Relevant bibliographies by topics / Bovine seminal ribonuclease

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Bovine seminal ribonuclease'

Author: Grafiati
Published: 11 March 2023

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Journal articles on the topic "Bovine seminal ribonuclease"

1

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

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

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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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4

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

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

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6

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

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

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8

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

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

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

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Dissertations / Theses on the topic "Bovine seminal ribonuclease"

1

VOTTARIELLO, FRANCESCA. "OLIGOMERIZATION OF RNase A:a) A STUDY OF THE INFLUENCE OF SERINE 80 RESIDUE ON THE 3D DOMAIN SWAPPING MECHANISMb) “ZERO-LENGTH” DIMERS OF RNase A AND THEIR CATIONIZATION WITH PEI." Doctoral thesis, 2010. http://hdl.handle.net/11562/344075.

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Abstract:
"Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound to each other through a zero-length amide bond [Simons, B.L. et al. (2007) Proteins 66, 183-195], were analyzed, and tested for their possible in vitro cytotoxic activity. Results: (i) Besides dimers, also trimers and higher oligomers can be identified among the products of the covalently linking reaction. (ii) The "zero-length" dimers prepared by us appear not to be a unique species, as was instead reported by Simons et al. The product is heterogeneous, as shown by the involvement in the amide bond of amino and carboxyl groups others than only those belonging to Lys66 and Glu9. This is demonstrated by results obtained with two RNase A mutants, E9A and K66A. (iii) The "zero-length" dimers degrade poly(A).poly(U) (dsRNA) and yeast RNA (ssRNA): while the activity against poly(A).poly(U) increases with the increase of the oligomer's basicity, the activity towards yeast RNA decreases with the increase of oligomers' basicity, in agreement with many previous data, but in contrast with the results reported by Simons et al. (iv) No cytotoxicity against various tumor cells lines could be evidenced in RNase A "zero-length" dimers. (v) They instead become cytotoxic if cationized by conjugation with polyethylenimine [Futami, J. et al. (2005) J. Biosci. Bioengin. 99, 95-103]. However, polyethylenimine derivatives of RNase A "zero-length" dimers and native, monomeric RNase A are equally cytotoxic. In other words, protein "dimericity" does not play any role in this case. Moreover, (vi) cytotoxicity seems not to be specific for tumor cells: polyethylenimine-cationized native RNase A is also cytotoxic towards human monocytes.
"Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound to each other through a zero-length amide bond [Simons, B.L. et al. (2007) Proteins 66, 183-195], were analyzed, and tested for their possible in vitro cytotoxic activity. Results: (i) Besides dimers, also trimers and higher oligomers can be identified among the products of the covalently linking reaction. (ii) The "zero-length" dimers prepared by us appear not to be a unique species, as was instead reported by Simons et al. The product is heterogeneous, as shown by the involvement in the amide bond of amino and carboxyl groups others than only those belonging to Lys66 and Glu9. This is demonstrated by results obtained with two RNase A mutants, E9A and K66A. (iii) The "zero-length" dimers degrade poly(A).poly(U) (dsRNA) and yeast RNA (ssRNA): while the activity against poly(A).poly(U) increases with the increase of the oligomer's basicity, the activity towards yeast RNA decreases with the increase of oligomers' basicity, in agreement with many previous data, but in contrast with the results reported by Simons et al. (iv) No cytotoxicity against various tumor cells lines could be evidenced in RNase A "zero-length" dimers. (v) They instead become cytotoxic if cationized by conjugation with polyethylenimine [Futami, J. et al. (2005) J. Biosci. Bioengin. 99, 95-103]. However, polyethylenimine derivatives of RNase A "zero-length" dimers and native, monomeric RNase A are equally cytotoxic. In other words, protein "dimericity" does not play any role in this case. Moreover, (vi) cytotoxicity seems not to be specific for tumor cells: polyethylenimine-cationized native RNase A is also cytotoxic towards human monocytes.
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Book chapters on the topic "Bovine seminal ribonuclease"

1

Mazzarella, L., L. Vitagliano, A. Zagari, and S. Capasso. "Subunit Assembly in Bovine Seminal Ribonuclease." In Topics in Molecular Organization and Engineering, 301–12. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0822-5_28.

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Di Donato, A., V. Cafaro, M. De Nigris, G. Minopoli, and G. D’Alessio. "Engineering of Bovine Seminal Ribonuclease: Expression of the Secreted Recombinant Protein." In Topics in Molecular Organization and Engineering, 187–92. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0822-5_15.

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3

Picone, Delia, Antonello Merlino, and Roberta Spadaccini. "Bovine Seminal Ribonuclease and Its Special Features: When Two is Better Than One." In Antitumor Potential and other Emerging Medicinal Properties of Natural Compounds, 93–113. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6214-5_7.

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4

Barone, G., F. Catanzano, G. Graziano, V. Cafaro, G. D’Alessio, and A. Di Donato. "Thermodynamic stability of a monomeric derivative of bovine seminal ribonuclease." In Progress in Biotechnology, 211–16. Elsevier, 1998. http://dx.doi.org/10.1016/s0921-0423(98)80032-4.

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You might also be interested in the extended bibliographies on the topic 'Bovine seminal ribonuclease' for particular source types:
Journal articles
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