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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Interactions of the cytotoxic RNase A dimers with the cytosolic ribonuclease inhibitor

GOTTE, Giovanni;
2005-01-01

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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
2005
ribonuclease A; protein dimerization; domain swapping; ribonuclease cytotoxicity; ribonuclease inhibitor; antitumor activity
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11562/230392
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