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Referencias:

• Dunn, B.M., Structure and mechanism of the pepsin-like family of aspartic peptidases (2002) Chem. Rev., 102 (12), pp. 4431-4458
• Devaraj, K.B., Gowda, L.R., Prakash, V., An unusual thermostable aspartic protease from the latex of Ficus racemosa (2008) Phytochemistry, 69 (3), pp. 647-655
• Rawlings, N.D., Barrett, A.J., Bateman, A., MEROPS: The database of proteolytic enzymes, their substrates and inhibitors (2012) Nucleic Acids Res., 40 (D1), pp. D343-D350
• Lufrano, D., Faro, R., Castanheira, P., Parisi, G., Verissimo, P., Vairo-Cavalli, S., Simöes, I., Faro, C., Molecular cloning and characterization of procirsin, an active aspartic protease precursor from Cirsium vulgare (Asteraceae) (2012) Phytochemistry, 81, pp. 7-18
• Rawlings, N.D., Morton, F.R., Kok, C.Y., Kong, J., Barrett, A.J., MEROPS: The peptidase database (2008) Nucleic Acids Res., 36, pp. D320-D325
• Park, H., Yamanaka, N., Mikkonen, A., Kusakabe, I., Kobayashi, H., Purification and characterization of aspartic proteinase from sunflower seeds (2000) Biosci. Biotechnol. Biochem., 64, pp. 931-939
• Cruz De Carvalho, M.H., D'arcy-Lameta, A., Roy-Macauley, H., Gareil, M., El Maarouf, H., Pham-Thi, A.T., Zuily-Fodil, Y., Aspartic protease in leaves of common bean (Phaseolus vulgaris L.) and cowpea (Vigna unguiculata L. Walp): Enzymatic activity, gene expression and relation to drought susceptibility (2001) FEBS Lett., 492 (3), pp. 242-246
• Guevara, M.G., Oliva, C.R., Machinandiarena, M., Daleo, G.R.E., Purification and properties of an aspartic protease from potato tuber that is inhibited by a basic chitinase (1999) Physiol. Plant., 106, pp. 164-169
• Cordeiro, M.C., Pais, M.S., Brodelius, P.E., Tissue-specific expression of multiple forms of cyprosin (aspartic proteinase) in flowers of Cynara cardunculus (1994) Physiol. Plant., 92, pp. 645-653
• Wang, L., Wang, M., Li, Q., Cai, T., Jiang, W., Partial properties of an aspartic protease in bitter gourd (Momordica charantia L.) fruit and its activation by heating (2008) Food Chem., 108, pp. 496-502
• Brodelius, M., Hiraiwa, M., Marttila, S., Karadaghi, S.A., Picaud, S., Brodelius, P.E., Immunolocalization of the saposin-like insert of plant aspartic proteinases exhibiting saposin C activity. Expression in young flower tissues and in barley seeds (2005) Physiol. Plant., 125, pp. 405-418
• Bi, X., Khush, G.S., Bennett, J., The rice nucellin gene ortholog OsAsp1 encodes and active aspartic peptidase without a plantspecific insert and is strongly expressed in RT early embryo (2005) Plant Cell Physiol., 46, pp. 87-98
• Radlowski, M., Kalinowski, A., Adamczyk, J., Proteolytic activity in the maize pollen wall (1996) Physiol. Plant., 98, pp. 172-178
• Tamura, T., Terauchi, K., Kiyosaki, T., Asakura, T., Funaki, J., Matsumoto, L., Misaka, T., Abe, K., Differential expression of wheat aspartic proteinases, WAP1 and WAP2, in germinating and maturing seeds (2007) J. Plant Physiol., 164, pp. 470-477
• Schaller, A., Ryan, C.A., Molecular cloning of a tomato leaf cDNA encoding an aspartic peptidase, a systemic wound response protein (1996) Plant Mol. Biol., 31, pp. 1073-1077
• Guilloteau, M., Laloi, M., Michaux, S., Bucheli, P., McCarthy, J., Identification and characterisation of the major aspartic proteinase activity in Theobroma cacao seeds (2005) J. Sci. Food Agric., 85, pp. 549-562
• Simöes, I., Faro, R., Bur, D., Faro, C., Characterization of recombinant CDR1, an Arabidopsis aspartic proteinase involved in disease resistance (2007) J. Biol. Chem., 282, pp. 31358-31365
• Vieira, M., Pissarr, J., Veríssimo, P., Castanheira, P., Costa, Y., Pires, E., Faro, C., Molecular cloning and characterization of cDNA encoding cardosin B, an aspartic proteinase accumulating extracel-lularly in the transmitting tissue of Cynara cardunculus L (2001) Plant Mol. Biol., 45, pp. 529-539
• Guevara, M.G., Almeida, C., Mendieta, J.R., Faro, C.J., Veríssimo, P., Vieyras Pires, E., Daleo, G.R., Molecular cloning of a potato leaf cDNA encoding an aspartic protease (StAsp) and its expression after P. Infestans infection (2005) Plant Physiol. Biochem., 43, pp. 882-889
• Huang, G.J., Huang, S.S., Chen, H.J., Chang, Y., Chang, S.J., Chang, H.Y., Hsieh, P.C., Lin, Y.H., Cloning and expression of aspartic proteinase cDNA from sweet potato storage roots (2009) Bot. Stud., 50, pp. 149-158
• Simöes, I., Faro, C., Structure and function of plant aspartic proteinases (2004) Eur. J. Biochem., 271, pp. 2067-2075
• Mutlu, A., Gal, S., Plant aspartic proteinases: Enzymes on the way to a function (1999) Physiol. Plant., 105, pp. 569-576
• Masson, O., Bach, A.S., Derocq, D., Prébois, C., Laurent-Matha, V., Pattingre, S., Liaudet-Coopman, E., Pathophysiological functions of cathepsin D: Targeting its catalytic activity versus its protein binding activity? (2010) Biochimie, 92 (11), pp. 1635-1643
• Mendieta, J.R., Pagano, M., Muñoz, R.R., Daleo, G.R., Guevara, M.G., Antimicrobial activity of potato aspartic peptidases (StAPs) involves membrane permeabilization (2006) Microbiology, 152, pp. 2039-2047
• Rocha, G., Fernández, G., Parisi, M., Estudios de caracterización cinética y fisicoquímica de una proteinasa aspártica aislada de frutos maduros de Salpichroa origanifolia (2010) Información Tecnológica, 21 (2), pp. 21-28
• Rocha, G., Kise, F., Rosso, A., Parisi, M., Péptidos con actividad antimicrobiana obtenidos por hidrólisis enzimática de proteínas lácteas con extractos de frutos de Salpichroa origanifolia (2013) Información Tecnológica, 24 (2), pp. 23-30
• Mongelli, E., Pampuro, S., Coussio, J., Salomón, H., Ciccia, G., Cytotoxic and DNA interaction activities of extracts from medicinal plants used in Argentina (2000) J. Ethnopharmacol., 71, pp. 145-151
• Boeris, M.A., Toso, R.E., Skliar, M., Actividad antiinflamatoria de Salpichroa origanifolia (2004) Acta Farm. Bonaerense, 23 (2), pp. 138-141
• Mareggiani, G., Picollo, M.I., Zerba, E., Burton, G., Tettamanzi, M.C., Benedetti-Doctorovich, M.O.V., Veleiro, A.S., Antifeedant activity of withanolides from Salpichroa origanifolia on Musca domestica (2000) J. Nat. Prod., 63, pp. 1113-1116
• Bado, S., Mareggiani, G., Amiano, N., Burton, G., Veleiro, A.S., Lethal and sublethal effects of withanolides from Salpichroa origanifolia and analogues on (2004) Ceratitis Capitata, J. Agric. Food Chem., 52, pp. 2875-2878
• Anson, L., The estimation of pepsin, trypsin, papain and cathepsin with haemoglobin (1938) J. Gen. Physiol., 22, pp. 79-89
• Parisi, M.G., Moreno, S., Fernández, G., Isolation and characterization of a dual function protein from Allium sativum bulbs which exhibits proteolytic and hemagglutinating activities (2008) Plant Physiol. Biochem., 46, pp. 403-413
• Dunn, B.M., Jiménez, M., Parten, B.F., Valler, M.J., Rolph, C.E., Kay, J., A systematic series of synthetic chromophoric substrates for aspartic proteinases (1986) Biochem. J., 237, pp. 899-906
• Bradford, M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of Protein-Dye Binding (1976) Anal. Biochem., 72, pp. 248-254
• Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
• Blum, H., Beier, H., Gross, H.J., Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels (1987) Electrophoresis, 8, pp. 93-99
• Kleiner, D.E., Stetler-Stevenson, W.G., Quantitative zymography: Detection of picogram quantities of gelatinases (1994) Anal. Biochem., 218, pp. 325-329
• Barrett, A.J., Rawlings, N.D., Woessner, J.F., (1998) Handbook of Proteolytic Enzymes., , Academic Press, New York
• Salvesen, G., Nagase, H., (1989) Inhibition of Proteolytic Enzymes, Proteolytic Enzymes: A Practical Approach, p. 83. , R.M. Beynon, J.S. Bond, eds.; IRL Press: Oxford, UK
• Chazarra, S., Sidrach, L., López-Molina, D., Rodríguez-López, J.N., Characterization of the milk-clotting properties of extracts from artichoke (Cynara scolymus, L.) flowers (2007) Int. Dairy J., 17 (12), pp. 1393-1400
• Barrett, A.J., Kirschke, H., Cathepsin B Cathepsin H Cathepsin L (1981) Method Enzymol., 80, pp. 535-561
• Helsens, K., Martens, L., Vandekerckhove, J., Gevaert, K., MascotDatfile: An open-source library to fully parse and analyse MASCOT MS/MS search results (2007) Proteomics, 7, pp. 364-366
• Mancone, C., Amicone, L., Fimia, G.M., Bravo, E., Piacentini, M., Tripodi, M., Alonzi, T., Proteomic analysis of human very lowdensity lipoprotein by two-dimensional gel electrophoresis and MALDI-TOF/TOF (2007) Proteomics, 7, pp. 143-154
• Tamura, K., Peterson, D., Peterson, N., Stecher, G., Nei, M., Kumar, S., Mega5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods (2011) Mol. Biol. Evol., 28, pp. 2731-2739
• Kervinen, J., (2013) Phytepsin. Handbook of Proteolytic Enzymes, 1, pp. 118-124. , Neil D. Rawlings and Guy S. Salvesen, eds.; Academic Press: Oxford
• Guevara, M.G., Daleo, G.R., Oliva, C.R., Purification and characterisation of an aspartic protease from potato leaves (2001) Physiol. Plant., 112, pp. 321-326
• Sidrach, L., Garcia-Cánovas, F., Tudela, J., Rodriguez-López, J.N., Purification of cynarases from artichoke (Cynara scolymus L.): Enzymatic properties of cynarase A (2005) Phytochemistry, 66, pp. 41-49
• Raposo, S., Domingos, A., Purification and characterization of milk-clotting aspartic proteinases from Centaurea calcitrapa cell suspension cultures (2008) Process Biochem., 43, pp. 139-144
• Vairo-Cavalli, S., Lufrano, D., Colombo, M.L., Priolo, N., Properties and application of phytepsins from thistle flowers (2013) Phytochemistry, 92, pp. 16-32
• Fujinaga, M., Chernaia, M.M., Tarasova, N.I., Mosimann, S.C., James, M.N.G., Crystal-structure of human pepsin and its complex with pepstatin (1995) Protein Sci., 4, pp. 960-972
• Rich, D.H., Sun, E.T.O., Mechanism of inhibition of pepsin by pepstatin effect of inhibitor structure on dissociation constant and time-dependent inhibition (1980) Biochem. Pharmacol., 29, pp. 2205-2212
• Carles, C., Ribadeau-Dumas, B., Kinetics of the action of chymosin (rennin) on a peptide bond of bovine αs1-casein, comparison of the behavior of this substrate with β-casein and κ-casein (1985) FEBS Lett., 185, pp. 282-286
• Ben-Khaled, H.B., Ghorbel-Bellaaj, O., Hmidet, N., Jellouli, K., El-Hadj Ali, N., Ghorbel, S., Nasri, M., A novel aspartic protease from the viscera of Sardinelle (Sardinella aurita) Purification and characterization (2011) Food Chem., 128, pp. 847-853
• Kumar, A., Khan, F., Rao, M., Biochemical Characterization of a Novel Aspartic Peptidase from Plutella xylostella, Diamondback moth (lepidoptera: Plutellidae) midgut: Inactivation by an aspartic peptidase inhibitor (2012) Int. J. Innov. Biol .Res., 1 (1), pp. 9-19
• Verissimo, P., Esteves, C., Faro, C., Pires, E., The vegetable rennet of Cynara cardunculus L. Contains two proteinases with chymosin and pepsin-like specificities (1995) Biotechnol. Lett., 17, pp. 621-626
• Sarmento, A.C., Lopes, H., Oliveira, C., Vitorino, R., Samyn, B., Sergeant, K., Debyser, G., Barros, M.T., Multiplicity of aspartic proteinases from Cynara cardunculus L (2009) Planta, 230, pp. 429-439
• Kervinen, J., Sarkkinen, P., Kalkkinen, N., Mikola, L., Saarma, M., Hydrolytic specificity of the barley grain aspartic proteinase (1993) Phytochemistry, 32, pp. 799-803
• Guevara, M.G., Veríssimo, P., Pires, E., Faro, C., Daleo, G.R., Potato aspartic proteases: Induction, antimicrobial activity and substrate specificity (2004) J. Plant Pathol., 86, pp. 233-238
• Foltmann, B., On the amino acid composition of prorennin, rennin and of peptides liberated during the activation of prorennin (1964) C R Travaux Lab Carlsberg, 34, pp. 275-286
• Sanger, F., Tuppy, H., The amino-acid sequence in the phenylalanyl chain of insulin: II the investigation of peptides from enzymatic hydrolysate (1981) Biochem. J., 49, pp. 481-490
• Kervinen, J., Törmäkangas, K., Runeberg-Roos, P., Guruprasad, K., Blundell, T., Teeri, T.H., Structure and possible function of aspartic proteinases in barley and other plants (1995) Adv. Exp. Med. Biol., 362, pp. 241-254
• Mazorra-Manzano, M., Yada, R., Expression and characterization of the recombinant aspartic proteinase A1 from (2008) Arabidopsis Thaliana. Phytochemistry, 69, pp. 2439-2448
• Muñoz, F.F., Mendieta, J.R., Pagano, M.R., Paggi, R.A., Daleo, G.R., Guevara, M.G., The swaposin-like domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens (2010) Peptides, 31, pp. 777-785
• Bryksa, B.C., Bhaumik, P., Magracheva, E., De Mour, D.C., Kurylowicz, M., Zdanov, A., Dutcher, J.R., Yada, R.Y., Structure and mechanism of the saposin-like domain of a plant aspartic protease (2011) J. Biol. Chem., 286, pp. 28265-28275
• Castanheira, P., Samyn, B., Sergeant, K., Clemente, J.C., Dunn, B.M., Pires, E., Van Beeumen, J., Faro, C., Activation proteolytic processing, and peptide specificity of recombinant cardosin A (2005) J. Biol. Chem., 280, pp. 13047-13054
• Payie, K., Tanaka, T., Gal, S., Yada, R., Construction expression and characterization of a chimaeric mammalian-plant aspartic proteinase (2003) Biochem. J., 372, pp. 671-678
• Yamauchi, Y., Sugimoto, T., Sueyoshi, K., Oji, Y., Emergence of proteases in germinating cucumber cotyledons and their roles in the two-step degradation of storage protein (1996) Plant Cell Physiol., 37, pp. 279-284
• Timotijevic, G.S., Milisavljevic, M.D., Radovic, S.R., Konstantinovic, M.M., Maksimovic, V.R., Seed-specific aspartic proteinase feap12 from buckwheat (Fagopyrum esculentum Moench) (2010) Arch. Biol. Sci., 62 (1), pp. 143-151
• An, C., Takekawa, S., Okazawa, A., Fukusaki, E., Kobayashi, A., Degradation of a peptide in pitcher fluid of the carnivorous plant nepenthes alata blanco (2002) Planta, 215, pp. 472-477
• Terauchi, K., Asakura, T., Nishizawa, N.K., Matsumoto, I., Abe, K., Characterization of the genes for two soybean aspartic proteinases and analysis of their different tissue-dependent expression (2004) Planta, 218, pp. 947-957
• Guo, R., Xu, X., Carole, B., Li, X., Gao, M., Zheng, Y., Wang, X., Genome-wide identification, evolutionary and expression analysis of the aspartic protease gene superfamily in grape (2013) BMC Genomics, 14, p. 554
• Thompson, J.D., Higgins, D.G., Gibson, T.J., CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice (1994) Nucleic Acids Res., 22 (22), pp. 4673-4680
• Nicholas, K.B., Nicholas, H.B., Jr., Deerfield, D.W., GeneDoc: Analysis and visualization of genetic variation (1997) Embnew.news, 4, p. 14
• Saitou, N., Nei, M., The neighbor-joining method: A new method for reconstructing phylogenetic trees (1987) Mol. Biol. Evol., 4, pp. 406-425
• Felsenstein, J., Confidence limits on phylogenies: An approach using the bootstrap (1985) Evolution, 39 (4), pp. 783-791

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