High content screening [[electronic resource] ] : science, techniques and applications / / edited by Steven A. Haney |
Pubbl/distr/stampa | Hoboken, N.J., : Wiley-Interscience, c2008 |
Descrizione fisica | 1 online resource (444 p.) |
Disciplina |
615.19
615/.19 |
Altri autori (Persone) | HaneySteven A |
Soggetto topico |
Biological systems - Research - Methodology
Combinatorial chemistry Computational biology |
ISBN |
1-281-28456-4
9786611284565 0-470-22986-1 0-470-22985-3 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
HIGH CONTENT SCREENING; CONTENTS; Preface; Contributors; SECTION I ESSENTIALS OF HIGH CONTENT SCREENING; 1. Approaching High Content Screening and Analysis: Practical Advice for Users; 1.1 Introduction; 1.2 What is HCS and Why Should I Care?; 1.3 How does HCS Compare with Current Assay Methods?; 1.4 The Basic Requirements to Implement HCS; 1.4.1 Cell Banking; 1.4.2 Plating, Cell Density, and the Assay Environment; 1.4.3 Compound Addition and Incubation; 1.4.4 Post-Assay Processing; 1.4.5 HCS Imaging Hardware; 1.4.6 HCS Analysis Software; 1.4.7 Informatics; 1.5 The Process
1.6 An Example Approach 1.7 Six Considerations for HCS Assays; 1.7.1 Garbage In, Garbage Out (GIGO); 1.7.2 This Is Not a Plate Reader; 1.7.3 Understand Your Biology; 1.7.4 Subtle Changes Can Be Measured and Are Significant; 1.7.5 HCS Workflow - Flexibility is the Key; 1.7.6 HCS is Hard - How Do I Learn It and Become Proficient at It?; References; 2. Automated High Content Screening Microscopy; 2.1 Introduction; 2.2 Automated HCS Imaging Requirements; 2.3 Components of Automated Imaging Platforms; 2.3.1 Fluorescence Imaging and Multiplexing; 2.3.2 Light Sources 2.3.3 Optical Designs: Confocal Versus Wide-Field 2.3.4 Objectives; 2.3.5 Detectors; 2.3.6 Autofocus; 2.3.7 Environmental Controls and On-Board Liquid Handling Capabilities; 2.4 Imaging Platform Software; 2.5 Data Storage and Management; 2.6 Selecting an HCS Platform; 2.7 Comparison of a SAPK Activation HCS Assay Read on an ArrayScan(®) 3.1, an ArrayScan(®) V(Ti), and an IN Cell 3000 Automated Imaging Platform; References; 3. A Primer on Image Informatics of High Content Screening; 3.1 Background; 3.2 HCS Image Processing; 3.2.1 Image Pre-Processing 3.2.2 Cell Detection, Segmentation, and Centerline Extraction 3.2.2.1 Cell Detection; 3.2.2.2 Particle Detection; 3.2.2.3 Cell Segmentation; 3.2.2.4 Centerline/Neurite Extraction; 3.2.3 Cell Tracking and Registration; 3.2.3.1 Simple Matching Algorithm; 3.2.3.2 Mean Shift; 3.2.3.3 Kalman Filter; 3.2.3.4 Mutual Information; 3.2.3.5 Fuzzy-System-Based Tracking; 3.2.3.6 Parallel Tracking; 3.2.4 Feature Extraction; 3.2.4.1 Features Extracted from Markov Chain Modeling of Time-Lapse Images; 3.3 Validation; 3.4 Information System Management; 3.5 Data Modeling 3.5.1 Novel Phenotype Discovery Using Clustering 3.5.2 Gene Function Study Using Clustering; 3.5.3 Screening Hits Selection and Gene Scoring for Effectors Discovery; 3.5.3.1 Fuzzy Gene Score Regression Model; 3.5.3.2 Experimental Results; 3.5.4 Metabolic Networks Validated by Using Genomics, Proteomics, and HCS; 3.5.5 Connecting HCS Analysis and Systems Biology; 3.5.6 Metabolic Networks; 3.6 Conclusions; 3.7 Acknowledgments; References; 4. Developing Robust High Content Assays; 4.1 Introduction; 4.2 Overview of a Typical Immunofluorescence-Based High Content Assay; 4.2.1 Staining Protocol 4.2.2 Sources of Variability |
Record Nr. | UNINA-9910146370303321 |
Hoboken, N.J., : Wiley-Interscience, c2008 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
High content screening : science, techniques and applications / / edited by Steven A. Haney |
Edizione | [1st ed.] |
Pubbl/distr/stampa | Hoboken, N.J., : Wiley-Interscience, c2008 |
Descrizione fisica | 1 online resource (444 p.) |
Disciplina |
615.19
615/.19 |
Altri autori (Persone) | HaneySteven A |
Soggetto topico |
Biological systems - Research - Methodology
Combinatorial chemistry Computational biology |
ISBN |
1-281-28456-4
9786611284565 0-470-22986-1 0-470-22985-3 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
HIGH CONTENT SCREENING; CONTENTS; Preface; Contributors; SECTION I ESSENTIALS OF HIGH CONTENT SCREENING; 1. Approaching High Content Screening and Analysis: Practical Advice for Users; 1.1 Introduction; 1.2 What is HCS and Why Should I Care?; 1.3 How does HCS Compare with Current Assay Methods?; 1.4 The Basic Requirements to Implement HCS; 1.4.1 Cell Banking; 1.4.2 Plating, Cell Density, and the Assay Environment; 1.4.3 Compound Addition and Incubation; 1.4.4 Post-Assay Processing; 1.4.5 HCS Imaging Hardware; 1.4.6 HCS Analysis Software; 1.4.7 Informatics; 1.5 The Process
1.6 An Example Approach 1.7 Six Considerations for HCS Assays; 1.7.1 Garbage In, Garbage Out (GIGO); 1.7.2 This Is Not a Plate Reader; 1.7.3 Understand Your Biology; 1.7.4 Subtle Changes Can Be Measured and Are Significant; 1.7.5 HCS Workflow - Flexibility is the Key; 1.7.6 HCS is Hard - How Do I Learn It and Become Proficient at It?; References; 2. Automated High Content Screening Microscopy; 2.1 Introduction; 2.2 Automated HCS Imaging Requirements; 2.3 Components of Automated Imaging Platforms; 2.3.1 Fluorescence Imaging and Multiplexing; 2.3.2 Light Sources 2.3.3 Optical Designs: Confocal Versus Wide-Field 2.3.4 Objectives; 2.3.5 Detectors; 2.3.6 Autofocus; 2.3.7 Environmental Controls and On-Board Liquid Handling Capabilities; 2.4 Imaging Platform Software; 2.5 Data Storage and Management; 2.6 Selecting an HCS Platform; 2.7 Comparison of a SAPK Activation HCS Assay Read on an ArrayScan(®) 3.1, an ArrayScan(®) V(Ti), and an IN Cell 3000 Automated Imaging Platform; References; 3. A Primer on Image Informatics of High Content Screening; 3.1 Background; 3.2 HCS Image Processing; 3.2.1 Image Pre-Processing 3.2.2 Cell Detection, Segmentation, and Centerline Extraction 3.2.2.1 Cell Detection; 3.2.2.2 Particle Detection; 3.2.2.3 Cell Segmentation; 3.2.2.4 Centerline/Neurite Extraction; 3.2.3 Cell Tracking and Registration; 3.2.3.1 Simple Matching Algorithm; 3.2.3.2 Mean Shift; 3.2.3.3 Kalman Filter; 3.2.3.4 Mutual Information; 3.2.3.5 Fuzzy-System-Based Tracking; 3.2.3.6 Parallel Tracking; 3.2.4 Feature Extraction; 3.2.4.1 Features Extracted from Markov Chain Modeling of Time-Lapse Images; 3.3 Validation; 3.4 Information System Management; 3.5 Data Modeling 3.5.1 Novel Phenotype Discovery Using Clustering 3.5.2 Gene Function Study Using Clustering; 3.5.3 Screening Hits Selection and Gene Scoring for Effectors Discovery; 3.5.3.1 Fuzzy Gene Score Regression Model; 3.5.3.2 Experimental Results; 3.5.4 Metabolic Networks Validated by Using Genomics, Proteomics, and HCS; 3.5.5 Connecting HCS Analysis and Systems Biology; 3.5.6 Metabolic Networks; 3.6 Conclusions; 3.7 Acknowledgments; References; 4. Developing Robust High Content Assays; 4.1 Introduction; 4.2 Overview of a Typical Immunofluorescence-Based High Content Assay; 4.2.1 Staining Protocol 4.2.2 Sources of Variability |
Record Nr. | UNINA-9910808584203321 |
Hoboken, N.J., : Wiley-Interscience, c2008 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Proteomics of biological systems [[electronic resource] ] : protein phosphorylation using mass spectrometry techniques / / Bryan M Ham |
Autore | Ham Bryan M |
Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, 2012 |
Descrizione fisica | 1 online resource (376 p.) |
Disciplina | 572/.62 |
Soggetto topico |
Proteomics - Methodology
Phosphorylation - Research - Methodology Phosphoproteins - Synthesis Mass spectrometry Biological systems - Research - Methodology |
ISBN |
1-283-28285-2
9786613282859 1-118-13703-5 1-118-13704-3 1-118-13701-9 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
PROTEOMICS OF BIOLOGICAL SYSTEMS: Protein Phosphorylation Using Mass Spectrometry Techniques; CONTENTS; PREFACE; ACKNOWLEDGMENTS; ABOUT THE AUTHOR; 1: Posttranslational Modification (PTM) of Proteins; 1.1 OVER 200 FORMS OF PTM OF PROTEINS; 1.2 THREE MAIN TYPES OF PTM STUDIED BY MS; 1.3 OVERVIEW OF NANO-ELECTROSPRAY/NANOFLOW LC-MS; 1.3.1 Definition and Description of MS; 1.3.2 Basic Design of Mass Analyzer Instrumentation; 1.3.3 ESI; 1.3.4 Nano-ESI; 1.4 OVERVIEW OF NUCLEIC ACIDS; 1.5 PROTEINS AND PROTEOMICS; 1.5.1 Introduction to Proteomics; 1.5.2 Protein Structure and Chemistry
1.5.3 Bottom-Up Proteomics: MS of Peptides1.5.3.1 History and Strategy; 1.5.3.2 Protein Identification through Product Ion Spectra; 1.5.3.3 High-Energy Product Ions; 1.5.3.4 De Novo Sequencing; 1.5.3.5 Electron Capture Dissociation (ECD); 1.5.4 Top-Down Proteomics: MS of Intact Proteins; 1.5.4.1 Background; 1.5.4.2 GP Basicity and Protein Charging; 1.5.4.3 Calculation of Charge State and Molecular Weight; 1.5.4.4 Top-Down Protein Sequencing; 1.5.5 Systems Biology and Bioinformatics; 1.5.6 Biomarkers in Cancer; REFERENCES; 2: Glycosylation of Proteins; 2.1 PRODUCTION OF A GLYCOPROTEIN 2.2 BIOLOGICAL PROCESSES OF PROTEIN GLYCOSYLATION2.3 N-LINKED AND O-LINKED GLYCOSYLATION; 2.4 CARBOHYDRATES; 2.4.1 Ionization of Oligosaccharides; 2.4.2 Carbohydrate Fragmentation; 2.4.3 Complex Oligosaccharide Structural Elucidation; 2.5 THREE OBJECTIVES IN STUDYING GLYCOPROTEINS; 2.6 GLYCOSYLATION STUDY APPROACHES; 2.6.1 MS of Glycopeptides; 2.6.2 Mass Pattern Recognition; 2.6.2.1 High Galactose Glycosylation Pattern; 2.6.3 Charge State Determination; 2.6.4 Diagnostic Fragment Ions; 2.6.5 High-Resolution/High-Mass Accuracy Measurement and Identification; 2.6.6 Digested Bovine Fetuin REFERENCES3: Sulfation of Proteins as Posttranslational Modification; 3.1 GLYCOSAMINOGLYCAN SULFATION; 3.2 CELLULAR PROCESSES INVOLVED IN SULFATION; 3.3 BRIEF EXAMPLE OF PHOSPHORYLATION; 3.4 SULFOTRANSFERASE CLASS OF ENZYMES; 3.5 FRAGMENTATION NOMENCLATURE FOR CARBOHYDRATES; 3.6 SULFATED MUCIN OLIGOSACCHARIDES; 3.7 TYROSINE SULFATION; 3.8 TYROSYLPROTEIN SULFOTRANSFERASES TPST1 AND TPST2; 3.9 O-SULFATED HUMAN PROTEINS; 3.10 SULFATED PEPTIDE PRODUCT ION SPECTRA; 3.11 USE OF HIGHER ENERGY COLLISIONS; 3.12 ELECTRON CAPTURE DISSOCIATION (ECD); 3.13 SULFATION VERSUS PHOSPHORYLATION; REFERENCES 4: Eukaryote PTM as Phosphorylation: Normal State Studies4.1 MASS SPECTRAL MEASUREMENT WITH EXAMPLES OF HELA CELL PHOSPHOPROTEOME; 4.1.1 Introduction; 4.1.2 Protein Phosphatase and Kinase; 4.1.3 Hydroxy-Amino Acid Phosphorylation; 4.1.4 Traditional Phosphoproteomic Approaches; 4.1.5 Current Approaches; 4.1.5.1 Phosphoproteomic Enrichment Techniques; 4.1.5.2 IMAC; 4.1.5.3 MOAC; 4.1.5.4 Methylation of Peptides prior to IMAC or MOAC Enrichment; 4.1.6 The Ideal Approach; 4.1.7 One-Dimensional (1-D) Sodium Dodecyl Sulfate (SDS) PAGE; 4.1.8 Tandem MS Approach; 4.1.8.1 pS Loss of Phosphate Group 4.1.8.2 pT Loss of Phosphate Group |
Record Nr. | UNINA-9910139593603321 |
Ham Bryan M
![]() |
||
Hoboken, N.J., : John Wiley & Sons, 2012 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Proteomics of biological systems : protein phosphorylation using mass spectrometry techniques / / Bryan M Ham |
Autore | Ham Bryan M |
Edizione | [1st ed.] |
Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, 2012 |
Descrizione fisica | 1 online resource (376 p.) |
Disciplina | 572/.62 |
Soggetto topico |
Proteomics - Methodology
Phosphorylation - Research - Methodology Phosphoproteins - Synthesis Mass spectrometry Biological systems - Research - Methodology |
ISBN |
1-283-28285-2
9786613282859 1-118-13703-5 1-118-13704-3 1-118-13701-9 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
PROTEOMICS OF BIOLOGICAL SYSTEMS: Protein Phosphorylation Using Mass Spectrometry Techniques; CONTENTS; PREFACE; ACKNOWLEDGMENTS; ABOUT THE AUTHOR; 1: Posttranslational Modification (PTM) of Proteins; 1.1 OVER 200 FORMS OF PTM OF PROTEINS; 1.2 THREE MAIN TYPES OF PTM STUDIED BY MS; 1.3 OVERVIEW OF NANO-ELECTROSPRAY/NANOFLOW LC-MS; 1.3.1 Definition and Description of MS; 1.3.2 Basic Design of Mass Analyzer Instrumentation; 1.3.3 ESI; 1.3.4 Nano-ESI; 1.4 OVERVIEW OF NUCLEIC ACIDS; 1.5 PROTEINS AND PROTEOMICS; 1.5.1 Introduction to Proteomics; 1.5.2 Protein Structure and Chemistry
1.5.3 Bottom-Up Proteomics: MS of Peptides1.5.3.1 History and Strategy; 1.5.3.2 Protein Identification through Product Ion Spectra; 1.5.3.3 High-Energy Product Ions; 1.5.3.4 De Novo Sequencing; 1.5.3.5 Electron Capture Dissociation (ECD); 1.5.4 Top-Down Proteomics: MS of Intact Proteins; 1.5.4.1 Background; 1.5.4.2 GP Basicity and Protein Charging; 1.5.4.3 Calculation of Charge State and Molecular Weight; 1.5.4.4 Top-Down Protein Sequencing; 1.5.5 Systems Biology and Bioinformatics; 1.5.6 Biomarkers in Cancer; REFERENCES; 2: Glycosylation of Proteins; 2.1 PRODUCTION OF A GLYCOPROTEIN 2.2 BIOLOGICAL PROCESSES OF PROTEIN GLYCOSYLATION2.3 N-LINKED AND O-LINKED GLYCOSYLATION; 2.4 CARBOHYDRATES; 2.4.1 Ionization of Oligosaccharides; 2.4.2 Carbohydrate Fragmentation; 2.4.3 Complex Oligosaccharide Structural Elucidation; 2.5 THREE OBJECTIVES IN STUDYING GLYCOPROTEINS; 2.6 GLYCOSYLATION STUDY APPROACHES; 2.6.1 MS of Glycopeptides; 2.6.2 Mass Pattern Recognition; 2.6.2.1 High Galactose Glycosylation Pattern; 2.6.3 Charge State Determination; 2.6.4 Diagnostic Fragment Ions; 2.6.5 High-Resolution/High-Mass Accuracy Measurement and Identification; 2.6.6 Digested Bovine Fetuin REFERENCES3: Sulfation of Proteins as Posttranslational Modification; 3.1 GLYCOSAMINOGLYCAN SULFATION; 3.2 CELLULAR PROCESSES INVOLVED IN SULFATION; 3.3 BRIEF EXAMPLE OF PHOSPHORYLATION; 3.4 SULFOTRANSFERASE CLASS OF ENZYMES; 3.5 FRAGMENTATION NOMENCLATURE FOR CARBOHYDRATES; 3.6 SULFATED MUCIN OLIGOSACCHARIDES; 3.7 TYROSINE SULFATION; 3.8 TYROSYLPROTEIN SULFOTRANSFERASES TPST1 AND TPST2; 3.9 O-SULFATED HUMAN PROTEINS; 3.10 SULFATED PEPTIDE PRODUCT ION SPECTRA; 3.11 USE OF HIGHER ENERGY COLLISIONS; 3.12 ELECTRON CAPTURE DISSOCIATION (ECD); 3.13 SULFATION VERSUS PHOSPHORYLATION; REFERENCES 4: Eukaryote PTM as Phosphorylation: Normal State Studies4.1 MASS SPECTRAL MEASUREMENT WITH EXAMPLES OF HELA CELL PHOSPHOPROTEOME; 4.1.1 Introduction; 4.1.2 Protein Phosphatase and Kinase; 4.1.3 Hydroxy-Amino Acid Phosphorylation; 4.1.4 Traditional Phosphoproteomic Approaches; 4.1.5 Current Approaches; 4.1.5.1 Phosphoproteomic Enrichment Techniques; 4.1.5.2 IMAC; 4.1.5.3 MOAC; 4.1.5.4 Methylation of Peptides prior to IMAC or MOAC Enrichment; 4.1.6 The Ideal Approach; 4.1.7 One-Dimensional (1-D) Sodium Dodecyl Sulfate (SDS) PAGE; 4.1.8 Tandem MS Approach; 4.1.8.1 pS Loss of Phosphate Group 4.1.8.2 pT Loss of Phosphate Group |
Record Nr. | UNINA-9910821480603321 |
Ham Bryan M
![]() |
||
Hoboken, N.J., : John Wiley & Sons, 2012 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|