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Auteur : Grafiati
Publié le 11 mars 2023

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1

Catanzano, Francesca, et G. Graziano. « Domains in bovine seminal ribonuclease ». Journal of Thermal Analysis and Calorimetry 91, no 1 (1 octobre 2007) : 61–66. http://dx.doi.org/10.1007/s10973-007-8537-2.

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2

Poučková, P., J. Souček, J. Matoušek, M. Zadinová, D. Hloušková, J. Polívková et L. Navrátil. « Antitumor action of bovine seminal ribonuclease ». Folia Microbiologica 43, no 5 (octobre 1998) : 511–12. http://dx.doi.org/10.1007/bf02820807.

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3

Slav�k, Tom�?, Josef Matou?ek, Josef Fulka et Ronald T. Raines. « Effect of bovine seminal ribonuclease and bovine pancreatic ribonuclease A on bovine oocyte maturation ». Journal of Experimental Zoology 287, no 5 (2000) : 394–99. http://dx.doi.org/10.1002/1097-010x(20001001)287:5<394 ::aid-jez7>3.0.co;2-e.

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4

Mancheno, J. M., M. Gasset, M. Onaderra, J. G. Gavilanes et G. Dalessio. « Bovine Seminal Ribonuclease Destabilizes Negatively Charged Membranes ». Biochemical and Biophysical Research Communications 199, no 1 (février 1994) : 119–24. http://dx.doi.org/10.1006/bbrc.1994.1202.

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5

Kim, J. S., et R. T. Raines. « Bovine seminal ribonuclease produced from a synthetic gene ». Journal of Biological Chemistry 268, no 23 (août 1993) : 17392–96. http://dx.doi.org/10.1016/s0021-9258(19)85347-4.

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6

Lee, J. Eugene, et Ronald T. Raines. « Cytotoxicity of Bovine Seminal Ribonuclease : Monomer versus Dimer† ». Biochemistry 44, no 48 (décembre 2005) : 15760–67. http://dx.doi.org/10.1021/bi051668z.

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7

Mazzarella, L., S. Capasso, D. Demasi, G. Di Lorenzo, C. A. Mattia et A. Zagari. « Bovine seminal ribonuclease : structure at 1.9 Å resolution ». Acta Crystallographica Section D Biological Crystallography 49, no 4 (1 juillet 1993) : 389–402. http://dx.doi.org/10.1107/s0907444993003403.

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8

Denigris, M., N. Russo, R. Piccoli, G. Dalessio et A. Didonato. « Expression of Bovine Seminal Ribonuclease in Escherichia coli ». Biochemical and Biophysical Research Communications 193, no 1 (mai 1993) : 155–60. http://dx.doi.org/10.1006/bbrc.1993.1603.

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9

Spadaccini, Roberta, Carmine Ercole, Giuseppe Graziano, Rainer Wechselberger, Rolf Boelens et Delia Picone. « Mechanism of 3D domain swapping in bovine seminal ribonuclease ». FEBS Journal 281, no 3 (13 décembre 2013) : 842–50. http://dx.doi.org/10.1111/febs.12651.

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10

Kim, Jin-Soo, et Ronald T. Raines. « A Misfolded but Active Dimer of Bovine Seminal Ribonuclease ». European Journal of Biochemistry 224, no 1 (août 1994) : 109–14. http://dx.doi.org/10.1111/j.1432-1033.1994.tb20001.x.

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11

Chakrabarti, Kalyan S, B. S. Sanjeev et Saraswathi Vishveshwara. « Stability and Dynamics of Domain-Swapped Bovine-Seminal Ribonuclease ». Chemistry & ; Biodiversity 1, no 5 (mai 2004) : 802–18. http://dx.doi.org/10.1002/cbdv.200490062.

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12

Catanzano, Francesca, Giuseppe Graziano, Valeria Cafaro, Giuseppe D'Alessio, Alberto Di Donato et Guido Barone. « From Ribonuclease A toward Bovine Seminal Ribonuclease : A Step by Step Thermodynamic Analysis† ». Biochemistry 36, no 47 (novembre 1997) : 14403–8. http://dx.doi.org/10.1021/bi971358j.

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13

Matousek, Josef, Josef Soucek, Jan Riha, Todd R. Zankel et Steven A. Benner. « Immunosuppressive activity of angiogenin in comparison with bovine seminal ribonuclease and pancreatic ribonuclease ». Comparative Biochemistry and Physiology Part B : Biochemistry and Molecular Biology 112, no 2 (octobre 1995) : 235–41. http://dx.doi.org/10.1016/0305-0491(95)00075-5.

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14

Piccoli, R., A. Di Donato et G. D'Alessio. « Co-operativity in seminal ribonuclease function. Kinetic studies ». Biochemical Journal 253, no 2 (15 juillet 1988) : 329–36. http://dx.doi.org/10.1042/bj2530329.

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Kinetic studies with substrates of the hydrolytic rate-limiting reaction step revealed that the non-hyperbolic kinetics of bovine seminal RNAse may not be ascribed to microheterogeneity of the enzyme or to hysteretic effects. The substrate saturation curves with intermediate plateau and the activating and inhibiting effects of the reaction product, respectively at low and high concentrations, are explained in terms of mixed co-operativity, with binding at subsites that is a prerequisite for full activity of the enzyme. A model is proposed that is supported also by the results of binding studies.
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15

Di Donato, A., R. Piccoli et G. D'Alessio. « Co-operativity in seminal ribonuclease function : binding studies ». Biochemical Journal 241, no 2 (15 janvier 1987) : 435–40. http://dx.doi.org/10.1042/bj2410435.

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Binding of nucleotides to bovine seminal RNAase was studied by differential spectrophotometry and equilibrium dialysis. Cytidine 3′-phosphate, the reaction product of the hydrolytic, rate-limiting step of the reaction, was found to be capable, in contrast to related nucleotides, of discriminating between the two structurally identical active sites of the enzyme. Negative co-operativity, with a ‘half-of-sites’ reactivity, was found at lower concentrations of ligand, whereas at higher concentrations positive co-operativity was detected. These findings exclude that the non-hyperbolic kinetics previously reported for the hydrolytic step of the reaction are due to hysteretic effect. A model of mixed-type co-operativity is proposed for interpreting the binding data.
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16

Leonidas, Demetres D., Kyriaki Dossi, Joe Hayes, Vicky Tsirkone, Josef Matoušek, Pavla Poučková, Josef Souček, Marie Zadinova et Spyros E. Zographos. « The binding of pyrimidinyl phosphonucleotide inhibitors to bovine seminal ribonuclease ». Acta Crystallographica Section A Foundations of Crystallography 65, a1 (16 août 2009) : s147. http://dx.doi.org/10.1107/s0108767309097062.

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17

Giancola, Concetta, Pompea Del Vecchio, Claudia De Lorenzo, Roberto Barone, Renata Piccoli, Giuseppe D'Alessio et Guido Barone. « Thermodynamic Stability of the Two Isoforms of Bovine Seminal Ribonuclease† ». Biochemistry 39, no 27 (juillet 2000) : 7964–72. http://dx.doi.org/10.1021/bi992953j.

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18

Kim, Jin-Soo, Josef Sou&;ek, Josef Matou&;ek et Ronald T. Raines. « Structural Basis for the Biological Activities of Bovine Seminal Ribonuclease ». Journal of Biological Chemistry 270, no 18 (5 mai 1995) : 10525–30. http://dx.doi.org/10.1074/jbc.270.18.10525.

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SUZUKI, Hisanori, Augusto PARENTE, Benedetta FARINA, Luigi GRECO, Renato LA MONTAGNA et Enzo LEONE. « Complete Amino-Acid Sequence of Bovine Seminal Ribonuclease, a Dimeric Protein from Seminal Plasma ». Biological Chemistry Hoppe-Seyler 368, no 2 (janvier 1987) : 1305–12. http://dx.doi.org/10.1515/bchm3.1987.368.2.1305.

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20

Murthy, B. S., et R. Sirdeshmukh. « Sensitivity of monomeric and dimeric forms of bovine seminal ribonuclease to human placental ribonuclease inhibitor ». Biochemical Journal 281, no 2 (15 janvier 1992) : 343–48. http://dx.doi.org/10.1042/bj2810343.

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We have studied the inhibition of bovine pancreatic RNAase (RNAase A) and bovine seminal RNAase in its native dimeric form (RNAase BS-1) and in monomeric carboxymethylated form (MCM RNAase BS-1) by human placental RNAase inhibitor (RNAase inhibitor) in order to understand the effect of enzyme structure on its response to the inhibitor. Study of the inhibition as a function of inhibitor concentration revealed that RNAase A and MCM RNAase BS-1 were inhibited fully and the inhibitor-sensitivities of the two were comparable. But under identical inhibitor concentrations RNAase BS-1 was found to be virtually insensitive to the inhibitor; at higher (3-10-fold) inhibitor concentrations marginal inhibition of the native enzyme could be observed. When RNAase BS-1 was pretreated with 5 mM-dithiothreitol (DTT) and assayed, it exhibited greater inhibitor-sensitivity, presumably as a result of its partial monomerization on exposure to DTT. This DTT-mediated change in the response of RNAase BS-1 to the inhibitor did not, however, seem to occur either in the assay conditions (which included DTT) or even when the enzyme was pretreated with DTT in the presence of the substrate, suggesting an effect of the substrate on the enzyme behaviour towards the inhibitor. Independently, gel-filtration runs revealed that, although DTT treatment caused monomerization of RNase BS-1, this change did not take place when DTT treatment was carried out in the presence of the substrate. From our observations, we infer that differential inhibitor-sensitivity of the dimeric and monomeric forms of RNAase BS-1, the relative contents of the two forms and the influence of the substrate on them may be important determinants of the net enzyme activity in the presence of the inhibitor.
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21

BRACALE, Aurora, Daniela SPALLETTI-CERNIA, Mariarosaria MASTRONICOLA, Francesco CASTALDI, Roberta MANNUCCI, Lucio NITSCH et Giuseppe D’ALESSIO. « Essential stations in the intracellular pathway of cytotoxic bovine seminal ribonuclease ». Biochemical Journal 362, no 3 (15 mars 2002) : 553. http://dx.doi.org/10.1042/0264-6021:3620553.

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BRACALE, Aurora, Daniela SPALLETTI-CERNIA, Mariarosaria MASTRONICOLA, Francesco CASTALDI, Roberta MANNUCCI, Lucio NITSCH et Giuseppe D'ALESSIO. « Essential stations in the intracellular pathway of cytotoxic bovine seminal ribonuclease ». Biochemical Journal 362, no 3 (8 mars 2002) : 553–60. http://dx.doi.org/10.1042/bj3620553.

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Bovine seminal RNase (BS-RNase) is a dimeric RNase selectively cytotoxic for malignant cells. No information is available on its pathway from the extracellular matrix through the cytosol, where it degrades rRNA. An investigation of this pathway is reported here, carried out by immunofluorescence studies, by assessing the effects on BS-RNase cytotoxicity of drugs that affect specific intracellular compartments and by assaying the behaviour of a protein variant, BS-RNase-KDEL (BS-RNase in which a Lys-Asp-Glu-Leu peptide segment is inserted at the C-terminal ends of the subunit chains), endowed with a consensus sequence that directs proteins to the endoplasmic reticulum. BS-RNase was found to bind both normal and malignant cells and to be internalized by both cell types in endosome vesicles. Non-cytotoxic RNases, such as RNase A and a monomeric derivative of BS-RNase, did not bind to the cell surface and were not internalized. However, an engineered, dimeric and cytotoxic variant of RNase A bound effectively and permeated cells. The results of immunofluorescence studies, the effects of nigericin, monensin and brefeldin A on the cytotoxic action of seminal RNase, and the behaviour of the BS-RNase-KDEL variant, led to the conclusion that the pathway of BS-RNase in malignant cells from the extracellular matrix to the cytosol has two essential intracellular stations: endosomes and the trans-Golgi network. In normal cells, however, the protein does not progress from the endosomal compartment to the Golgi complex.
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23

Preuβ, Klaus-Dieter, Sabine Wagner, Johannes Freudenstein et Karl Heinz Scheit. « Cloning of cDNA encoding the complete precursor for bovine seminal ribonuclease ». Nucleic Acids Research 18, no 4 (1990) : 1057. http://dx.doi.org/10.1093/nar/18.4.1057.

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24

Berisio, R., F. Sica, C. De Lorenzo, A. Di Fiore, R. Piccoli, A. Zagari et L. Mazzarella. « Crystal structure of the dimeric unswapped form of bovine seminal ribonuclease ». FEBS Letters 554, no 1-2 (8 octobre 2003) : 105–10. http://dx.doi.org/10.1016/s0014-5793(03)01114-1.

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PALMIERIE, Marta, Antonella CARSANA, Adriana FURIA et Massimo LIBONATI. « Sequence analysis of a cloned cDNA coding for bovine seminal ribonuclease ». European Journal of Biochemistry 152, no 2 (octobre 1985) : 275–77. http://dx.doi.org/10.1111/j.1432-1033.1985.tb09194.x.

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DONADIO, Stefano, Maurizio TAMBURRINI, Alberto DI DONATO, Renata PICCOLI et Giuseppe D'ALESSIO. « Site-directed alkylation and site-site interactions in bovine seminal ribonuclease ». European Journal of Biochemistry 157, no 3 (juin 1986) : 475–80. http://dx.doi.org/10.1111/j.1432-1033.1986.tb09691.x.

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Souček, Josef, Iuri Marinov, Jiří Beneš, Ivan Hilgert, Josef Matoušek et Ronald T. Raines. « Immunosuppressive Activity of Bovine Seminal Ribonuclease and its Mode of Action. » Immunobiology 195, no 3 (août 1996) : 271–85. http://dx.doi.org/10.1016/s0171-2985(96)80045-3.

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28

Matoušek, J., V. Hruban, J. Hradecky, A. Hrubá et J. Soućek. « Effect of bovine seminal ribonuclease (BS-RNase) on pigs bone marrow cells ». Archives Animal Breeding 44, no 1 (10 octobre 2001) : 53–64. http://dx.doi.org/10.5194/aab-44-53-2001.

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Abstract. The effect of bovine seminal ribonuclease (BS RNase) on bone marrow cells in miniature pigs was studied. BS RNase at the concentration 20 and l00 ug/ml preincubated 1 h with bone marrow cells from normal miniature pigs did not influence the formation of CFU-GM and BFU-E colonies cultivated in methylcellulose medium. The bone marrow cells kept in 4 °C survived better in the presence of BS RNase than control cells cocultivated with bovine serum albumin (BSA). There was proved that pig bone marrow cells are able to bind the BS RNase on their surface without any morphological damage. For the experimental bone marrow transplantation in miniature pigs the whole body irradiation of 8G with a cobalt source was used. Two recipients from seven accepted semi-incompatible bone marrow cells preincubated 2 h with BS RNase (10 mg/5 x l08 cells). No recipient from eight transplanted control animals accepted semi-incompatible bone marrow cells preincubated with BSA.
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Ercole, Carmine, Roberta Spadaccini, Caterina Alfano, Teodorico Tancredi et Delia Picone. « A New Mutant of Bovine Seminal Ribonuclease with a Reversed Swapping Propensity† ». Biochemistry 46, no 8 (février 2007) : 2227–32. http://dx.doi.org/10.1021/bi0613630.

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Matousek, J. « Comprehensive comparison of the cytotoxic activities of onconase and bovine seminal ribonuclease ». Comparative Biochemistry and Physiology Part C : Toxicology & ; Pharmacology 136, no 4 (décembre 2003) : 343–56. http://dx.doi.org/10.1016/j.cca.2003.10.005.

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Fagagnini, Andrea, Andrea Pica, Sabrina Fasoli, Riccardo Montioli, Massimo Donadelli, Marco Cordani, Elena Butturini, Laura Acquasaliente, Delia Picone et Giovanni Gotte. « Onconase dimerization through 3D domain swapping : structural investigations and increase in the apoptotic effect in cancer cells* ». Biochemical Journal 474, no 22 (6 novembre 2017) : 3767–81. http://dx.doi.org/10.1042/bcj20170541.

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Onconase® (ONC), a protein extracted from the oocytes of the Rana pipiens frog, is a monomeric member of the secretory ‘pancreatic-type’ RNase superfamily. Interestingly, ONC is the only monomeric ribonuclease endowed with a high cytotoxic activity. In contrast with other monomeric RNases, ONC displays a high cytotoxic activity. In this work, we found that ONC spontaneously forms dimeric traces and that the dimer amount increases about four times after lyophilization from acetic acid solutions. Differently from RNase A (bovine pancreatic ribonuclease) and the bovine seminal ribonuclease, which produce N- and C-terminal domain-swapped conformers, ONC forms only one dimer, here named ONC-D. Cross-linking with divinylsulfone reveals that this dimer forms through the three-dimensional domain swapping of its N-termini, being the C-terminus blocked by a disulfide bond. Also, a homology model is proposed for ONC-D, starting from the well-known structure of RNase A N-swapped dimer and taking into account the results obtained from spectroscopic and stability analyses. Finally, we show that ONC is more cytotoxic and exerts a higher apoptotic effect in its dimeric rather than in its monomeric form, either when administered alone or when accompanied by the chemotherapeutic drug gemcitabine. These results suggest new promising implications in cancer treatment.
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Sica, Filomena, Anna Di Fiore, Antonello Merlino et Lelio Mazzarella. « Structure and Stability of the Non-covalent Swapped Dimer of Bovine Seminal Ribonuclease ». Journal of Biological Chemistry 279, no 35 (9 juin 2004) : 36753–60. http://dx.doi.org/10.1074/jbc.m405655200.

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Opitz, Jochen G., Mauro I. Ciglic, Monika Haugg, Katrin Trautwein-Fritz, Sun Ai Raillard, Thomas M. Jermann et Steven A. Benner. « Origin of the Catalytic Activity of Bovine Seminal Ribonuclease against Double-Stranded RNA† ». Biochemistry 37, no 12 (mars 1998) : 4023–33. http://dx.doi.org/10.1021/bi9722047.

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Schein, Catherine H., Monika Haugg et Steven A. Benner. « Interferon-γ activates the cleavage of double-stranded RNA by bovine seminal ribonuclease ». FEBS Letters 270, no 1-2 (17 septembre 1990) : 229–32. http://dx.doi.org/10.1016/0014-5793(90)81275-s.

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Fiorini, Claudia, Giovanni Gotte, Federica Donnarumma, Delia Picone et Massimo Donadelli. « Bovine seminal ribonuclease triggers Beclin1-mediated autophagic cell death in pancreatic cancer cells ». Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1843, no 5 (mai 2014) : 976–84. http://dx.doi.org/10.1016/j.bbamcr.2014.01.025.

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36

Merlino, Antonello, Luigi Vitagliano, Filomena Sica, Adriana Zagari et Lelio Mazzarella. « Population shift vs induced fit : The case of bovine seminal ribonuclease swapping dimer ». Biopolymers 73, no 6 (2004) : 689–95. http://dx.doi.org/10.1002/bip.20016.

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Russo, Nello, Mena De Nigris, Alberto Di Donato et Giuseppe D'Alessio. « Expression of native dimers of bovine seminal ribonuclease in a eukaryotic cell system ». FEBS Letters 318, no 3 (8 mars 1993) : 242–44. http://dx.doi.org/10.1016/0014-5793(93)80520-5.

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Vatzaki, Efstratia H., Simon C. Allen, Demetres D. Leonidas, Katrin Trautwein-Fritz, Joseph Stackhouse, Steven A. Benner et K. Ravi Acharya. « Crystal structure of a hybrid between ribonuclease A and bovine seminal ribonuclease - the basic surface, at 2.0 A resolution ». European Journal of Biochemistry 260, no 1 (5 février 1999) : 176–82. http://dx.doi.org/10.1046/j.1432-1327.1999.00142.x.

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Sica, F., S. Adinolfi, R. Berisio, C. De Lorenzo, L. Mazzarella, R. Piccoli, L. Vitagliano et A. Zagari. « Crystallization of multiple forms of bovine seminal ribonuclease in the liganded and unliganded state ». Journal of Crystal Growth 196, no 2-4 (janvier 1999) : 305–12. http://dx.doi.org/10.1016/s0022-0248(98)00860-4.

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Filipec, Martin, Zdenka Hašková, Kateřina Havrlíková, Erik Letko, Vladimír Holáň, Josef Matoušek et Ivan Kalousek. « Immunosuppressive effect of bovine seminal ribonuclease on a model of corneal transplantation in rabbit ». Graefe's Archive for Clinical and Experimental Ophthalmology 234, no 9 (septembre 1996) : 586–90. http://dx.doi.org/10.1007/bf00448804.

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Kim, J. S., J. Soucek, J. Matousek et R. T. Raines. « Catalytic activity of bovine seminal ribonuclease is essential for its immunosuppressive and other biological activities ». Biochemical Journal 308, no 2 (1 juin 1995) : 547–50. http://dx.doi.org/10.1042/bj3080547.

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Bovine seminal ribonuclease (BS-RNase) is a homologue of RNase A with special biological properties, including potent immunosuppressive activity. A mutant BS-RNase was created in which His-119, the active-site residue that acts as a general acid during catalysis, was changed to an aspartic acid. H119D BS-RNase formed a dimer with quaternary structure similar to that of the wild-type enzyme but with values of kcat. and kcat./Km for the cleavage of UpA [uridylyl(3′-->5′)adenosine] that were 4 x 10(3)-fold lower. The mutant protein also demonstrated dramatically decreased immunosuppressive, anti-tumour, aspermatogenic, and embryotoxic activities. The catalytic activity of BS-RNase is therefore necessary for its special biological properties.
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42

Barone, G., P. Del Vecchio, D. Fessas, C. Giancola et G. Graziano. « The deconvolution of multi-state transition DSC curves of biological macromolecules : bovine serum albumin and bovine seminal ribonuclease ». Thermochimica Acta 227 (novembre 1993) : 185–95. http://dx.doi.org/10.1016/0040-6031(93)80261-8.

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43

Peters, David, et Jane Peters. « The ribbon of hydrogen bonds and the pseudomolecule in the three-dimensional structure of globular proteins. III. Bovine pancreatic ribonuclease A and bovine seminal ribonuclease ». Biopolymers 65, no 5 (18 octobre 2002) : 347–53. http://dx.doi.org/10.1002/bip.10265.

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44

Dossi, Kyriaki, Vicky G. Tsirkone, Joseph M. Hayes, Josef Matoušek, Pavla Poučková, Josef Souček, Marie Zadinova, Spyros E. Zographos et Demetres D. Leonidas. « Mapping the ribonucleolytic active site of bovine seminal ribonuclease. The binding of pyrimidinyl phosphonucleotide inhibitors ». European Journal of Medicinal Chemistry 44, no 11 (novembre 2009) : 4496–508. http://dx.doi.org/10.1016/j.ejmech.2009.06.039.

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45

Ulbrich, Karel, Jirí Strohalm, Daniela Plocová, David Oupický, Vladimir Subr, Josef Soucek, Pavla Poucková et Josef Matoušek. « Poly[N-(2-Hydroypropyl)Methacrylamide] Conjugates of Bovine Seminal Ribonuclease. Synthesis, Physicochemical, and Preliminary Biological Evaluation ». Journal of Bioactive and Compatible Polymers 15, no 1 (janvier 2000) : 4–26. http://dx.doi.org/10.1177/088391150001500102.

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46

Sica, Filomena, Anna Di Fiore, Adriana Zagari et Lelio Mazzarella. « The unswapped chain of bovine seminal ribonuclease : Crystal structure of the free and liganded monomeric derivative ». Proteins : Structure, Function, and Genetics 52, no 2 (23 juin 2003) : 263–71. http://dx.doi.org/10.1002/prot.10407.

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De Laet, Marie, Dimitri Gilis et Marianne Rooman. « Stability strengths and weaknesses in protein structures detected by statistical potentials : Application to bovine seminal ribonuclease ». Proteins : Structure, Function, and Bioinformatics 84, no 1 (9 décembre 2015) : 143–58. http://dx.doi.org/10.1002/prot.24962.

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Sica, Filomena, Salvatore Adinolfi, Luigi Vitagliano, Adriana Zagari, Sante Capasso et Lelio Mazzarella. « Cosolute effect on crystallization of two dinucleotide complexes of bovine seminal ribonuclease from concentrated salt solutions ». Journal of Crystal Growth 168, no 1-4 (octobre 1996) : 192–97. http://dx.doi.org/10.1016/0022-0248(96)00354-5.

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Sica, Filomena, Andrea Pica, Antonello Merlino, Irene Russo Krauss, Carmine Ercole et Delia Picone. « The multiple forms of bovine seminal ribonuclease : Structure and stability of a C-terminal swapped dimer ». FEBS Letters 587, no 23 (15 octobre 2013) : 3755–62. http://dx.doi.org/10.1016/j.febslet.2013.10.003.

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Giancola, Concetta, Carmine Ercole, Iolanda Fotticchia, Roberta Spadaccini, Elio Pizzo, Giuseppe D’Alessio et Delia Picone. « Structure-cytotoxicity relationships in bovine seminal ribonuclease : new insights from heat and chemical denaturation studies on variants ». FEBS Journal 278, no 1 (1 décembre 2010) : 111–22. http://dx.doi.org/10.1111/j.1742-4658.2010.07937.x.

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