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Authors = Rosa Terracciano

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Open AccessReview The Proteomics Big Challenge for Biomarkers and New Drug-Targets Discovery
Int. J. Mol. Sci. 2012, 13(11), 13926-13948; doi:10.3390/ijms131113926
Received: 24 September 2012 / Revised: 17 October 2012 / Accepted: 25 October 2012 / Published: 29 October 2012
Cited by 22 | Viewed by 2921 | PDF Full-text (877 KB) | HTML Full-text | XML Full-text
Abstract
In the modern process of drug discovery, clinical, functional and chemical proteomics can converge and integrate synergies. Functional proteomics explores and elucidates the components of pathways and their interactions which, when deregulated, lead to a disease condition. This knowledge allows the design of
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In the modern process of drug discovery, clinical, functional and chemical proteomics can converge and integrate synergies. Functional proteomics explores and elucidates the components of pathways and their interactions which, when deregulated, lead to a disease condition. This knowledge allows the design of strategies to target multiple pathways with combinations of pathway-specific drugs, which might increase chances of success and reduce the occurrence of drug resistance. Chemical proteomics, by analyzing the drug interactome, strongly contributes to accelerate the process of new druggable targets discovery. In the research area of clinical proteomics, proteome and peptidome mass spectrometry-profiling of human bodily fluid (plasma, serum, urine and so on), as well as of tissue and of cells, represents a promising tool for novel biomarker and eventually new druggable targets discovery. In the present review we provide a survey of current strategies of functional, chemical and clinical proteomics. Major issues will be presented for proteomic technologies used for the discovery of biomarkers for early disease diagnosis and identification of new drug targets. Full article
(This article belongs to the collection Advances in Proteomic Research)
Open AccessReview In Mesopore Protein Digestion: A New Forthcoming Strategy in Proteomics
Molecules 2011, 16(7), 5938-5962; doi:10.3390/molecules16075938
Received: 2 June 2011 / Revised: 7 July 2011 / Accepted: 13 July 2011 / Published: 15 July 2011
Cited by 16 | Viewed by 3501 | PDF Full-text (756 KB)
Abstract
The conventional protocols for in solution or in gel protein digestion require many steps and long reaction times. The use of trypsin immobilized onto solid supports has recently captured the attention of many research groups, because these systems can speed-up protein digestion significantly.
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The conventional protocols for in solution or in gel protein digestion require many steps and long reaction times. The use of trypsin immobilized onto solid supports has recently captured the attention of many research groups, because these systems can speed-up protein digestion significantly. The utilization of new materials such as mesoporous silica as supports, in which enzyme and substrate are dramatically concentrated and confined in the nanospace, offers new opportunities to reduce the complexity of proteomics workflows. An overview of the procedures for in situ proteolysis of single proteins or complex protein mixtures is reported, with a special focus on porous materials used as catalysts. The challenging efforts for designing such systems aimed at mimicking the biochemistry of living cells are reviewed. Potentials, limitations and challenges of this branch of enzyme catalysis, which we indicate as in mesopore digestion, are discussed, in relation to its suitability for high-speed and high-throughput proteomics. Full article
(This article belongs to the Special Issue Catalytic Asymmetric Synthesis)

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