Sandbox Reserved 199: Difference between revisions
From Proteopedia
Jump to navigationJump to search
/* Solution Structure and Dynamics of Human Pancreatic Ribonuclease<ref>PMID: 18495155</ref><ref> Rico, M. "The Solution Structure and Dynamics of Human Pancreatic Ribonuclease Determined by NMR Spectroscopy Provide Insight into Its Remarkable Biolog |
|||
| Line 44: | Line 44: | ||
Ribonucleases show specific toxicity to tumor cells. In fact, Onconase ® (an RNase A homolog from the [http://en.wikipedia.org/wiki/Northern_Leopard_Frog Northern Leopard Frog]) is currently in phase IIIb clinical trials for the treatment of malignant mesothelioma. However, due to possible immunogenicity of the frog enzyme, much effort has been focused on developing a cytotoxic human RNase, which evades inhibition by human ribonuclease inhibitor (HRI). HRI selectively binds to human pancreatic RNase (RNase 1) and impedes its enzymatic activity. Correctly characterizing the structure and binding specificity of RNase via NMR could assist in the development of RNase-based anti-cancer treatments. | Ribonucleases show specific toxicity to tumor cells. In fact, Onconase ® (an RNase A homolog from the [http://en.wikipedia.org/wiki/Northern_Leopard_Frog Northern Leopard Frog]) is currently in phase IIIb clinical trials for the treatment of malignant mesothelioma. However, due to possible immunogenicity of the frog enzyme, much effort has been focused on developing a cytotoxic human RNase, which evades inhibition by human ribonuclease inhibitor (HRI). HRI selectively binds to human pancreatic RNase (RNase 1) and impedes its enzymatic activity. Correctly characterizing the structure and binding specificity of RNase via NMR could assist in the development of RNase-based anti-cancer treatments. | ||
==NMR Study of Ribonuclease Folding Dynamics<ref> | ==NMR Study of Ribonuclease Folding Dynamics<ref>PMID: 2845278 </ref>== | ||
===Experimental Procedure=== | ===Experimental Procedure=== | ||
