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Referencias:

• Adham, I., Klemm, U., Maier, W., Engel, W., Molecular cloning of human preproacrosin cDNA (1990) Human Genet., 84, pp. 125-128
• Baba, T., Kashiwabara, S., Watanabe, K., Hisao, I., Michikawa, Y., Kimura, K., Takada, M., Arai, Y., Activation and maturation mechanism of boar acrosin zymogen based on the deduced primary structure (1989) J. Biol. Chem., 264, pp. 11920-11927
• Baba, T., Watanabe, K., Kashiwabara, S., Arai, Y., Primary structure of human proacrosin deduced from its cDNA sequence (1989) FEBS Lett., 244, pp. 296-300
• Baba, T., Michikawa, Y., Kawakura, K., Arai, Y., Activation of boar proacrosin is affected by processing at both N- and C-terminal portions of the zymogen molecule (1989) FEBS Lett., 244, pp. 132-136
• Baba, T., Niida, Y., Michikawa, Y., Kashiwabara, S., Kodaira, K., Takenaka, M., Kohno, N., Arai, Y., An acrosomal protein, sp32, in mammalian sperm is a binding protein specific for two proacrosin and an acrosin intermediate (1994) J. Biol. Chem., 269, pp. 10133-10140
• Brown, C.R., Harrison, R.A.P., The activation of proacrosin in spermatozoa from ram, bull and boar (1978) Biochim. Biophys. Acta, 526, pp. 22-217
• Bucher, P., Bairoch, A., A generalised profile syntax for biomolecular sequences motifs and its function in automated sequence interpretation (1994) ISMB-94, Proceedings 2nd International Conference on Intelligent Systems for Molecular Biology, pp. 53-61. , Altman, R., Brutlag, D., Karp, P., Lathrop, R., Searls, D. (Eds.). AAAI Press, Menlo Park
• Calvo, L., Vantman, D., Banks, S.M., Tezon, J., Koukoulis, G.N., Dennison, L., Sherins, R.I., Follicular fluid-induced acrosome reactin distinguishes a subgroup of men with unexplained infertility not identified by semen analysis (1989) Fertil. Steril., 52, p. 1048
• Crosby, J.A., Jones, R., Barros, C., Carballo, P., Characterisation of the functional domains of boar acrosin involved in nonenzymatic binding to homologous zona pellucida glycoproteins (1998) Mol. Reprod. Dev., 49, pp. 426-434
• De Jonge, C.J., Tarchala, S.M., Rawlins, R.G., Binor, Z., Radwanska, E., Acrosin activity in human spermatozoa in relation to semen quality and in-vitro fertilization (1993) Human Reprod., 8, pp. 253-257
• Eberspaecher, U., Gerwien, J., Habenicht, U., Schleuning, W., Donner, P., Activation and subsequent degradation of proacrosin is mediated by zona pellucida glycoproteins, negatively charged polysaccharides, and DNA (1991) Mol. Reprod. Dev., 30, pp. 164-170
• Florman, H.M., Tombes, R.M., First, N.L., Babcock, D.F., An adhesion-associated agonist from the zona pellucida activates G protein-promoted elevations of internal Ca2+ and pH that mediate mammalian sperm acrosomal exocytosis (1989) Dev. Biol., 135, pp. 133-146
• Furlong, L.I., Hellman, U., Krimer, A., Tezon, J.G., Charreau, E.H., Vazquez-Levin, M.H., Expression of human proacrosin in Escherichia coli and binding to zona pellucida (2000) Biol. Reprod., 62, pp. 606-615
• Gallo, J., Escalier, D., Grellier, P., Précigout, E., Albert, M., David, G., Schrével, A., Characterization of a monoclonal antibody to human proacrosin and its use in acrosomal status evaluation (1991) J. Histochem. Cytochem., 39, pp. 273-282
• Hardy, D.M., Oda, M.N., Friend, D.S., Huang, T.T.F., A mechanism for differential release of acrosomal enzymes during the acrosome reaction (1991) Biochem. J., 275, pp. 759-766
• Hofmann, K., Bucher, P., Falquet, L., Bairoch, A., The PROSITE database, its status in 1999 (1999) Nucleic Acid Res., 27, pp. 215-219
• Jansen, S., Jones, R., Jenneckens, I., Marschall, B., Kriegesmann, B., Coadwell, J., Brenig, B., Site-directed mutagenesis of boar proacrosin reveals residues involved in binding of zona pellucida glycoproteins (1998) Mol. Reprod. Dev., 51, pp. 184-192
• Jansen, S., Quigley, M., Reik, W., Jones, R., Analysis of polysulphate-binding domains in porcine proacrosin, a putative zona adhesion protein from mammalian spermatozoa (1995) Int. J. Dev. Biol., 39, pp. 501-510
• Jones, R., Identification of carbohydrate-binding proteins in mammalian spermatozoa (human, bull, boar, ram, stallion and hamster) using (125I)fucoidin and (125I)neoglycoproteins probes (1989) Human Reprod., 4, pp. 550-557
• Kennedy, W.P., Kaminski, J.M., Van der Ven, H.H., Jeyendran, R.S., Reid, D.S., Blackwell, J., Bielfeld, P., Zaneveld, L.J.D., A simple, clinical assay to evaluate the acrosin activity of human spermatozoa (1989) J. Androl., 10, pp. 221-231
• Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 27, pp. 680-685
• Leyton, L., De Ioannes, A., Croxatto, H.B., Graham, E.J., Elce, J.S., Two satisfactory methods for purification of human acrosin (1986) Biochem. Cell Biol., 64, pp. 1020-1024
• Meizel, S., Mukerji, S.K., Biochemical studies of proacrosin and acrosin from hamster cauda epididymal spermatozoa (1976) Biol. Reprod., 14, pp. 444-450
• Menkveld, R., Rhemrev, J.P.T., Franken, D.R., Vermeiden, J.P.W., Kruger, T.F., Acrosomal morphology as a novel criterion for male fertility diagnosis: Relation with acrosin activity, morphology (strict criteria), and fertilization in vitro (1996) Fertil. Steril., 65, pp. 637-644
• Moos, J., Peknicova, J., Tesarik, J., Relatioship between molecular conversions of acrosin and the progression of exocytosis in the calcium ionophore-induced acrosome reaction (1993) Biochim. Biophys. Acta, 1176, pp. 199-207
• Moos, J., Tesarik, J., Leca, G., Peknicova, J., Mechanism of maturation and nature of carbohydrate chains of boar sperm acrosin (1991) FEBS Lett., 294, pp. 27-30
• Moreno, R.D., Sepulveda, M.S., De Ioannes, A., Barros, C., The polysulphate binding domain of human proacrosin/acrosin is involved in both the enzyme activation and spermatozoa-zona pellucida interaction (1998) Zygote, 6, pp. 75-83
• Nuzzo, N.A., Anderson, R.A., Zaneveld, L.J.D., Proacrosin activation and acrosin release during the guinea pig acrosome reaction (1990) Mol. Reprod. Dev., 25, pp. 52-60
• Parrish, R.F., Straus, J.W., Polakoski, K.L., Dombrose, F.A., Phospholipid vesicle stimulation of proacrosin activation (1978) Proc. Natl. Acad. Sci. USA, 75, pp. 149-152
• Polakoski, K.L., Parrish, R.F., Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm (1977) J. Biol. Chem., 252, pp. 1888-1894
• Polakoski, K.L., Zahler, W.L., Paulson, J.D., Demonstration of proacrosin and quantitation of proacrosin in ejaculated human spermatozoa (1977) Fertil. Steril., 28, pp. 668-670
• Richardson, R.T., O'Rand, M.G., Site-directed mutagenesis of rabbit proacrosin. Identification of residues involved in zona pellucida binding (1996) J. Biol. Chem., 271, pp. 24069-24074
• Schleuning, W., Hell, R., Fritz, H., Multiple forms of Human acrosin: Isolation and properties (1976) Hoppe-Seyler's Z. Physiol. Chem., 357, pp. 855-865
• Schneider, T.D., Stephens, R.M., Sequence logos: A new way to display consensus sequences (1990) Nucleic Acids Res., 18, pp. 6097-6100
• Senn, A., Germond, M., De Grandi, P., Immunofluorescence study of actin, acrosin, dynein, tubulin, and hyaluronidase and their impact on in-vitro fertilization (1992) Human Reprod., 7, pp. 841-849
• Sharma, R., Hogg, J., Bromham, D.R., Is spermatozoan acrosin a predictor of fertilization and embryo quality in the human? (1993) Fertil. Steril., 60, pp. 881-887
• Shimizu, Y., Kodama, H., Fukuda, J., Tanaka, T., Evidence of proacrosin molecule abnormality as a possible cause of low acrosin activity and unexplained failure of fertilization in vitro (1997) J. Androl., 18, pp. 281-288
• Siegel, M.S., Polakoski, K.L., Evaluation of the human sperm proacrosin-acrosin system using gelatin-sodium dodecyl sulfate-polyacrylamide gel electrophoresis (1985) Biol. Reprod., 32, pp. 713-720
• Siegel, M.S., Bechtold, D.S., Kopta, C.I., Polakoski, K.L., The rapid purification and partial characterization of human sperm proacrosin using an automated fast protein liquid chromatography (FPLC) system (1986) Biochim. Biophys. Acta, 883, pp. 567-573
• Smith, R., Jenkins, A., Lourbakos, A., Thompson, P., Ramakrisnan, Tomlinson, J., Deshpande, U., Pike, R.N., Evidence for the activation of PAR-2 by the sperm protease, acrosin: Expression of the receptor on oocytes (2000) FEBS Lett., 484, pp. 285-290
• Srivastava, P.N., Ninjoor, V., Isolation of rabbit testicular cathepsin D and its role in the activation of proacrosin (1982) Biochem. Biophys. Res. Comm., 109, pp. 63-69
• Suarez, S.S., Wolf, D.P., Meizel, S., Induction of the acrosome reaction in human spermatozoa by a fraction of human follicular fluid (1986) Gamete Res., 14, pp. 107-121
• Takano, H., Yanagimachi, R., Urch, U.A., Evidence that acrosin activity is important for the development of fusibility of mammalian spermatozoa with the oolema; inhibitor studies using the golden hamster (1993) Zygote, 1, pp. 79-91
• Tesarik, J., Drahorad, J., Peknicová, J., Subcellular immunochemical localization of acrosin in human spermatozoa during the acrosome reaction and zona pellucida penetration (1988) Fertil. Steril., 50, pp. 133-141
• Tesarik, J., Drahorad, J., Testart, J., Mendoza, C., Acrosin activation follows its surface exposure and precedes membrane fusion in human sperm acrosome reaction (1990) Development, 110, pp. 391-400
• Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G., The Clustal_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools (1997) Nucleic Acids Res., 25, pp. 4876-4882
• Towbin, H., Staeheling, T., Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications (1979) Proc. Natl. Acad. Sci. USA, 76, pp. 4350-4354
• Tranter, R., Read, J.A., Jones, R., Brady, R.L., Effector sites in the three-dimensional structure of mammalian sperm β-acrosin (2000) Structure, 8, pp. 1179-1188
• Tummon, I.S., Yuzpe, A.A., Daniel, S.A.J., Deutsch, A., Total acrosin activity correlates with fertility potential after fertilization in vitro (1991) Fertil. Steril., 56, pp. 933-938
• Urch, U.A., Biochemistry and function of acrosin (1991) Elements of Mammalian Fertilization, pp. 233-248. , Wassarman, P (Ed.). CRC Press, Boca Raton, FL
• Urch, U.A., Patel, H., The interaction of boar sperm proacrosin with its natural substrate, the zona pellucida, and with polysulphated polysaccharides (1991) Development, 111, pp. 1165-1172
• Urch, U.A., Wardrip, N.J., Hedrick, J.L., Proteolysis of the zona pellucida by acrosin: The nature of the hydrolysis products (1985) J. Exp. Zool., 263, pp. 239-243
• Valdivia, M., Yunes, R., Melendez, J., De Ioannes, A.E., Leyton, L., Becker, M.I., Barros, C., Immunolocalization of proacrosin/acrosin in rabbit sperm during acrosome reaction and in spermatozoa recovered from the perivitelline space (1994) Mol. Reprod. Dev., 37, pp. 216-222
• Van der Ven, H.H., Kaminski, J., Bauer, L., Zaneveld, L.J., Inhibition of human sperm penetration into zona-free hamster oocytes by proteinase inhibitors (1985) Fertil. Steril., 43, pp. 609-616
• (1992) Laboratory Manual of Examination of Human Semen and Semen-Cervical Mucus Interaction, 3rd edn., pp. 46-50. , Cambridge University Press, Cambridge
• Working, P.K., Meizel, S., Correlation of increased intraacrosomal pH with the hamster sperm acrosome reaction (1983) J. Exp. Zool., 227, pp. 97-107
• Yamagata, K., Murayama, K., Okabe, M., Toshimori, K., Nakanishi, T., Kashiwabara, S., Baba, T., Acrosin accelerates the dispersal of sperm acrosomal proteins during acrosome reaction (1998) J. Biol. Chem., 273, pp. 10470-10474

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