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        The 3D structure and function of digestive cathepsin L-like proteinases of Tenebrio molitor larval midgut 

        Beton, Daniela; Guzzo, Cristiane R.; Ribeiro, Alberto F.; Farah, Chuck S.; Terra, Walter R. (PERGAMON-ELSEVIER SCIENCE LTDOXFORD, 2012)
        Cathepsin L-like proteinases (CAL) are major digestive proteinases in the beetle Tenebrio molitor. Procathepsin Ls 2 (pCAL2) and 3 (pCAL3) were expressed as recombinant proteins in Escherichia coil, purified and activated ...

        Digestive physiology and characterization of digestive cathepsin L-like proteinase from the sugarcane weevil Sphenophorus levis 

        SOARES-COSTA, Andrea; DIAS, Alcides B.; DELLAMANO, Marcia; PAULA, Fernando Fonseca Pereira de; CARMONA, Adriana K.; TERRA, Walter R.; HENRIQUE-SILVA, Flavio (PERGAMON-ELSEVIER SCIENCE LTD, 2011)
        Sugarcane is an important crop that has recently become subject to attacks from the weevil Sphenophorus levis, which is not efficiently controlled with chemical insecticides. This demands the development of new control ...

        Cathepsin X binds to cell surface heparan sulfate proteoglycans 

        Nascimento, F. D.; Rizzi, CCA; Nantes, I. L.; Stefe, L.; Turk, B.; Carmona, A. K.; Nader, H. B.; Juliano, L.; Tersariol, ILS (Elsevier B.V., 2005-04-15)
        Glycosaminoglycans have been shown to be important regulators of activity of several papain-like cathepsins. Binding of glycosaminoglycans to cathepsins thus directly affects catalytic activity, stability or the rate of ...

        Characterization of two cysteine proteinases secreted by Fasciola hepatica and demonstration of their kininogenase activity 

        Cordova, M.; Jara, J.; Del Nery, E.; Hirata, I. Y.; Araujo, M. S.; Carmona, A. K.; Juliano, M. A.; Juliano, L. (Elsevier B.V., 2001-09-03)
        We have isolated and purified two cysteine proteinases of molecular weights 25 and 26 kDa, secreted by Fasciola hepatica adult worm. Their 15 N-terminal residues were found to be identical to those of earlier described ...

        Meloidogyne incognita: molecular cloning and characterization of a cDNA encoding a cathepsin D-like aspartic proteinase. 

        FRAGOSO, R. da R.; LOURENÇO, I. T.; BATISTA, J. A. N.; OLIVEIRA NETO, O. B.; SILVA, M. C. M.; ROCHA, T. L.; COUTINHO, M. V.; GROSSI DE SÁ, M. F. (2009)

        New, sensitive fluorogenic substrates for human cathepsin G based on the sequence of serpin-reactive site loops 

        Rehault, S.; Brillard-Bourdet, M.; Juliano, Maria Aparecida [UNIFESP]; Juliano, Luiz [UNIFESP]; Gauthier, F.; Moreau, T. (Amer Soc Biochemistry Molecular Biology Inc, 1999-05-14)
        Cathepsin G has both trypsin- and chymotrypsin-like activity, but studies on its enzymatic properties have been limited by a lack of sensitive synthetic substrates. Cathepsin G activity is physiologically controlled by the ...

        Prey digestion in the midgut of the predatory bug Podisus nigrispinus (Hemiptera: Pentatomidae) 

        Fialho, Maria C. Q.; Moreira, Nathalia R.; Zanuncio, Jose C.; Ribeiro, Alberto Augusto Gonçalves de Freitas Castro; Terra, Walter Ribeiro; Serrao, Jose E. (PERGAMON-ELSEVIER SCIENCE LTDOXFORD, 2012)
        Pre-oral digestion is described as the liquefaction of the solid tissues of the prey by secretions of the predator. It is uncertain if pre-oral digestion means pre-oral dispersion of food or true digestion in the sense of ...

        Purificação parcial e caracterização das proteinases digestivas de Dysdercus peruvianus (Hemiptera - Pyrrhocoridae) : papel na hidrólise da urease de Canavalia ensiformis 

        Salvadori, Juliana de Marco (2007)

        Characterization of proteinases from the midgut of Rhipicephalus (Boophilus) microplus involved in the generation of antimicrobial peptides 

        Cruz, Carlos E; Fogaça, Andréa C; Nakayasu, Ernesto S; Angeli, Claudia B; Belmonte, Rodrigo; Almeida, Igor C; Miranda, Antonio; Miranda, Maria Terêsa M; Tanaka, Aparecida S; Braz, Gloria R; Craik, Charles S; Schneider, Eric; Caffrey, Conor R; Daffre, Sirlei (BIOMED CENTRAL LTD, 2010-07-27)
        Background: Hemoglobin is a rich source of biologically active peptides, some of which are potent antimicrobials (hemocidins). A few hemocidins have been purified from the midgut contents of ticks. Nonetheless, how ...

        Characterization of proteinases from the midgut of Rhipicephalus (Boophilus) microplus involved in the generation of antimicrobial peptides 

        Cruz, Carlos E; Fogaça, Andréa C; Nakayasu, Ernesto S; Angeli, Claudia B; Belmonte, Rodrigo; Almeida, Igor C; Miranda, Antônio; Miranda, Maria T M; Tanaka, Aparecida S; Braz, Glória R; Craik, Charles S; Schneider, Eric; Caffrey, Conor R; Daffre, Sirlei (BioMed Central, 2010-07-27)
        Abstract Background Hemoglobin is a rich source of biologically active peptides, some of which are potent antimicrobials (hemocidins). A few hemocidins have been purified ...
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        Red de Repositorios Latinoamericanos
        + of 4.000.000
        Available publications
        163 Participating institutions
        Dirección de Servicios de Información y Bibliotecas (SISIB)
        Universidad de Chile
        Membership Login
        Featured collections
        • Latin American Theses
        • Argentinean Theses
        • Chilean Theses
        • Peruvian Theses
        Latest collections added
        • Argentina
        • Brazil
        • Colombia
        • México
        Dirección de Servicios de Información y Bibliotecas (SISIB)
        Universidad de Chile
        Red de Repositorios Latinoamericanos | 2006-2018