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Proteomics for drug discovery : methods and protocols / edited by Iulia M. Lazar, Maria Kontoyianni, Alexandru C. Lazar.

Contributor(s): Material type: TextTextSeries: Methods in molecular biology (Clifton, N.J.) ; v. 1647.Publisher: New York : Humana Press : Springer, [2017]Copyright date: ©2017Description: 1 online resource (xi, 302 pages) : illustrations (some color)Content type:
  • text
Media type:
  • computer
Carrier type:
  • online resource
ISBN:
  • 9781493972012
  • 1493972014
Subject(s): Genre/Form: Additional physical formats: Print version:: No titleDDC classification:
  • 615.1/9 23
LOC classification:
  • RM301.25
NLM classification:
  • W1
  • QV 745
Online resources:
Contents:
Photoaffinity labeling-based chemoproteomics strategy for unbiased target deconvolution of small molecule drug candidates / Jason R. Thomas, Scott M. Brittain, Jennifer Lipps, Luis Llamas, Rishi K. Jain, and Markus Schirle -- Multiplexed liquid chromatography-multiple reaction monitoring mass spectrometry quantification of cancer signaling proteins / Yi Chen, Kate J. Fisher, Mark Lloyd, Elizabeth R. Wood, Domenico Coppola, Erin Siegel, David Shibata, Yian A. Chen, and John M. Koomen -- Monitoring dynamic changes of the cell surface glycoproteome by quantitative proteomics / Mathias Kalxdorf, Hans Christian Eberl, and Marcus Bantscheff -- High-resolution parallel reaction monitoring with electron transfer dissociation for middle-down proteomics : an application to study the quantitative changes induced by histone modifying enzyme inhibitors and activators / Michael J. Sweredoski, Annie Moradian, and Sonja Hess -- Preparation and immunoaffinity depletion of fresh frozen tissue homogenates for mass spectrometry-based proteomics in the context of drug target/biomarker discovery / DaRue A. Prieto, King C. Chan, Donald J. Johann Jr, Xiaoying Ye, Gordon Whitely, and Josip Blonder -- Target identification using cell permeable and cleavable chloroalkane derivatized small molecules / Jacqui L. Mendez-Johnson, Danette L. Daniels, Marjeta Urh, and Rachel Friedman Ohana -- Microfluidics-mass spectrometry of protein-carbohydrate interactions : applications to the development of therapeutics and Biomarker Discovery / Alina D. Zamfir -- Studying protein-protein interactions by biotin AP-tagged pulldown and LTQ-qrbitrap mass spectrometry / Zhongqiu Xie, Yuemeng Jia, and Hui Li -- Post-translational modification profiling-functional proteomics for the analysis of immune regulation / Avital Eisenberg-Lerner, Ifat Regev, and Yifat Merbl -- Reverse phase protein arrays and drug discovery / Kenneth G. Macleod, Bryan Serrels, and Neil O. Carragher -- Probing protein kinase-ATP interactions using a fluorescent ATP analog / Leslie E.W. LaConte, Sarika Srivastava, and Konark Mukherjee -- Preparation of disease-related protein assemblies for single particle electron microscopy / A. Cameron Varano, Naoe Harafuji, William Dearnaley, Lisa Guay-Woodford, and Deborah F. Kelly -- Identification of lipid binding modulators using the protein-lipid overlay assay / Tuo-Xian Tang, Wen Xiong, Carla V. Finkielstein, and Daniel G.S. Capelluto -- Resazurin live cell assay : setup and fine-tuning for reliable cytotoxicity results / Jose A . Rodrıguez-Corrales and Jatinder S. Josan -- Exploring protein-protein interactions as drug targets for anti-cancer therapy with in silico workflows / Alexander Goncearenco, Minghui Li, Franco L. Simonetti, Benjamin A. Shoemaker, and Anna R. Panchenko -- Method to identify silent codon mutations that may alter peptide elongation kinetics and co-translational protein folding / Ronald Worthington, Elijah Ball, Brentsen Wolf, and Gregory Takacs -- In silico design of anticancer peptides / Shailesh Kumar and Hui Li -- Docking and virtual screening in drug discovery / Maria Kontoyianni -- Bioinformatics resources for interpreting proteomics mass spectrometry data / Iulia M. Lazar -- Erratum to : Probing protein kinase-ATP interactions using a fluorescent ATP analog / Leslie E. LaConte, Sarika Srivastava, Konark Mukherjee.
Summary: This book reflects the drug development communitys interest in proteomics methods by providing researchers with the necessary knowledge for the implementation of a number of basic experimental and bioinformatics protocols in the drug discovery research laboratory. The focus of the collection is on select protocols and methodologies that address the analysis of post-translational modifications, targeted protein quantification, protein-protein, protein-lipid, or protein-ATP interactions, in silicolead identification, protein arrays, tissue and cell extract preparation, labeling, chemoproteomics, and drug efficacy assessment. Emphasis was placed not just on methods that describe large-scale protein analysis, but also on ones that are amenable to future implementation in a high-throughput format. Written in the highly successfulMethods in Molecular Biologyseries format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Practical and authoritative, Proteomics for Drug Discovery: Methods and Protocolsaims to provide a deep knowledge of the fundamentals of disease biology as well the means that were developed for probing the complex biological milieu.
Holdings
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Includes bibliographical references and index.

Photoaffinity labeling-based chemoproteomics strategy for unbiased target deconvolution of small molecule drug candidates / Jason R. Thomas, Scott M. Brittain, Jennifer Lipps, Luis Llamas, Rishi K. Jain, and Markus Schirle -- Multiplexed liquid chromatography-multiple reaction monitoring mass spectrometry quantification of cancer signaling proteins / Yi Chen, Kate J. Fisher, Mark Lloyd, Elizabeth R. Wood, Domenico Coppola, Erin Siegel, David Shibata, Yian A. Chen, and John M. Koomen -- Monitoring dynamic changes of the cell surface glycoproteome by quantitative proteomics / Mathias Kalxdorf, Hans Christian Eberl, and Marcus Bantscheff -- High-resolution parallel reaction monitoring with electron transfer dissociation for middle-down proteomics : an application to study the quantitative changes induced by histone modifying enzyme inhibitors and activators / Michael J. Sweredoski, Annie Moradian, and Sonja Hess -- Preparation and immunoaffinity depletion of fresh frozen tissue homogenates for mass spectrometry-based proteomics in the context of drug target/biomarker discovery / DaRue A. Prieto, King C. Chan, Donald J. Johann Jr, Xiaoying Ye, Gordon Whitely, and Josip Blonder -- Target identification using cell permeable and cleavable chloroalkane derivatized small molecules / Jacqui L. Mendez-Johnson, Danette L. Daniels, Marjeta Urh, and Rachel Friedman Ohana -- Microfluidics-mass spectrometry of protein-carbohydrate interactions : applications to the development of therapeutics and Biomarker Discovery / Alina D. Zamfir -- Studying protein-protein interactions by biotin AP-tagged pulldown and LTQ-qrbitrap mass spectrometry / Zhongqiu Xie, Yuemeng Jia, and Hui Li -- Post-translational modification profiling-functional proteomics for the analysis of immune regulation / Avital Eisenberg-Lerner, Ifat Regev, and Yifat Merbl -- Reverse phase protein arrays and drug discovery / Kenneth G. Macleod, Bryan Serrels, and Neil O. Carragher -- Probing protein kinase-ATP interactions using a fluorescent ATP analog / Leslie E.W. LaConte, Sarika Srivastava, and Konark Mukherjee -- Preparation of disease-related protein assemblies for single particle electron microscopy / A. Cameron Varano, Naoe Harafuji, William Dearnaley, Lisa Guay-Woodford, and Deborah F. Kelly -- Identification of lipid binding modulators using the protein-lipid overlay assay / Tuo-Xian Tang, Wen Xiong, Carla V. Finkielstein, and Daniel G.S. Capelluto -- Resazurin live cell assay : setup and fine-tuning for reliable cytotoxicity results / Jose A . Rodrıguez-Corrales and Jatinder S. Josan -- Exploring protein-protein interactions as drug targets for anti-cancer therapy with in silico workflows / Alexander Goncearenco, Minghui Li, Franco L. Simonetti, Benjamin A. Shoemaker, and Anna R. Panchenko -- Method to identify silent codon mutations that may alter peptide elongation kinetics and co-translational protein folding / Ronald Worthington, Elijah Ball, Brentsen Wolf, and Gregory Takacs -- In silico design of anticancer peptides / Shailesh Kumar and Hui Li -- Docking and virtual screening in drug discovery / Maria Kontoyianni -- Bioinformatics resources for interpreting proteomics mass spectrometry data / Iulia M. Lazar -- Erratum to : Probing protein kinase-ATP interactions using a fluorescent ATP analog / Leslie E. LaConte, Sarika Srivastava, Konark Mukherjee.

Online resource; title from PDF title page (SpringerProtocol, viewed August 16, 2017).

This book reflects the drug development communitys interest in proteomics methods by providing researchers with the necessary knowledge for the implementation of a number of basic experimental and bioinformatics protocols in the drug discovery research laboratory. The focus of the collection is on select protocols and methodologies that address the analysis of post-translational modifications, targeted protein quantification, protein-protein, protein-lipid, or protein-ATP interactions, in silicolead identification, protein arrays, tissue and cell extract preparation, labeling, chemoproteomics, and drug efficacy assessment. Emphasis was placed not just on methods that describe large-scale protein analysis, but also on ones that are amenable to future implementation in a high-throughput format. Written in the highly successfulMethods in Molecular Biologyseries format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Practical and authoritative, Proteomics for Drug Discovery: Methods and Protocolsaims to provide a deep knowledge of the fundamentals of disease biology as well the means that were developed for probing the complex biological milieu.

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