The crystal structure of the domain-swapped dimer of onconase highlights some catalytic and antitumor activity features of the enzyme-Reference-Cited by-同舟云学术

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The crystal structure of the domain-swapped dimer of onconase highlights some catalytic and antitumor activity features of the enzyme

Published:2021-11 Issue: Volume:191 Page:560-571
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Gotte Giovanni,Campagnari Rachele,Loreto Domenico,Bettin Ilaria,Calzetti Federica,Menegazzi Marta,Merlino Antonello

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference74 articles.

1. Amino acid sequence of an anti-tumor protein from Rana pipiens oocytes and early embryos. Homology to pancreatic ribonucleases;Ardelt;J. Biol. Chem.,1991

2. Human pancreatic-type and nonpancreatic-type ribonucleases: a direct side-by-side comparison of their catalytic properties;Sorrentino;Arch. Biochem. Biophys.,1994

3. Refined 1.7 a X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity;Mosimann;J. Mol. Biol.,1994

4. Interaction of onconase with the human ribonuclease inhibitor protein;Turcotte;Biochem. Biophys. Res. Commun.,2008

5. Evasion of ribonuclease inhibitor as a determinant of ribonuclease cytotoxicity;Rutkoski;Curr. Pharm. Biotechnol.,2008

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