Antitumor Activity of Ribonuclease Multimers Created by Site-Specific Covalent Tethering

Site-specific cross-linking can generate homogeneous multimeric proteins of defined valency. Pancreatic-type ribonucleases are an especially attractive target, as their natural dimers can enter mammalian cells, evade the cytosolic ribonuclease inhibitor (RI), and exert their toxic ribonucleolytic ac...

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Veröffentlicht in:	Bioconjugate chemistry 2010-09, Vol.21 (9), p.1691-1702
Hauptverfasser:	Rutkoski, Thomas J, Kink, John A, Strong, Laura E, Schilling, Christine I, Raines, Ronald T
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antineoplastic Agents - chemistry Antineoplastic Agents - pharmacology Antineoplastic Agents - toxicity Biochemistry Cattle Cell Proliferation - drug effects Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology Enzyme Inhibitors - toxicity Erlotinib Hydrochloride Humans Lung Neoplasms - metabolism Lung Neoplasms - pathology Male Mice Pancreas Prostatic Neoplasms - metabolism Prostatic Neoplasms - pathology Protein Binding - drug effects Proteins Quinazolines - chemistry Quinazolines - pharmacology Quinazolines - toxicity Ribonuclease, Pancreatic - antagonists & inhibitors Ribonuclease, Pancreatic - chemistry Ribonuclease, Pancreatic - metabolism Ribonucleases Ribonucleic acid RNA Rodents Sulfhydryl Compounds - chemistry Tumor Cells, Cultured
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