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Journal articles on the topic 'Bovine pancreatic ribonuclease A'

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Published: 11 March 2023

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1

Slav�k, Tom�?, Josef Matou?ek, Josef Fulka, and 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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2

Bello, Carlo, Adriana Lucchiari, Orfeo Buso, and Mauro Tonellato. "Semisynthetic studies on bovine pancreatic ribonuclease." International Journal of Peptide and Protein Research 23, no. 1 (January 12, 2009): 61–71. http://dx.doi.org/10.1111/j.1399-3011.1984.tb02693.x.

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3

Jeremy Johnson, R., Mary Andorfer, Ashton Chaffee, Melanie Clark, Nathan Clarke, Grace Douglass, Elizabeth Ellis, et al. "Proteopedia entry: Bovine pancreatic ribonuclease a." Biochemistry and Molecular Biology Education 40, no. 1 (November 26, 2011): 75. http://dx.doi.org/10.1002/bmb.20568.

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4

Ye, X. Y., and T. B. Ng. "First demonstration of lactoribonuclease, a ribonuclease from bovine milk with similarity to bovine pancreatic ribonuclease." Life Sciences 67, no. 16 (September 2000): 2025–32. http://dx.doi.org/10.1016/s0024-3205(00)00784-0.

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5

Tarragona-Fiol, A., C. J. Taylorson, and B. R. Rabin. "Cloning and Expression of An Engineered Human Pancreatic Ribonuclease." Protein & Peptide Letters 1, no. 2 (September 1994): 76–83. http://dx.doi.org/10.2174/0929866501666220424121436.

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The coding sequence for the human pancreatic ribonuclease (HP-RNase) gene has been obtained from genomic DNA extracted from buccal epithelial cells. In order to direct the expression of the recombinant human pancreatic enzyme to the periplasmic space of E.coli, the bovine pancreatic RNase signal sequence has been fused 5' to the human gene. Initial attempts to express the recombinant enzyme were not successful, consequently site-directed mutagenesis tehniques were used to genetically engineer the HP-RNase gene to enable expression in E.coli. The resultant engineered enzyme shows similar kinetic characteristics to the homologous bovine enzyme.
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6

RAMNATH, S., and PAUL J. VITHAYATHIL. "IRREVERSIBLE THERMAL DENATURATION OF BOVINE PANCREATIC RIBONUCLEASE-A." International Journal of Peptide and Protein Research 17, no. 1 (January 12, 2009): 107–17. http://dx.doi.org/10.1111/j.1399-3011.1981.tb01973.x.

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7

Fedorov, Alexander A., Diane Joseph-McCarthy, Elena Fedorov, Dora Sirakova, Isaac Graf, and Steven C. Almo. "Ionic Interactions in Crystalline Bovine Pancreatic Ribonuclease A†,‡." Biochemistry 35, no. 50 (January 1996): 15962–79. http://dx.doi.org/10.1021/bi961533g.

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8

Leich, Franziska, Jens Köditz, Renate Ulbrich-Hofman, and Ulrich Arnold. "Tandemization Endows Bovine Pancreatic Ribonuclease with Cytotoxic Activity." Journal of Molecular Biology 358, no. 5 (May 2006): 1305–13. http://dx.doi.org/10.1016/j.jmb.2006.03.007.

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9

Matousek, Josef, Josef Soucek, Jan Riha, Todd R. Zankel, and 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 (October 1995): 235–41. http://dx.doi.org/10.1016/0305-0491(95)00075-5.

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10

NAMBIAR, Krishnan P., Joseph STACKHOUSE, Scott R. PRESNELL, and Steven A. BENNER. "Expression of bovine pancreatic ribonuclease A in Escherichia coli." European Journal of Biochemistry 163, no. 1 (February 1987): 67–71. http://dx.doi.org/10.1111/j.1432-1033.1987.tb10737.x.

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11

Picone, Delia, Federica Donnarumma, Giarita Ferraro, Irene Russo Krauss, Andrea Fagagnini, Giovanni Gotte, and Antonello Merlino. "Platinated oligomers of bovine pancreatic ribonuclease: Structure and stability." Journal of Inorganic Biochemistry 146 (May 2015): 37–43. http://dx.doi.org/10.1016/j.jinorgbio.2015.02.011.

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12

Tarragona-Fiol, Antonio, Christopher J. Taylorson, John M. Ward, and Brian R. Rabin. "Production of mature bovine pancreatic ribonuclease in Escherichia coli." Gene 118, no. 2 (September 1992): 239–45. http://dx.doi.org/10.1016/0378-1119(92)90194-t.

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13

Vilà, Roger, Antoni Benito, Marc Ribó, and Maria Vilanova. "Mapping the stability clusters in bovine pancreatic ribonuclease A." Biopolymers 91, no. 12 (April 16, 2009): 1038–47. http://dx.doi.org/10.1002/bip.21204.

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14

Kurapkat, Günther, Peter Krüger, Axel Wollmer, Jörg Fleischhauer, Bernd Kramer, Elke Zobel, Axel Koslowski, Henrik Botterweck, and Robert W. Woody. "Calculations of the CD spectrum of bovine pancreatic ribonuclease." Biopolymers 41, no. 3 (March 1997): 267–87. http://dx.doi.org/10.1002/(sici)1097-0282(199703)41:3<267::aid-bip3>3.0.co;2-q.

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15

Ferraro, Giarita, Alessandro Pratesi, Luigi Messori, and Antonello Merlino. "Protein interactions of dirhodium tetraacetate: a structural study." Dalton Transactions 49, no. 8 (2020): 2412–16. http://dx.doi.org/10.1039/c9dt04819g.

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The interactions between the cytotoxic paddlewheel dirhodium complex [Rh2(μ-O2CCH3)4] and the model protein bovine pancreatic ribonuclease (RNase A) were investigated by high-resolution mass spectrometry and X-ray crystallography.
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16

Parise, A., N. Russo, and T. Marino. "The platination mechanism of RNase A by arsenoplatin: insight from the theoretical study." Inorganic Chemistry Frontiers 8, no. 7 (2021): 1795–803. http://dx.doi.org/10.1039/d0qi01165g.

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A detailed metalation process of the bovine pancreatic ribonuclease (RNase A) by a novel multitarget anti-cancer agent arsenoplatin-1, ([Pt(μ-NHC(CH3)O)2ClAs(OH)2]), performed at DFT level and using different models size is provided.
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17

Fagagnini, Andrea, Andrea Pica, Sabrina Fasoli, Riccardo Montioli, Massimo Donadelli, Marco Cordani, Elena Butturini, Laura Acquasaliente, Delia Picone, and Giovanni Gotte. "Onconase dimerization through 3D domain swapping: structural investigations and increase in the apoptotic effect in cancer cells*." Biochemical Journal 474, no. 22 (November 6, 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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18

Juminaga, D., W. J. Wedemeyer, and H. A. Scheraga. "Proline Isomerization in Bovine Pancreatic Ribonuclease A. 1. Unfolding Conditions†." Biochemistry 37, no. 33 (August 1998): 11614–20. http://dx.doi.org/10.1021/bi981028e.

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19

Dung, M. H., and J. A. Bell. "Structure of Crystal Form IX of Bovine Pancreatic Ribonuclease A." Acta Crystallographica Section D Biological Crystallography 53, no. 4 (July 1, 1997): 419–25. http://dx.doi.org/10.1107/s0907444997000929.

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20

Bhat, Rajiv, William J. Wedemeyer, and Harold A. Scheraga. "Proline Isomerization in Bovine Pancreatic Ribonuclease A. 2. Folding Conditions†." Biochemistry 42, no. 19 (May 2003): 5722–28. http://dx.doi.org/10.1021/bi030024t.

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21

Sasaki, Diane M., Carmen E. Restrepo Kelly, Philip D. Martin, Brian F. P. Edwards, and Marilynn S. Doscher. "A semisynthetic bovine pancreatic ribonuclease containing a unique nitrotyrosine residue." Archives of Biochemistry and Biophysics 241, no. 1 (August 1985): 132–40. http://dx.doi.org/10.1016/0003-9861(85)90369-8.

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22

Alonso, Juli, M. Victòria Nogués, and Claudi M. Cuchillo. "Modification of bovine pancreatic ribonuclease A with 6-chloropurine riboside." Archives of Biochemistry and Biophysics 246, no. 2 (May 1986): 681–89. http://dx.doi.org/10.1016/0003-9861(86)90324-3.

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23

Rothwarf, David M., and Harold A. Scheraga. "Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution." Biochemistry 32, no. 10 (March 16, 1993): 2671–79. http://dx.doi.org/10.1021/bi00061a027.

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24

Rothwarf, David M., and Harold A. Scheraga. "Regeneration of bovine pancreatic ribonuclease A. 2. Kinetics of regeneration." Biochemistry 32, no. 10 (March 16, 1993): 2680–89. http://dx.doi.org/10.1021/bi00061a028.

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25

Schein, C. H., E. Boix, M. Haugg, K. P. Holliger, S. Hemmi, G. Frank, and H. Schwalbe. "Secretion of mammalian ribonucleases from Escherichia coli using the signal sequence of murine spleen ribonuclease." Biochemical Journal 283, no. 1 (April 1, 1992): 137–44. http://dx.doi.org/10.1042/bj2830137.

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A nucleotide sequence identical with that of the recently identified murine pancreatic ribonuclease (RNAase) was isolated from a murine spleen cDNA library. Active RNAase was expressed and secreted from Escherichia coli lon-htpr- transformed with a plasmid containing the E. coli trp promoter followed by the murine RNAase gene sequence, including the original eukaryotic 26-amino-acid signal sequence. Approx. 1 mg of properly matured RNAase protein/litre was secreted into the medium of a fermentor culture after the promotor was induced by tryptophan starvation. When the signal sequence was deleted from the plasmid, intracellular RNAase activity was very low and there was no significant supernatant RNAase activity. Even higher RNAase yields were obtained with a synthetic gene for bovine pancreatic ribonuclease cloned after the signal sequence of the murine gene. About 2 mg of correctly processed RNAase A/litre was isolated from the growth medium, and a further 8-10 mg of correctly processed RNAase/litre could be isolated from the soluble fraction of the cells. Thus this eukaryotic signal sequence is both recognized by the E. coli transport and processing apparatus and gives efficient secretion, as well as export, of active, mature mammalian RNAases.
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26

Katoh, Hideo, Makkiko Yoshinaga, Tamami Yanagita, Kazuko Ohgi, Masachika Irie, Jaap J. Beintema, and Durk Meinsma. "Kinetic studies on turtle pancreatic ribonuclease: a comparative study of the base specificities of the B2 and P0 sites of bovine pancreatic ribonuclease A and turtle pancreatic ribonuclease." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 873, no. 3 (October 1986): 367–71. http://dx.doi.org/10.1016/0167-4838(86)90085-3.

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27

Kurpiewska, K., J. Font, M. Ribó, M. Vilanova, and K. Lewiński. "Structural insight into protein stability – bovine pancreatic ribonuclease A variants studies." Acta Crystallographica Section A Foundations of Crystallography 62, a1 (August 6, 2006): s175. http://dx.doi.org/10.1107/s0108767306096504.

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28

WANG, Ming-Hua, Zhi-Xin WANG, and Kang-Yuan ZHAO. "Kinetics of inactivation of bovine pancreatic ribonuclease A by bromopyruvic acid." Biochemical Journal 320, no. 1 (November 15, 1996): 187–92. http://dx.doi.org/10.1042/bj3200187.

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The kinetic theory of substrate reaction during the modification of enzyme activity [Duggleby (1986) J. Theor. Biol. 123, 67–80; Wang and Tsou (1990) J. Theor. Biol. 142, 531–549] has been applied to a study of the inactivation kinetics of ribonuclease A by bromopyruvic acid. The results show that irreversible inhibition belongs to a non-competitive complexing type inhibition. On the basis of the kinetic equation of substrate reaction in the presence of the inhibitor, all microscopic kinetic constants for the free enzyme, the enzyme–substrate complex and the enzyme–product complex have been determined. The non-competitive inhibition type indicates that neither the substrate nor the product affects the binding of bromopyruvic acid to the enzyme and that the ionization state of His-119 may be the same in both the enzyme–substrate and the enzyme–product complexes.
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29

Venkatesh, Yeldur P., and Paul J. Vithayathil. "Isolation and characterization of monodeamidated derivatives of bovine pancreatic Ribonuclease A." International Journal of Peptide and Protein Research 23, no. 5 (January 12, 2009): 494–505. http://dx.doi.org/10.1111/j.1399-3011.1984.tb02750.x.

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30

Cuchillo, Claudi M., M. Victòria Nogués, and Ronald T. Raines. "Bovine Pancreatic Ribonuclease: Fifty Years of the First Enzymatic Reaction Mechanism." Biochemistry 50, no. 37 (September 20, 2011): 7835–41. http://dx.doi.org/10.1021/bi201075b.

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31

Liu, W., and C. L. Tsou. "Activity change during unfolding of bovine pancreatic ribonuclease A in guanidine." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 916, no. 3 (December 1987): 455–64. http://dx.doi.org/10.1016/0167-4838(87)90192-0.

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32

PARÉS, XAVIER, PERE PUIGDOMÉNECH, and CLAUDI M. CUCHILLO. "REACTION OF BOVINE PANCREATIC RIBONUCLEASE A WITH 6-CHLOROPURINE RIBOSIDE 5‘-MONOPHOSPHATE." International Journal of Peptide and Protein Research 16, no. 4 (January 12, 2009): 241–44. http://dx.doi.org/10.1111/j.1399-3011.1980.tb02582.x.

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33

RICO, Manuel, Marta BRUIX, Jorge SANTORO, Carlos GONZALEZ, Jose Luis NEIRA, Jose Luis NIETO, and Jose HERRANZ. "Sequential 1H-NMR assignment and solution structure of bovine pancreatic ribonuclease A." European Journal of Biochemistry 183, no. 3 (August 1989): 623–38. http://dx.doi.org/10.1111/j.1432-1033.1989.tb21092.x.

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34

Trautwein, Katrin, Philipp Holliger, Joseph Stackhouse, and Steven A. Benner. "Site-directed mutagenesis of bovine pancreatic ribonuclease: Lysine-41 and aspartate-121." FEBS Letters 281, no. 1-2 (April 9, 1991): 275–77. http://dx.doi.org/10.1016/0014-5793(91)80410-5.

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35

Talluri, S., and H. A. Scheraga. "Amide HD exchange in the thermal transition of bovine pancreatic Ribonuclease A." Biochemical and Biophysical Research Communications 172, no. 2 (October 1990): 800–803. http://dx.doi.org/10.1016/0006-291x(90)90745-9.

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36

Okorokov, A. L., K. I. Panov, R. H. T. Poele, H. J. Breukelman, A. Furia, M. Y. Karpeisky, and J. J. Beintema. "An Efficient System for Active Bovine Pancreatic Ribonuclease Expression in Escherichia coli." Protein Expression and Purification 6, no. 4 (August 1995): 472–80. http://dx.doi.org/10.1006/prep.1995.1063.

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37

Asgari, Somayeh, Behzad Shareghi, Parisa Nooraei, Nayere Bahamin, and Sadegh Farhadian. "Denaturation studies on bovine pancreatic ribonuclease A by cationic and anionic surfactants." Clinical Biochemistry 44, no. 13 (September 2011): S89—S90. http://dx.doi.org/10.1016/j.clinbiochem.2011.08.199.

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38

Merlino, Antonello, Delia Picone, Carmine Ercole, Anna Balsamo, and Filomena Sica. "Chain termini cross-talk in the swapping process of bovine pancreatic ribonuclease." Biochimie 94, no. 5 (May 2012): 1108–18. http://dx.doi.org/10.1016/j.biochi.2012.01.010.

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39

Slifman, N. R., D. A. Loegering, D. J. McKean, and G. J. Gleich. "Ribonuclease activity associated with human eosinophil-derived neurotoxin and eosinophil cationic protein." Journal of Immunology 137, no. 9 (November 1, 1986): 2913–17. http://dx.doi.org/10.4049/jimmunol.137.9.2913.

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Abstract The eosinophil granule contains a series of basic proteins, including major basic protein, eosinophil peroxidase, eosinophil-derived neurotoxin (EDN), and eosinophil cationic protein (ECP). Both EDN and ECP are neurotoxins and helminthotoxins. Comparison of the partial N-terminal amino acid sequences of EDN and ECP showed 67% identity; surprisingly, they also showed structural homology to pancreatic ribonuclease (RNase). Therefore, we determined whether EDN and ECP possess RNase enzymatic activity. By spectrophotometric assay of acid soluble nucleotides formed from yeast RNA, purified EDN showed RNase activity similar to bovine pancreatic RNase, whereas ECP was 50 to 100 times less active. The RNase activity associated with ECP was not significantly inhibited after exposure of ECP to polyclonal or monoclonal antibody to EDN. These results indicate that EDN and ECP both possess RNase activity, the RNase activity of EDN and ECP is specific, and EDN and ECP have maintained not only structural but also functional homology to pancreatic RNase.
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40

Murthy, B. S., and R. Sirdeshmukh. "Sensitivity of monomeric and dimeric forms of bovine seminal ribonuclease to human placental ribonuclease inhibitor." Biochemical Journal 281, no. 2 (January 15, 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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41

OKAMOTO, YUKO. "TACKLING THE MULTIPLE-MINIMA PROBLEM IN PROTEIN FOLDING BY MONTE CARLO SIMULATED ANNEALING AND GENERALIZED-ENSEMBLE ALGORITHMS." International Journal of Modern Physics C 10, no. 08 (December 1999): 1571–82. http://dx.doi.org/10.1142/s0129183199001352.

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Monte Carlo simulations based on simulated annealing and multicanonical algorithm have been performed to predict the secondary and tertiary structures of oligopeptide systems. Two oligopeptides, C-peptide of ribonuclease A and the fragment BPTI(16-36) of bovine pancreatic trypsin inhibitor, were studied. Only the amino-acid sequence information was used as input and initial conformations were randomly generated. The lowest-energy conformations obtained have α-helix structure and β-sheet structure for C-peptide and BPTI(16-36), respectively, in remarkable agreement with experimental results.
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42

Laity, J. H., S. Shimotakahara, and H. A. Scheraga. "Expression of wild-type and mutant bovine pancreatic ribonuclease A in Escherichia coli." Proceedings of the National Academy of Sciences 90, no. 2 (January 15, 1993): 615–19. http://dx.doi.org/10.1073/pnas.90.2.615.

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43

Tanimizu, N., H. Ueno, and R. Hayashi. "Role of Phe120 in the Activity and Structure of Bovine Pancreatic Ribonuclease A." Journal of Biochemistry 124, no. 2 (August 1, 1998): 410–16. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a022127.

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44

Wower, Jacek, Michael Aymie, Stephen S. Hixson, and Robert A. Zimmermann. "Photochemical labeling of bovine pancreatic ribonuclease A with 8-azidoadenosine 3',5'-bisphosphate." Biochemistry 28, no. 4 (February 21, 1989): 1563–67. http://dx.doi.org/10.1021/bi00430a021.

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45

Rico, M., J. Santoro, C. Gonzalez, M. Bruix, J. L. Neira, and J. L. Nieto. "Refined solution structure of bovine pancreatic Ribonuclease A by1H NMR methods. Sidechain dynamics." Applied Magnetic Resonance 4, no. 4 (June 1993): 385–415. http://dx.doi.org/10.1007/bf03162456.

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46

Rothwarf, David M., and Harold A. Scheraga. "Regeneration of bovine pancreatic ribonuclease A. 4. Temperature dependence of the regeneration rate." Biochemistry 32, no. 10 (March 16, 1993): 2698–703. http://dx.doi.org/10.1021/bi00061a030.

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47

Fiorini, Claudia, Giovanni Gotte, Federica Donnarumma, Delia Picone, and 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 (May 2014): 976–84. http://dx.doi.org/10.1016/j.bbamcr.2014.01.025.

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48

Trifonova, Ekaterina A., Mikhail V. Sapotsky, Marina L. Komarova, Andrey B. Scherban, Vladimir K. Shumny, Albina M. Polyakova, Larisa A. Lapshina, Alex V. Kochetov, and Vladimir I. Malinovsky. "Protection of transgenic tobacco plants expressing bovine pancreatic ribonuclease against tobacco mosaic virus." Plant Cell Reports 26, no. 7 (January 23, 2007): 1121–26. http://dx.doi.org/10.1007/s00299-006-0298-z.

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49

Russo, Nello, Robert Shapiro, and Bert L. Vallee. "5′-Diphosphoadenosine 3′-Phosphate Is a Potent Inhibitor of Bovine Pancreatic Ribonuclease A." Biochemical and Biophysical Research Communications 231, no. 3 (February 1997): 671–74. http://dx.doi.org/10.1006/bbrc.1997.6167.

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50

Peters, David, and 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 (October 18, 2002): 347–53. http://dx.doi.org/10.1002/bip.10265.

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