Bibliographies thématiques / Bovine seminal ribonuclease

Littérature scientifique sur le sujet « Bovine seminal ribonuclease »

Auteur : Grafiati

Publié le 11 mars 2023

Créez une référence correcte selon les styles APA, MLA, Chicago, Harvard et plusieurs autres

Choisissez une source :

Sommaire

Articles de revues
Thèses
Chapitres de livres

Consultez les listes thématiques d’articles de revues, de livres, de thèses, de rapports de conférences et d’autres sources académiques sur le sujet « Bovine seminal ribonuclease ».

À côté de chaque source dans la liste de références il y a un bouton « Ajouter à la bibliographie ». Cliquez sur ce bouton, et nous générerons automatiquement la référence bibliographique pour la source choisie selon votre style de citation préféré : APA, MLA, Harvard, Vancouver, Chicago, etc.

Vous pouvez aussi télécharger le texte intégral de la publication scolaire au format pdf et consulter son résumé en ligne lorsque ces informations sont inclues dans les métadonnées.

Articles de revues sur le sujet "Bovine seminal ribonuclease"

Catanzano, Francesca, et G. Graziano. « Domains in bovine seminal ribonuclease ». Journal of Thermal Analysis and Calorimetry 91, n^o 1 (1 octobre 2007) : 61–66. http://dx.doi.org/10.1007/s10973-007-8537-2.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

Poučková, P., J. Souček, J. Matoušek, M. Zadinová, D. Hloušková, J. Polívková et L. Navrátil. « Antitumor action of bovine seminal ribonuclease ». Folia Microbiologica 43, n^o 5 (octobre 1998) : 511–12. http://dx.doi.org/10.1007/bf02820807.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

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, n^o 5 (2000) : 394–99. http://dx.doi.org/10.1002/1097-010x(20001001)287:5<394 ::aid-jez7>3.0.co;2-e.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

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, n^o 1 (février 1994) : 119–24. http://dx.doi.org/10.1006/bbrc.1994.1202.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

Kim, J. S., et R. T. Raines. « Bovine seminal ribonuclease produced from a synthetic gene ». Journal of Biological Chemistry 268, n^o 23 (août 1993) : 17392–96. http://dx.doi.org/10.1016/s0021-9258(19)85347-4.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

Lee, J. Eugene, et Ronald T. Raines. « Cytotoxicity of Bovine Seminal Ribonuclease : Monomer versus Dimer† ». Biochemistry 44, n^o 48 (décembre 2005) : 15760–67. http://dx.doi.org/10.1021/bi051668z.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

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, n^o 4 (1 juillet 1993) : 389–402. http://dx.doi.org/10.1107/s0907444993003403.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

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, n^o 1 (mai 1993) : 155–60. http://dx.doi.org/10.1006/bbrc.1993.1603.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

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, n^o 3 (13 décembre 2013) : 842–50. http://dx.doi.org/10.1111/febs.12651.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

Kim, Jin-Soo, et Ronald T. Raines. « A Misfolded but Active Dimer of Bovine Seminal Ribonuclease ». European Journal of Biochemistry 224, n^o 1 (août 1994) : 109–14. http://dx.doi.org/10.1111/j.1432-1033.1994.tb20001.x.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

Plus de sources

Thèses sur le sujet "Bovine seminal ribonuclease"

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.

Texte intégral

Résumé :

"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.

Styles APA, Harvard, Vancouver, ISO, etc.

Chapitres de livres sur le sujet "Bovine seminal ribonuclease"

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

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

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

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

Picone, Delia, Antonello Merlino et Roberta Spadaccini. « Bovine Seminal Ribonuclease and Its Special Features : When Two is Better Than One ». Dans 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.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

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

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

Nous offrons des réductions sur tous les plans premium pour les auteurs dont les œuvres sont incluses dans des sélections littéraires thématiques. Contactez-nous pour obtenir un code promo unique!