Biochemical and Biophysical Research Communications. 2008 Dec 12;377(2):512-4. Epub 2008 Oct 16. [Link] Turcotte RF, Raines RT. Medical Scientist Training Program and Biophysics Graduate Program, University of Wisconsin-Madison, Madison, WI 53706, USA. Abstract One of the tightest known protein–protein interactions in biology is that between members of the ribonuclease A superfamily and the ribonuclease inhibitor…

Read More

Cell Cycle. 2008 Oct;7(20):3258-61. Epub 2008 Oct 25. [Link] Zhao H, Ardelt B, Ardelt W, Shogen K, Darzynkiewicz Z. Department of Pathology, Brander Cancer Research Institute, New York Medical College, Valhalla, New York 10595, USA. Abstract Onconase (Onc), a ribonuclease from oocytes of Northern Leopard frogs (Rana pipiens) is cytostatic and cytotoxic to a variety…

Read More

Current Pharmaceutical Biotechnology. 2008 Jun;9(3):185-9. Link Rutkoski TJ, Raines RT. Department of Biochemistry, University of Wisconsin-Madison, 433 Babcock Drive, Madison, WI 53706 1544, USA. Abstract Onconase® (ONC) is an amphibian member of the bovine pancreatic ribonuclease (RNase A) superfamily that exhibits innate antitumoral activity. ONC has been granted both orphan-drug and fast-track status by the…

Read More

Current Pharmaceutical Biotechnology. 2008 Jun;9(3):215-25. Link Ardelt W, Shogen K, Darzynkiewicz Z. Alfacell Corporation, 300 Atrium Drive, Somerset, NJ 08873, USA. wardelt@alfacell.com Abstract Rana pipiens oocytes contain two homologues of pancreatic ribonuclease A that are cytostatic and cytotoxic to human cancer cells. Extensively studied Onconase is in advanced Phase IIIb clinical trials against malignant mesothelioma,…

Read More

Current Pharmaceutical Biotechnology. 2008 Jun;9(3):226-30. Link Rybak SM. Bionanomics, LLC, 411 Walnut Street, Green Cove Springs, FL 32043, USA. rybak@mindspring.com Abstract Onconase, a member of the pancreatic ribonuclease A superfamily, is currently in Phase III clinical trials for treatment of unresectable malignant mesothelioma. The anticancer effect of onconase may relate to its intracellular target, a…

Read More

Current Pharmaceutical Biotechnology. 2008 Jun;9(3):231-4. Link Krauss J, Arndt MA, Dübel S, Rybak SM. Natinal center for tumor diseases (NCT), Universit6y of Heidelberg, Im Neuenheimer Fild 350, D-69120 Heidleberg, Germany. juergen.krauss@med.uni-heidelberg.de Abstract Ribonucleases (RNases) of the superfamily A exhibit potent antineoplastic activity yet do not mediate appreciable immunogenicity or non-specific toxicity in both animal models…

Read More

Molecular Cancer Therapeutics. 2008 Jul 7. [Epub ahead of print] [Link] Ramos-Nino ME, Littenberg B. Departments of Pathology and Medicine and Nursing, University of Vermont, Burlington, Vermont. Abstract Accumulating evidence supports the idea that two known phosphatidylinositol 3′-kinase (PI3K) downstream proteins, Fra-1 and Survivin, are potential targets for cancer therapy. Increased expression of Fra-1, a…

Read More

Expert Opinion on Biological Therapy. 2008 Jun;8(6):813-27. [Link] Assaly M, Bongiovanni M, Kumar N, Egger JF, Pelte MF, Genevay M, Finci V, Tschanz E, Pache JC. Department of Pathology, Geneva University Hospital, Geneva, Switzerland. Abstract Background: Ranpirnase, a cytotoxic amphibian ribonuclease, is effective against cancer cells, inducing apoptosis independently of p53 protein. Onconase® (the smallest…

Read More

Cancer Biology & Therapy. 2008 Apr 19;7(7) [Epub ahead of print] [Link] Ita M, Halicka HD, Tanaka T, Kurose A, Ardelt B, Shogen K, Darzynkiewicz Z. Brander Cancer Research Institute and Department of Pathology, New York Medical College, Valhalla, NY, 10595; Ita Dental Clinic, Kama-city, Fukuoka 820-0501, Japan. Abstract Onconase (Onc), a ribonuclease from oocytes…

Read More