title: Interactions of the cytotoxic RNase A dimers with the cytosolic ribonuclease inhibitor.
abstract: Ribonuclease A (RNase A) dimers have been recently found to be endowed with some of the special, i.e., non-catalytic biological activities of RNases, such as antitumor and aspermatogenic activities. These activities have been so far attributed to RNases which can escape the neutralizing action of the cytosolic RNase inhibitor (cRI). However, when the interactions of the two cytotoxic RNase A dimers with cRI were investigated in a quantitative fashion and at the molecular level, the dimers were found to bind cRI with high affinity and to form tight complexes.
authors.affiliation: Dipartimento di Biologia Strutturale e Funzionale, Università di Napoli Federico II, Italy.
authors.forename: Mariarosaria
authors.initials: M
authors.lastname: Naddeo
authors.forename: Luigi
authors.initials: L
authors.lastname: Vitagliano
authors.forename: Aniello
authors.initials: A
authors.lastname: Russo
authors.forename: Giovanni
authors.initials: G
authors.lastname: Gotte
authors.forename: Giuseppe
authors.initials: G
authors.lastname: D'Alessio
authors.forename: Salvatore
authors.initials: S
authors.lastname: Sorrentino
mesh_terms: D000818:Animals; D002417:Cattle; D003600:Cytosol / Q000201:enzymology*; D003603:Cytotoxins / Q000235:genetics* / Q000378:metabolism*; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008958:Models, Molecular; D011485:Protein Binding; D012259:Ribonuclease, Pancreatic / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D013053:Spectrophotometry
chemical_list: D003603:Cytotoxins; D004791:Enzyme Inhibitors; C046366:angiogenin; D012259:Ribonuclease, Pancreatic