Academic literature on the topic 'Oligomerization, ribonucleases'
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Journal articles on the topic "Oligomerization, ribonucleases"
Gotte, Giovanni, and Massimo Libonati. "Oligomerization of Ribonuclease A." Journal of Biological Chemistry 279, no. 35 (June 24, 2004): 36670–79. http://dx.doi.org/10.1074/jbc.m404780200.
Full textGotte, Giovanni, and Massimo Libonati. "Oligomerization of ribonuclease A under reducing conditions." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1784, no. 4 (April 2008): 638–50. http://dx.doi.org/10.1016/j.bbapap.2007.12.013.
Full textLibonati, M., G. Gotte, and F. Vottariello. "A Novel Biological Actions Acquired by Ribonuclease Through Oligomerization." Current Pharmaceutical Biotechnology 9, no. 3 (June 1, 2008): 200–209. http://dx.doi.org/10.2174/138920108784567308.
Full textLIBONATI, Massimo, and Giovanni GOTTE. "Oligomerization of bovine ribonuclease A: structural and functional features of its multimers." Biochemical Journal 380, no. 2 (June 1, 2004): 311–27. http://dx.doi.org/10.1042/bj20031922.
Full textFagagnini, Andrea, Miguel Garavís, Irene Gómez-Pinto, Sabrina Fasoli, Giovanni Gotte, and Douglas V. Laurents. "NMR Characterization of Angiogenin Variants and tRNAAla Products Impacting Aberrant Protein Oligomerization." International Journal of Molecular Sciences 22, no. 3 (February 1, 2021): 1439. http://dx.doi.org/10.3390/ijms22031439.
Full textYan, Yong-Bin, Jun Zhang, Hua-Wei He, and Hai-Meng Zhou. "Oligomerization and Aggregation of Bovine Pancreatic Ribonuclease A: Characteristic Events Observed by FTIR Spectroscopy." Biophysical Journal 90, no. 7 (April 2006): 2525–33. http://dx.doi.org/10.1529/biophysj.105.071530.
Full textZhang, Jun, and Yong-Bin Yan. "Oligomerization and Aggregation of Bovine Pancreatic Ribonuclease A:Backbone Hydration Probed by Infrared Band-Shift." Protein & Peptide Letters 15, no. 7 (July 1, 2008): 650–57. http://dx.doi.org/10.2174/092986608785133645.
Full textSokurenko, Yulia, Alsu Nadyrova, Vera Ulyanova, and 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.
Full textBombaci, 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 (March 7, 2022): e202101226. http://dx.doi.org/10.26508/lsa.202101226.
Full textCanals, Albert, Joan Pous, Alı́cia Guasch, Antoni Benito, Marc Ribó, Maria Vilanova, and 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 (October 2001): 967–76. http://dx.doi.org/10.1016/s0969-2126(01)00659-1.
Full textDissertations / Theses on the topic "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.
Full textsabrina, fasoli. "STRUCTURAL DETERMINANTS AFFECTING THE OLIGOMERIZATION TENDENCY OF SOME PANCREATIC RIBONUCLEASES." Doctoral thesis, 2020. http://hdl.handle.net/11562/1017109.
Full textFAGAGNINI, 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.
Full textVOTTARIELLO, 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.
Full text"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.