., Polarity in filamentous fungi: Moving beyond the yeast paradigm (2004) Fungal Genet Biol, 41, pp. 391-400
• Harris, S.D., Read, N.D., Roberson, R.W., Shaw, B., Seiler, S., Plamann, M., Momany, M., Polarisome meets spitzenkorper: Microscopy, genetics, and genomics converge (2005) Eukar Cell, 4, pp. 225-229
• Ibrahim, A.S., Bowman, J.C., Avanessian, V., Brown, K., Spellberg, B., Edwards Jr., J.E., Douglas, C.M., Caspofungin inhibits Rhizopus oryzae 1,3-beta-D-glucan synthase, lowers burden in brain measured by quantitative PCR, and improves survival at a low but not a high dose during murine disseminated zygomycosis (2005) Antimicrob Agents Chemother, 49, pp. 721-727
• Inoue, S.B., Qadota, H., Arisawa, M., Anraku, Y., Watanabe, T., Ohya, Y., Signaling toward yeast 1,3-beta-glucan synthesis (1996) Cell Struct Funct, 5, pp. 395-402
• Jaffe, A.B., Hall, A., Rho GTPases: Biochemistry and biology (2005) Annu Rev Cell Dev Biol, 21, pp. 247-269
• Kurtz, M.B., Heath, I.B., Marrinan, J., Dreikorn, S., Onishi, J., Douglas, C., Morphological effects of lipopeptides against Aspergillus fumigatus correlate with activities against (1,3)-β-D-glucan synthase (1994) Antimicrob Agents Chemother, 38, pp. 1480-1489
• Lang, P., Gesbert, F., Delespine-Carmagnat, M., Stancou, R., Pouchelet, M., Bertoglio, J., Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes (1996) EMBO J, 15, pp. 510-519
• Lee, N., D'Souza, C.A., Kronstad, J.W., Of smuts, blasts, mildews, and blights: cAMP signaling in phytopathogenic fungi (2003) Annu Rev Phytopathol, 41, pp. 399-427
• Lengeler, K.B., Davidson, R.C., D'Souza, C.A., Harashima, T., Shen, W.C., Wang, P., Pan, X., Heitman, J., Signal transduction cascades regulating fungal development and virulence (2000) Microbiol Mol Biol Rev, 64, pp. 746-785
• Letscher-Bru, V., Herbrecht, R., Caspofungin: The first representative of a new antifungal class (2003) J Antimicrob Chemother, 51, pp. 513-521
• Levin, D.E., Cell wall integrity signaling in Saccharomyces cerevisiae (2005) Microbiol Mol Biol Rev, 69, pp. 262-291
• Linz, J.E., Katayama, C., Sypherd, P.S., Three genes for the elongation factor EF-1α in Mucor racemosus (1986) Mol Cell Biol, 6, pp. 593-600
• Madaule, P., Axel, R., Myers, A.M., Characterization of two members of the rho gene family from the yeast Saccharomyces cerevisiae (1987) Proc Natl Acad Sci USA, 84, pp. 779-783
• Madhani, H.D., Fink, G.D., The control of filamentous differentiation and virulence in fungi (1998) Trends Cell Biol, 8, pp. 335-348
• Odds, F.C., Brown, A.J., Gow, N.A., Antifungal agents: Mechanisms of action (2003) Trends Microbiol, 11, pp. 272-279
• Paduch, M., Jeleń, F., Otlewski, J., Structure of small G proteins and their regulators (2001) Acta Biochim Pol, 48, pp. 829-850
• Peitsch, M.C., Protein modeling by E-mail (1995) Bio/Technology, 13, pp. 658-660
• Peitsch, M.C., ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling (1996) Biochem Soc Trans, 24, pp. 274-279
• Pereyra, E., Mizyrycki, C., Moreno, S., Threshold level of protein kinase A activity and polarized growth in Mucor rouxii (2000) Microbiology, 146, pp. 1949-1958
• Pereyra, E., Argimón, S., Jackson, S.L., Moreno, S., RGD-containing peptides and cAMP have antagonistic roles in the morphology of Mucor rouxii (2003) Protoplasma, 222, pp. 23-30
• Pereyra, E., Zaremberg, V., Moreno, S., The effect of dibutyryl-cAMP on growth and morphology of germinating Mucor rouxii sporangiospores (1992) Exp Mycol, 16, pp. 93-101
• Pereyra, E., Ingerfeld, M., Neal, A., Jackson, S.L., Moreno, S., (2006) Mucor Rouxii Ultrastructure: CAMP and Actin Cytoskeleton, , Protoplasma in press
• Qadota, H., Anraku, Y., Botstein, D., Ohya, Y., Conditional lethality of a yeast strain expressing human RHOA in place of RHO1 (1994) Proc Natl Acad Sci USA, 91, pp. 9317-9321
• Ramirez-Ramirez, N., Garcia-Soto, J., Gonzalez-Hernandez, A., Martinez-Cadena, G., The small GTP-binding protein Rho is expressed differentially during spore germination of Phycomyces blakesleeanus (1999) Microbiology, 145, pp. 1097-1104
• Rolli-Derkinderen, M., Sauzeau, V., Boyer, L., Lemichez, E., Baron, C., Henrion, D., Loirand, G., Pacaud, P., Phosphorylation of serine 188 protects RhoA from ubiquitin/ proteasome-mediated degradation in vascular smooth muscle cells (2005) Circ Res, 96, pp. 1152-1160
• Rose, T.M., Henikoff, J.G., Henikoff, S., CODEHOP (COnsensus-DEgenerate Hybrid Oligonucleotide Primer) PCR primer design (2003) Nucleic Acids Res, 31, pp. 3763-3766
• Roskoski, R., Assays of protein kinase (1983) Methods Enzymol, 99, pp. 3-6
• Roze, L.V., Mahanti, N., Mehigh, R., McConnell, D.G., Linz, J.E., Evidence that MRas1 and MRas3 proteins are associated with distinct cellular functions during growth and morphogenesis in the fungus Mucor racemosus (1999) Fungal Genet Biol, 28, pp. 171-189
• Rua, D., Tobe, B.T., Kron, S.J., Cell cycle control of yeast filamentous growth (2001) Curr Opin Microbiol, 4, pp. 720-727
• Ruge, E., Korting, H.C., Borelli, C., Current state of three-dimensional characterisation of antifungal targets and its use for molecular modelling in drug design (2005) Int J Antimicrob Agents, 26, pp. 427-441
• Seiler, S., Plamann, M., The genetic basis of cellular morphogenesis in the filamentous fungus Neurospora crassa (2003) Mol Biol Cell, 14, pp. 4352-4364
• Wendland, J., Comparison of morphogenetic networks of filamentous fungi and yeast (2001) Fungal Genet Biol, 34, pp. 63-82
• Wendland, J., Walther, A., Ashbya gossypii: A model for fungal developmental biology (2005) Nature Rev Microbiol, 3, pp. 421-429
• Zaremberg, V., Donella-Deana, A., Moreno, S., Mechanism of activation of cAMP-dependent protein kinase: In Mucor rouxii the apparent specific activity of the cAMP-activated holoenzyme is different than that of its free catalytic subunit (2000) Arch Biochem Biophys, 381, pp. 74-82

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