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  • 1
    Online Resource
    Online Resource
    Dordrecht :Springer Netherlands,
    Keywords: Proteins -- Analysis -- Data processing -- Congresses. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (285 pages)
    Edition: 1st ed.
    ISBN: 9789401792028
    Series Statement: Translational Bioinformatics Series ; v.6
    DDC: 572.6
    Language: English
    Note: Intro -- Preface -- Contents -- Chapter 1: Introduction to Genomics and Proteomics for Clinical Discovery and Development -- 1.1 1.1 Genomics and Proteomics for Clinical Discovery and Development -- 1.2 1.2 The ENCODE Project -- 1.3 1.3 HPP - The Human Proteome Project -- 1.4 1.4 Personalized Medicine -- 1.5 1.5 Biobanking -- References -- Chapter 2: Identification of Missing Proteins: Toward the Completion of Human Proteome -- 2.1 Introduction -- 2.2 Current State of Human Protein Project -- 2.3 Methods for Identification -- 2.4 Databases -- 2.5 Application of Selected Reaction Monitoring Mass Spectrometry -- 2.6 Conclusions -- References -- Chapter 3: Chromosome Transcriptome Profiling in the Context of High-Throughput Proteomics Studies -- 3.1 Introduction -- 3.2 Bioinformatics Methods in Proteogenomics -- 3.2.1 Databases for Annotation of Genes and Proteins -- 3.2.2 Analysis of Whole Transcriptome Experiments -- 3.2.2.1 Microarray Data Analysis -- 3.2.2.2 Next-Generation Sequencing Data Analysis -- 3.2.3 Analysis of Whole Proteome Experiments -- 3.3 Chromosome Transcriptome Profiling Oriented Towards Proteome Research -- 3.3.1 C-HPP Genome Annotation -- 3.3.2 Whole Transcriptome Profiling Using Microarrays -- 3.3.3 Extension of the Chromosome Transcriptome Profiling with RNA-Seq Data -- 3.3.3.1 Tissue Specific Expression of Human Genes -- 3.3.3.2 In-Depth Analysis of Missing Proteins -- 3.4 Summary -- References -- Chapter 4: Standards for Proteomics Data Dissemination and Experiments Reporting -- 4.1 Background: Basic Principles -- 4.2 Data Standards: HUPO-PSI-XML, MIAPEs and CVS -- 4.2.1 Reporting Guidelines: Minimal Information About a Proteomic Experiment (MIAPE Documents) -- 4.2.2 The Extensible Markup Language (XML) to Standardize Proteomics Data Storage -- 4.2.3 Controlled Vocabularies. , 4.3 Repositories for Proteomics and Biological Data -- 4.3.1 MS-Based Data: ProteomeXchange Consortium -- 4.3.1.1 PRIDE ( http://www.ebi.ac.uk/pride/) -- 4.3.1.2 PeptideAtlas ( http://www.peptideatlas.org/) -- 4.3.1.3 Global Protein Machine Database - GPM/gpmDB ( ­http://www.thegpm.org/) -- 4.3.2 Proteomics Data Submission to Public Repositories -- 4.3.3 Proteomics Related Data: Human Resources -- 4.3.3.1 Universal Protein Resource Knowledge Base, UniProtKB ( http://www.uniprot.org/) -- 4.3.3.2 National Center for Biotechnology Information, NCBI ( http://www.ncbi.nlm.nih.gov) -- 4.3.3.3 A Knowledge Platform for Human Proteins: neXtprot ( http://www.nextprot.org/) -- 4.3.3.4 The Human Protein Atlas ( http://www.proteinatlas.org/) -- 4.3.3.5 The Human Protein Reference Database HPRD ( http://www.hprd.org/) -- 4.4 Tools for Automatic Data Retrieving -- 4.4.1 Genomics and Transcriptomic Data: Babelomics, GeneCodis -- 4.4.2 Genomics and Proteomics Enrichment: DAVID -- 4.4.3 Proteomics Data Integration: PIKE -- 4.5 Example Using PIKE -- 4.5.1 How to Start? -- 4.5.2 Entering Your Query -- 4.5.3 Showing the Results -- 4.5.4 Poring Over the Data -- 4.5.5 Integrating the Results -- 4.6 Conclusions -- References -- Chapter 5: Mass Spectrometry-Based Protein Sequencing Platforms -- 5.1 Introduction -- 5.2 MS-Based Sequencing of Polypeptides -- 5.2.1 Collision-Induced Dissociation (CID) (Paizs and Suhai 2005) -- 5.2.1.1 Charge-Directed Fragmentation Pathways -- 5.2.1.2 Charge-Remote Fragmentations -- 5.2.2 Electron-Transfer Dissociation (ETD) -- 5.2.2.1 Direct Dissociation-Like Cleavage of N-C α Bond -- 5.2.2.2 Decision Tree (DT)-Driven Shotgun Sequencing -- 5.2.2.3 Peptide Sequencing by Dual Fragmentation (Frese et al. 2012) -- 5.3 LC/MS-Based Shotgun Cancer Proteomics -- 5.3.1 Proteolysis Prior to Sequencing Proteins. , 5.3.2 Sample Preparations of Clinical Specimens -- 5.3.2.1 Plasma Samples -- 5.3.2.2 FFPE Tissue Specimens -- 5.3.3 Differential Protein Expression Analysis -- 5.4 Bioinformatics for Sequence Identification -- 5.4.1 Database Search Approach -- 5.4.2 Spectral-Library Matching Approach (Tharakan et al. 2010 -- Ning et al. 2010 -- Ahrne et al. 2009) -- 5.4.3 De novo Spectrum Sequencing (Seidler et al. 2010 -- Frank et al. 2007 -- Pan et al. 2010 -- Frank and Pevzner 2005 -- Ma et al. 2003 -- Tanner et al. 2005 -- Dasari et al. 2010) -- 5.4.4 Sequence-Tag/Hybrid Approaches -- 5.4.5 Statistical Confidence on Peptide Identification -- 5.4.5.1 False Discovery Rate (FDR) -- 5.4.5.2 Machine Learning Methods -- 5.4.6 Protein Inference Problem (Nesvizhskii and Aebersold 2005 -- Nesvizhskii 2010 -- Li and Radivojac 2012) -- 5.5 Perspectives -- References -- Chapter 6: Post-translational Modifications in the Human Proteome -- 6.1 Introduction -- 6.2 Protein Acetylation -- 6.3 Protein Phosphorylation -- 6.4 Protein Glycosylation -- 6.5 Protein Ubiquitination -- 6.6 Lipid Modifications of Proteins -- 6.7 Inference of PTMs from MS Data -- 6.8 Summary -- References -- Chapter 7: Biomarker Discovery Utilizing Biobanking Archives and the Diagnostic Market -- 7.1 7.1 Introduction -- 7.2 7.2 Biomarkers and Diagnostics -- 7.3 7.3 Clinical Diagnostics and Treatment for Research -- 7.4 7.4 Biobanking -- 7.5 7.5 Biomarker Discovery -- References -- Chapter 8: Protein Microarrays: Overview, Applications and Challenges -- 8.1 Introduction -- 8.2 Protein Microarrays -- 8.3 Array Format -- 8.3.1 Planar Array -- 8.3.1.1 Array Chemistries -- 8.3.1.2 Array Printing -- 8.3.1.3 Assay Execution -- 8.3.1.4 Assay Detection -- 8.3.2 Beads Arrays -- 8.4 Content -- 8.4.1 Assembled Arrays -- 8.4.1.1 Antibody Arrays -- Assembled Array Signal Detection -- 8.4.2 Reverse-Phase Arrays. , 8.4.3 Self-Assembled Protein Microarrays -- 8.4.3.1 In Situ Protein Expression Systems -- 8.5 Types of  In Situ Protein Arrays -- 8.5.1 PISA -- 8.5.2 DAPA -- 8.5.3 PuCA -- 8.5.4 NAPPA -- 8.6 Applications of NAPPA Arrays -- 8.6.1 NAPPA Arrays for Vaccine Development -- 8.6.2 NAPPA for Protein-Protein Interaction -- 8.6.3 NAPPA Arrays for Detecting Autoimmune Response -- 8.7 Conclusions and Future Directions -- References -- Chapter 9: Clinical Bioinformatics: A New Emerging Science of Biomarker Development -- 9.1 Introduction -- 9.2 Significance of Clinical Bioinformatics -- 9.3 Introduction of Systems Clinical Medicine -- 9.4 Biomarkers, Network Biomarkers, and Dynamic Network Biomarkers -- 9.5 Applied Methodologies -- 9.6 Development and Application of DESS -- References -- Chapter 10: Rapid Advances in the Field of Epigenetics -- 10.1 Epigenetic Regulation -- 10.1.1 What Is Epigenome? -- 10.1.2 X-Inactivation and Genomic Imprinting -- 10.1.3 Structure of Chromatin and Epigenetic Modification -- 10.1.4 DNA Modification -- 10.1.5 Histone Modification and Variants -- 10.1.6 RNA -- 10.1.7 Polycomb and Trithorax -- 10.1.8 Xist and Heterochromatin Formation -- 10.1.9 Reprogramming -- 10.1.10 Cell Division -- 10.1.11 Retrotransposon -- 10.1.12 None-Histone Target of Epigenetic Enzyme -- 10.1.13 Vitamin -- 10.1.14 Infection -- 10.2 Approach for Epigenetic Analysis -- 10.2.1 Introduction -- 10.2.2 Epigenetic Regulators as Drug Targets -- 10.2.3 Epigenome Associated Protein Complex as Drug Target -- 10.2.4 Development of Epigenetic Regulator Inhibitor -- 10.2.5 Analysis with Next Generation DNA Sequencer (NGS) -- 10.2.6 Analysis with Mass Spectrometry -- 10.2.6.1 Chemistry of Histone -- 10.2.6.2 Sample Preparation -- 10.2.6.3 High Performance Liquid Chromatography (HPLC) -- 10.2.6.4 Mass Spectrometry (MS) -- 10.2.6.5 Tandem Mass Spectrometry (MS/MS). , 10.2.6.6 Database Search -- 10.2.6.7 Quantification -- 10.2.6.8 Analysis of Histone H4 and H3 Tails -- 10.2.6.9 Perspective -- 10.2.7 Summary -- References -- Chapter 11: Pharmacogenomics in Drug Development -- 11.1 Introduction -- 11.2 Determinants of Drug Disposition -- 11.3 Drug Metabolizing Phase I Enzymes and Polymorphism -- 11.3.1 CYP2D6 -- 11.3.2 CYP2C19 -- 11.3.3 CYP2C9 -- 11.4 Drug Metabolizing Phase II Enzymes and Polymorphism -- 11.5 Drug Transporters and Polymorphism -- 11.5.1 OATP1B1 -- 11.6 Pharmacogenomics in Drug Development -- 11.7 Concluding Remarks and Future Perspectives -- References -- Chapter 12: The Role of Proteomics in the Development of Personalized Medicine, Diagnostic Methods and Large Scale Biobanking -- 12.1 12.1 Introduction -- 12.2 12.2 Biobanking - Regulatory Aspects -- 12.3 12.3 Patient Donors and Sample Integrity -- 12.4 12.4 Proteomics in Clinical Diagnostics - Analytical Aspects -- 12.5 12.5 Concluding Remarks -- References -- Chapter 13: Imaging Techniques in Proteomics Research -- 13.1 Introduction -- 13.2 Mass Spectrometry Imaging (MSI) -- 13.3 Matrix-Assisted Laser Desorption Ionization (MALDI)-MSI -- 13.4 Secondary Ion Mass Spectrometry (SIMS) Imaging -- 13.5 Desorption Electro Spray Ionization (DESI) Imaging -- 13.6 Rapid Evaporative Ionization Mass Spectrometry (REIMS) Imaging -- 13.7 Targets in MSI -- 13.7.1 MSI of Peptides and Proteins -- 13.7.2 MSI of Lipids -- 13.7.3 MSI of Pharmaceuticals -- 13.7.4 MSI of Neurotransmitters and Endogenous Metabolites -- 13.7.5 MSI of Inorganic Ions -- 13.8 MSI Data Analysis Software -- 13.8.1 Open MSI -- 13.9 Conclusion and Future Perspectives -- References -- Index.
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Analytical chemistry 56 (1984), S. 2066-2069 
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1612-1112
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 0006-3592
    Keywords: biosensor ; ethanol ; fermentation ; lignocellulose hydrolysate ; liquid chromatography ; microdialysis ; on-line ; sampling ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: During a 70-h fermentation of a lignocellulose hydrolysate, the ethanol produced was monitored on-line using a microdialysis probe as an in situ sampling device. The dialysate components were then separated in a column liquid chromatographic system and the ethanol was selectively detected by an amperometric alcohol biosensor. The result was compared with two off-line analysis methods: one chromatographic method with refractive index (RI) detection and one enzymatic method based on spectrophotometric detection. The two methods base on enzymes were shown to give lower values than the chromatographic method based on RI detection, which is discussed n terms of selectivity. The investigated on-line setup was found to be a flexible system for monitoring of fermentations, allowing a sampling frequency of at least 12 h-1 and with a delay between sampling and detection of less than 5 min. © 1994 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1040-0397
    Keywords: Amperometry ; Composite electrode ; Tyrosinase ; Catechol ; Teflon ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Amperometric biosensors incorporating tyrosinase into Teflon/graphite composite were developed for the detection of catechol. The homogeneity of Teflon/graphite was elucidated by means of chronoamperometry (using ferricyanide) and the calculation of the electrochemically active and total surface area of the electrodes. The homogeneity of composite is increased when working with the frozen Teflon. The mechanical strength, sensitivity, apparent Michaelis-Menten constant, maximum currents, and the compatibility with methanol and acetonitrile of the bioelectrodes were investigated. It was found that 10-30% of graphite in Teflon were suitable for the preparation of electrodes of high mechanical strength and low electrical resistivity. The sensitivity was found to be dependent on the ratio of Teflon/graphite where higher percentage of graphite gave the highest sensitivity. Electrode responses for catechol decreased 5% during one hour of its operation in buffer solution containing 10% methanol.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1040-0397
    Keywords: Review ; liquid chromatography ; immobilized enzyme ; electrochemical detection ; chemically modified electrodes ; carbohydrates ; fermentations ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The first part of the paper provides a review of the pre- and postcolumn derivatization systems used in Column Liquid Chromatography (CLC) in combination with immobilized enzyme reactors (IMERs) and electrochemical detection (EC). In the second part, an outline of important factors to consider in the optimization of CLC-IMER-EC systems are presented. Three industrial applications are described utilizing enzyme-based detection or enzymes for sample handling purposes. In two of the cases, CLC-IMER were used in combination with amperometric detection using chemically modified electrodes (CME). These applications were performed in our laboratory, and the high selectivity and sensitivity of these systems as well as the problems encountered in these complex samples will be discussed.
    Additional Material: 19 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 11 (1998), S. 182-184 
    ISSN: 0952-3499
    Keywords: Flow immunoassay ; restricted access column ; pesticides ; atrazine ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: This paper describes a heterogeneous competitive flow immunoassay with a high sample throughput which can be used for the screening of smaller analytes in various samples. The method is based on off-line incubation of the analyte (Ag), a fluorescent labelled tracer (Ag*) and the corresponding antibody (Ab). The separation of bound (Ab-Ag*) and free tracer (Ag*) is based on a size exclusion and reversed phase mechanism utilizing a restricted access (RA) column. The column traps the free unbound tracer (Ag*) in its hydrophobic (C18) inner cavity but excludes the large Ab-Ag* complex, which is passed on and measured by the fluorescence detector. The flow immunoassay was developed using the triazine herbicide atrazine as a model compound owing to its human toxicity and widespread use. A sample throughput of 80 samples per hour and a detection limit of 300 pg ml-1 in water were obtained. Urine samples were successfully applied for direct injections into the flow system, while for human plasma samples an additional clean-up step using solid phase extraction was efficiently included where pure extract is obtained with the highly stable and biocompatible extracting column material. The resulting detection limits for atrazine in plasma and water samples using this clean-up and trace enrichment procedure were found to be 2 ng ml-1 and 20 pg ml-1 respectively. Copyright © 1998 John Wiley & Sons, Ltd.
    Additional Material: 3 Ill.
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  • 10
    ISSN: 1040-0397
    Keywords: Tyrosinase ; Zeolite ; Biosensor ; Phenols ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The dependence of electrode response on additive properties in enzyme-modified carbon paste was studied. Four different HY-zeolite powders, dealuminated to different extents and characterized by both Si/Al ratio and hydrophilicity, were used as the carbon paste modifiers. The enzyme tyrosinase used in biosensors for the detection of catechol and other phenolic compounds was chosen as the model system for the construction of a composite carbon paste biosensor incorporating different HY-zeolites as additives. Tyrosinase was trapped on the HY-zeolite particles from a buffer solution, dried and mixed with graphite powder and a pasting oil. It was found that by incorporating HY-zeolites into the carbon paste the heterogeneous reaction rate of catechol redox conversion and the signal response for catechol were increased. In the latter case a higher response was observed for increased hydrophilicity, i.e., decreased Si/Al ratio of the HY-zeolite. The carbon paste/solution interface is considered to be an aqueous/organic phase and the characteristics of the enzyme- modified carbon paste electrode are related to theories, explaining enzymatic catalysis in organic solvents.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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