Littérature scientifique sur le sujet « Oligomerization, ribonucleases »
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Articles de revues sur le sujet "Oligomerization, ribonucleases"
Gotte, Giovanni, et Massimo Libonati. « Oligomerization of Ribonuclease A ». Journal of Biological Chemistry 279, no 35 (24 juin 2004) : 36670–79. http://dx.doi.org/10.1074/jbc.m404780200.
Texte intégralGotte, Giovanni, et Massimo Libonati. « Oligomerization of ribonuclease A under reducing conditions ». Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1784, no 4 (avril 2008) : 638–50. http://dx.doi.org/10.1016/j.bbapap.2007.12.013.
Texte intégralLibonati, M., G. Gotte et F. Vottariello. « A Novel Biological Actions Acquired by Ribonuclease Through Oligomerization ». Current Pharmaceutical Biotechnology 9, no 3 (1 juin 2008) : 200–209. http://dx.doi.org/10.2174/138920108784567308.
Texte intégralLIBONATI, Massimo, et Giovanni GOTTE. « Oligomerization of bovine ribonuclease A : structural and functional features of its multimers ». Biochemical Journal 380, no 2 (1 juin 2004) : 311–27. http://dx.doi.org/10.1042/bj20031922.
Texte intégralFagagnini, Andrea, Miguel Garavís, Irene Gómez-Pinto, Sabrina Fasoli, Giovanni Gotte et Douglas V. Laurents. « NMR Characterization of Angiogenin Variants and tRNAAla Products Impacting Aberrant Protein Oligomerization ». International Journal of Molecular Sciences 22, no 3 (1 février 2021) : 1439. http://dx.doi.org/10.3390/ijms22031439.
Texte intégralYan, Yong-Bin, Jun Zhang, Hua-Wei He et Hai-Meng Zhou. « Oligomerization and Aggregation of Bovine Pancreatic Ribonuclease A : Characteristic Events Observed by FTIR Spectroscopy ». Biophysical Journal 90, no 7 (avril 2006) : 2525–33. http://dx.doi.org/10.1529/biophysj.105.071530.
Texte intégralZhang, Jun, et Yong-Bin Yan. « Oligomerization and Aggregation of Bovine Pancreatic Ribonuclease A:Backbone Hydration Probed by Infrared Band-Shift ». Protein & ; Peptide Letters 15, no 7 (1 juillet 2008) : 650–57. http://dx.doi.org/10.2174/092986608785133645.
Texte intégralSokurenko, Yulia, Alsu Nadyrova, Vera Ulyanova et Olga Ilinskaya. « Extracellular Ribonuclease fromBacillus licheniformis(Balifase), a New Member of the N1/T1 RNase Superfamily ». BioMed Research International 2016 (2016) : 1–9. http://dx.doi.org/10.1155/2016/4239375.
Texte intégralBombaci, Giuseppe, Mayuresh Anant Sarangdhar, Nicola Andina, Aubry Tardivel, Eric Chi-Wang Yu, Gillian M. Mackie, Matthew Pugh et al. « LRR-protein RNH1 dampens the inflammasome activation and is associated with COVID-19 severity ». Life Science Alliance 5, no 6 (7 mars 2022) : e202101226. http://dx.doi.org/10.26508/lsa.202101226.
Texte intégralCanals, Albert, Joan Pous, Alı́cia Guasch, Antoni Benito, Marc Ribó, Maria Vilanova et Miquel Coll. « The Structure of an Engineered Domain-Swapped Ribonuclease Dimer and Its Implications for the Evolution of Proteins toward Oligomerization ». Structure 9, no 10 (octobre 2001) : 967–76. http://dx.doi.org/10.1016/s0969-2126(01)00659-1.
Texte intégralThèses sur le sujet "Oligomerization, ribonucleases"
Nissbeck, Mikael. « Determining the oligomeric structure of PARN ». Thesis, Uppsala universitet, Institutionen för cell- och molekylärbiologi, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-167233.
Texte intégralsabrina, fasoli. « STRUCTURAL DETERMINANTS AFFECTING THE OLIGOMERIZATION TENDENCY OF SOME PANCREATIC RIBONUCLEASES ». Doctoral thesis, 2020. http://hdl.handle.net/11562/1017109.
Texte intégralFAGAGNINI, ANDREA. « Oligomerization of RNase A and onconase : structural determinants and influence on the functional features of the two enzymes ». Doctoral thesis, 2017. http://hdl.handle.net/11562/961013.
Texte intégralVOTTARIELLO, 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"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.