4.6.1.18	evolution	the enzyme belongs to the pancreatic-type secretory ribonuclease superfamily	729310	
4.6.1.18	evolution	the enzyme belongs to the pancreatic-type secretory ribonuclease superfamily as a unique natively dimeric member	729310	
4.6.1.18	evolution	the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview	729713	
4.6.1.18	evolution	the enzyme is a member of the pancreatic ribonuclease (RNase) superfamily	730422	
4.6.1.18	evolution	the enzyme is one of the key models in studies of evolutionary innovation and functional diversification, evolution and the function of Caniformia RNASE1 genes, phylogenetic analysis, overview. Four independent gene duplication events in the families of superfamily Musteloidea, including Procyonidae, Ailuridae, Mephitidae and Mustelidae	730952	
4.6.1.18	malfunction	mechanistic model for the denaturation of bovine pancreatic ribonuclease A in urea, a direct interaction between urea and protonated histidine as the initial step for protein inactivation followed by hydrogen bond formation with polar residues, and the breaking of hydrophobic collapse as the final steps for protein denaturation	707508	
4.6.1.18	malfunction	RNase A tandem enzymes, in which two RNase A molecules are artificially connected by a peptide linker, and thus have a pseudodimeric structure, exhibit remarkable cytotoxic activity, but can be inhibited by the cytosolic ribonuclease inhibitor in vitro. Structure modeling, overview	717596	
4.6.1.18	metabolism	the enzyme lacks cytotoxic activity as it is inactivated by intracellular cytosolic ribonuclease inhibitor	750772	
4.6.1.18	additional information	analysis of synthesis and maturation, folding, quality control, and secretion, of pancreatic RNase in the endoplasmic reticulum of live cells, overview. Human RNase folds rapidly and is secreted mainly in glycosylated forms	717861	
4.6.1.18	additional information	analysis of synthesis and maturation, folding, quality control, and secretion, of pancreatic RNase in the endoplasmic reticulum of live cells, overview. In contrast to the slow in vitro refolding, the protein folds almost instantly after translation and translocation into the endoplasmatic reticulum lumen. Despite high stability of the native protein, only about half of the RNase reaches a secretion competent, monomeric form and is rapidly transported from the rough endoplasmic reticulum via the Golgi complex to the extracellular space	717861