{"title":"COFRADIC™: the Hubble telescope of proteomics","authors":"Kris Gevaert, Joël Vandekerckhove","doi":"10.1016/S1741-8372(04)02416-8","DOIUrl":"10.1016/S1741-8372(04)02416-8","url":null,"abstract":"<div><p>COFRADIC™ is a diagonal chromatographic technique designed to select peptides from complex mixtures. It consists of two consecutive identical chromatographic separations, with a modification step targeted to a subset of peptides between the two separations. The modified peptides obtain different chromatographic properties and segregate from the bulk of unaltered peptides in the second run. The final analysis is limited to the sorted peptides, thereby reducing the complexity but keeping all of the characteristics of the proteome.</p></div>","PeriodicalId":100382,"journal":{"name":"Drug Discovery Today: TARGETS","volume":"3 2","pages":"Pages 16-22"},"PeriodicalIF":0.0,"publicationDate":"2004-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1741-8372(04)02416-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90688195","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Translational genomics: safeguarding patient privacy and harnessing the genomic revolution in medicine","authors":"Ashok R Amin","doi":"10.1016/S1741-8372(04)02407-7","DOIUrl":"10.1016/S1741-8372(04)02407-7","url":null,"abstract":"","PeriodicalId":100382,"journal":{"name":"Drug Discovery Today: TARGETS","volume":"3 2","pages":"Pages 43-45"},"PeriodicalIF":0.0,"publicationDate":"2004-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1741-8372(04)02407-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72642228","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Moonlighting proteins: complications and implications for proteomics research","authors":"Constance J. Jeffery","doi":"10.1016/S1741-8372(04)02405-3","DOIUrl":"10.1016/S1741-8372(04)02405-3","url":null,"abstract":"<div><p><span><span>Proteomics projects involving biochemical, genetic and computational methods are being used to elucidate the functions of thousands of proteins in healthy and disease states. The results provide valuable information both for understanding basic </span>physiological processes<span><span> and for the development of novel therapeutics. However, the ability of a protein to moonlight, or to have more than one function, can complicate the interpretation and application of the results from these proteomics studies. This review provides examples of how moonlighting proteins can affect the results of proteomics projects being used to determine protein function based on patterns of </span>protein expression, protein–protein interactions, analysis of </span></span>protein sequences and structures, and other methods.</p></div>","PeriodicalId":100382,"journal":{"name":"Drug Discovery Today: TARGETS","volume":"3 2","pages":"Pages 71-78"},"PeriodicalIF":0.0,"publicationDate":"2004-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1741-8372(04)02405-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89543790","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Factors that contribute to the complexity of protein digests","authors":"Éva Hunyadi-Gulyás , Katalin F. Medzihradszky","doi":"10.1016/S1741-8372(04)02415-6","DOIUrl":"10.1016/S1741-8372(04)02415-6","url":null,"abstract":"<div><p>High-throughput proteomics<span> is one of the most dynamically developing research areas. Frequently, the whole protein content of a cell is digested, fractionated and analyzed in a completely automated way, including data analysis. Not only are proteins identified this way, but quantitative studies are also performed, and posttranslational modifications and covalently labeled derivatives are identified. Because the presence of unexpected and/or unconsidered contaminants or covalently modified peptides can lead to data misinterpretation in such an environment, it is mandatory that we attempt to identify, understand and evaluate the factors that can contribute to the complexity of protein digest mixtures.</span></p></div>","PeriodicalId":100382,"journal":{"name":"Drug Discovery Today: TARGETS","volume":"3 2","pages":"Pages 3-10"},"PeriodicalIF":0.0,"publicationDate":"2004-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1741-8372(04)02415-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91221250","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Quality analysis and integration of large-scale molecular data sets","authors":"Lars J. Jensen, Peer Bork","doi":"10.1016/S1741-8372(04)02408-9","DOIUrl":"10.1016/S1741-8372(04)02408-9","url":null,"abstract":"<div><p>One of the major challenges in bioinformatics today is to integrate and interpret the heterogeneous biological data that are being produced at an ever increasing pace. As this type of analysis is still in its infancy, all studies so far have relied on applying simple rule-based criteria on only a small subset of the available data. To enable comprehensive studies to be undertaken with a statistical framework, standardized repositories from which all datasets can be easily obtained and benchmarks that quantify the often high error rates of large-scale datasets are needed. Quality control, benchmark and integration efforts from protein interaction networks in the context of genome and transcriptome data are reviewed.</p></div>","PeriodicalId":100382,"journal":{"name":"Drug Discovery Today: TARGETS","volume":"3 2","pages":"Pages 51-56"},"PeriodicalIF":0.0,"publicationDate":"2004-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1741-8372(04)02408-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75709702","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Q TRAP™ mass spectrometer technology for proteomics applications","authors":"James W. Hager","doi":"10.1016/S1741-8372(04)02421-1","DOIUrl":"10.1016/S1741-8372(04)02421-1","url":null,"abstract":"<div><p><span>Mass spectrometry (MS) can play an important part in the characterization of protein posttranslational modifications. The specificity of triple-quadrupole scan modes combined with the sensitivity of the linear ion-trap operational modes in Q TRAP™ MS instruments presents new opportunities for automated investigation of posttranslational modifications in biological samples. The triple-quadrupole precursor ion and constant neutral loss scans are very powerful for identifying peptides that have been posttranslationally modified. In addition, the ion-trap product ion scans can provide valuable information for </span>amino acid sequence determination and sites of modification.</p></div>","PeriodicalId":100382,"journal":{"name":"Drug Discovery Today: TARGETS","volume":"3 2","pages":"Pages 31-36"},"PeriodicalIF":0.0,"publicationDate":"2004-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1741-8372(04)02421-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72942039","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Targets for Alzheimer's disease: lessons learnt from flies","authors":"M. Konsolaki, D. Cohen","doi":"10.1016/S1741-8372(04)02395-3","DOIUrl":"10.1016/S1741-8372(04)02395-3","url":null,"abstract":"<div><p><span>Neurodegenerative diseases, including </span>Alzheimer's disease (AD), are a major focus of the pharmaceutical industry. Recently, human genetic analyses have aided in the successful identification of a handful of genes responsible for genetically inherited forms of AD, but our understanding of basic mechanisms that lead to the more common sporadic forms of this disease is still limited.</p></div>","PeriodicalId":100382,"journal":{"name":"Drug Discovery Today: TARGETS","volume":"3 2","pages":"Pages 64-70"},"PeriodicalIF":0.0,"publicationDate":"2004-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1741-8372(04)02395-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81195196","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"New genetic strategies for protein discovery based on whole-genome sequences","authors":"Michael J. DeVit , Trey Powers","doi":"10.1016/S1741-8372(04)02403-X","DOIUrl":"10.1016/S1741-8372(04)02403-X","url":null,"abstract":"<div><p>Determining the genomic sequences of the most commonly used model organisms has led to a new era in genetic studies. Each predicted gene of a sequenced organism can now be inactivated to create collections of all possible loss-of-function mutants. Whole-genome mutant collections are now available for the yeast <span><em>Saccharomyces cerevisiae</em><em>,</em></span> and reagents are available to inactivate every gene in the roundworm <span><em>Caenorhabditis elegans</em></span>. This article describes how these collections have stimulated the development of novel genetic screening methods that have accelerated the pace of genetic research.</p></div>","PeriodicalId":100382,"journal":{"name":"Drug Discovery Today: TARGETS","volume":"3 2","pages":"Pages 57-63"},"PeriodicalIF":0.0,"publicationDate":"2004-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1741-8372(04)02403-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86050996","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}