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Cellzome publishes novel approach for the systematic use of protein interaction maps in drug discovery in Nature

HEIDELBERG, Germany, January 10, 2002 Cellzome AG today announced the publication of a pioneering study in the proteomics field in the January 10 issue of the journal Nature describing the first draft of a functional map of the yeast proteome. The map visualizes an entire network of protein complexes and their interactions in yeast Saccharomyces cerevisae, forming a basis for the operative organization underlying a cells activity under different conditions, thereby making the map a first of its kind.

These maps will enable researchers to more fully assess the roles of individual proteins in biology and provide for a more comprehensive approach in choosing targets for drug discovery, said Dr. Giulio Superti-Furga, Vice President, Biology, of Cellzome. By knowing the molecular context in which targets act, investigators can better predict the effect of drug candidates on the parameters that influence safety and efficacy, while protein interaction maps provide the framework on which to add data mined from the literature and from other experimental approaches. Taken together, this information can be used to improve the efficiency of the drug discovery process.

The paper entitled Functional Organization of the Yeast Proteome by Systematic Analysis of Protein Complexes, appears on the cover of Nature (vol. 415), and portrays a functional proteomic map for the yeast Saccharomyces cerevisiae, a commonly used eukaryotic model in pharmaceutical development. The map characterizes the function and interactions of 1,440 yeast proteins comprising 232 multi-protein assemblies, or complexes, which directly affect biological activity. An interdisciplinary team at Cellzome used a proprietary protein complex assembly and retrieval technology that was originally developed at the European Molecular Biology Laboratory (EMBL) to isolate multi-protein assemblies directly from cells under near physiological conditions.

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Noonan/Russo Communications
9-Jan-2002


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