AbstractRibonuclease 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
AbstractMany ribonucleases (RNases) are highly cytotoxic. In some cases, they attack selectively mal...
8 pags, 3 pagsProtein aggregation via 3D domain swapping is a complex mechanism which can lead to th...
Dimeric proteins can arise by the swapping of structural domains between monomers. The prevalence of...
Ribonuclease A (RNase A) dimers have been recently found to be endowed with some of the special, i.e...
AbstractRibonuclease A (RNase A) dimers have been recently found to be endowed with some of the spec...
AbstractProtein aggregation via 3D domain swapping is a complex mechanism which can lead to the acqu...
Dimers, trimers, and tetramers of bovine ribonuclease A, obtained by lyophilization of the enzyme fr...
A growing number of pancreatic-type ribonucleases (RNases) present cytotoxic activity against malign...
The ability to retain ribonucleolytic activity in the presence of the ribonuclease inhibitor (RI) is...
"Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound...
Pancreatic ribonucleases, thanks to their ability to degrade RNA, represent potential antitumor ther...
Ribonucleases (RNases) are a large number of enzymes gathered into different bacterial or eukaryotic...
Cytosolic RNase inhibitor binds to and neutralizes most members of the pancreatic type RNase superfa...
"Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound...
The cytotoxic action of some ribonucleases homologous to bovine pancreatic RNase A, the superfamily ...
AbstractMany ribonucleases (RNases) are highly cytotoxic. In some cases, they attack selectively mal...
8 pags, 3 pagsProtein aggregation via 3D domain swapping is a complex mechanism which can lead to th...
Dimeric proteins can arise by the swapping of structural domains between monomers. The prevalence of...
Ribonuclease A (RNase A) dimers have been recently found to be endowed with some of the special, i.e...
AbstractRibonuclease A (RNase A) dimers have been recently found to be endowed with some of the spec...
AbstractProtein aggregation via 3D domain swapping is a complex mechanism which can lead to the acqu...
Dimers, trimers, and tetramers of bovine ribonuclease A, obtained by lyophilization of the enzyme fr...
A growing number of pancreatic-type ribonucleases (RNases) present cytotoxic activity against malign...
The ability to retain ribonucleolytic activity in the presence of the ribonuclease inhibitor (RI) is...
"Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound...
Pancreatic ribonucleases, thanks to their ability to degrade RNA, represent potential antitumor ther...
Ribonucleases (RNases) are a large number of enzymes gathered into different bacterial or eukaryotic...
Cytosolic RNase inhibitor binds to and neutralizes most members of the pancreatic type RNase superfa...
"Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound...
The cytotoxic action of some ribonucleases homologous to bovine pancreatic RNase A, the superfamily ...
AbstractMany ribonucleases (RNases) are highly cytotoxic. In some cases, they attack selectively mal...
8 pags, 3 pagsProtein aggregation via 3D domain swapping is a complex mechanism which can lead to th...
Dimeric proteins can arise by the swapping of structural domains between monomers. The prevalence of...