Please use this identifier to cite or link to this item: https://doi.org/10.1039/b513935j
Title: Protein and small molecule microarrays: Powerful tools for high-throughput proteomics
Authors: Uttamchandani, M. 
Wang, J.
Yao, S.Q. 
Issue Date: 2006
Citation: Uttamchandani, M., Wang, J., Yao, S.Q. (2006). Protein and small molecule microarrays: Powerful tools for high-throughput proteomics. Molecular BioSystems 2 (1) : 58-68. ScholarBank@NUS Repository. https://doi.org/10.1039/b513935j
Abstract: Advances in genomics and proteomics have opened up new possibilities for the rapid functional assignment and global characterization of proteins. Large-scale studies have accelerated this effort by using tools and strategies that enable highly parallel analysis of huge repertoires of biomolecules. Organized assortments of molecules on arrays have furnished a robust platform for rapid screening, lead discovery and molecular characterization. The essential advantage of microarray technology is attributed to the massive throughput attainable, coupled with a highly miniaturized platform - potentially driving discovery both as an analytical and diagnostic tool. The scope of microarrays has in recent years expanded impressively. Virtually every biological component - from diverse small molecules and macromolecules (such as DNA and proteins) to entire living cells - has been harnessed on microarrays in attempts to dissect the bewildering complexity of life. Herein we highlight strategies that address challenges in proteomics using microarrays of immobilized proteins and small molecules. Of specific interest are the techniques involved in stably immobilizing proteins and chemical libraries on slide surfaces as well as novel strategies developed to profile activities of proteins on arrays. As a rapidly maturing technology, microarrays pave the way forward in high-throughput proteomic exploration. © The Royal Society of Chemistry 2006.
Source Title: Molecular BioSystems
URI: http://scholarbank.nus.edu.sg/handle/10635/77634
ISSN: 1742206X
DOI: 10.1039/b513935j
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