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Protein and peptide mass spectrometry in drug discovery [[electronic resource] /] / edited by Michael L. Gross, Guodong Chen, Birendra N. Pramanik
| Protein and peptide mass spectrometry in drug discovery [[electronic resource] /] / edited by Michael L. Gross, Guodong Chen, Birendra N. Pramanik |
| Pubbl/distr/stampa | Hoboken, NJ, : Wiley, c2012 |
| Descrizione fisica | 1 online resource (496 p.) |
| Disciplina | 615/.19 |
| Altri autori (Persone) |
GrossMichael L
ChenGuodong <1966-> PramanikBirendra N. <1944-> |
| Soggetto topico |
Drug development
Peptides - Spectra Proteins - Spectra |
| ISBN |
1-283-28278-X
9786613282781 1-118-11654-2 1-118-11655-0 1-118-11653-4 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein and Peptide Mass Spectrometry in Drug Discovery; CONTENTS; PREFACE; CONTRIBUTORS; PART I: METHODOLOGY; 1 Ionization Methods in Protein Mass Spectrometry; 1.1 History of the Development of Protein Mass Spectrometry; 1.2 Laser-Based Ionization Methods for Proteins; 1.2.1 Matrix-Assisted Laser Desorption/Ionization (MALDI); 1.2.2 Atmospheric Pressure Matrix-Assisted Laser Desorption/Ionization (AP-MALDI); 1.2.3 Surface-Enhanced Laser Desorption/Ionization (SELDI); 1.2.4 Nanostructure-Initiator Mass Spectrometry (NIMS); 1.3 Spray-Based Ionization Methods for Proteins
1.3.1 Electrospray Ionization (ESI)1.3.2 Sonic Spray Ionization (SSI); 1.3.3 Electrosonic Spray Ionization (ESSI); 1.4 Ambient Ionization Methods; 1.4.1 Desorption Electrospray Ionization (DESI); 1.4.2 Fused-Droplet Electrospray Ionization (FD-ESI); 1.4.3 Electrospray-Assisted Laser Desorption Ionization (ELDI); 1.4.4 Matrix-Assisted Laser Desorption Electrospray Ionization (MALDESI); 1.5 Conclusions; Acknowledgments; References; 2 Ion Activation and Mass Analysis in Protein Mass Spectrometry; 2.1 Introduction; 2.1.1 Mass Accuracy; 2.1.2 Mass Resolving Power; 2.1.3 Mass Range 2.1.4 Scan Speed2.1.5 Tandem MS Analysis; 2.2 Ion Activation and Tandem MS Analysis; 2.2.1 Introduction: Fragmentation in Protein MS; 2.2.2 Collisional Activation Methods; 2.2.3 Photodissociation; 2.2.4 Electron-Induced Dissociation; 2.2.5 Other Radical-Induced Fragmentation Methods; 2.3 Mass Analyzers; 2.3.1 Time-of-Flight Mass Analyzer; 2.3.2 Quadrupole Mass Analyzer and Quadrupole Ion Trap; 2.3.3 Fourier-Transform Ion Cyclotron Resonance Mass Spectrometer; 2.3.4 Orbitrap; 2.3.5 Ion-Mobility Instruments; References; 3 Target Proteins: Bottom-up and Top-down Proteomics 3.1 Mass Spectral Approaches to Targeted Protein Identification3.2 Bottom-up Proteomics; 3.2.1 Peptide Mass Fingerprinting; 3.2.2 Bottom-up Proteomics Using Tandem MS: GeLC-MS/MS and Shotgun Digests; 3.2.3 GeLC-MS/MS; 3.2.4 Shotgun Digest; 3.3 Top-down Approaches; 3.4 Next-Generation Approaches; References; 4 Quantitative Proteomics by Mass Spectrometry; 4.1 Introduction; 4.2 In-Cell Labeling; 4.2.1 15N Metabolic Labeling; 4.2.2 Stable Isotope Labeling by Amino Acid (SILAC); 4.3 Quantitation via Isotopic Labeling of Proteins; 4.3.1 2D PAGE-Based Quantitation 4.3.2 Proteolytic Labeling Using 18O Water4.3.3 Quantitative Labeling by Chemical Tagging; 4.4 Quantitation via Isotopic Labeling on Peptides; 4.4.1 ICAT; 4.4.2 iTRAQ; 4.4.3 SoPIL; 4.4.4 Absolute Quantitation; 4.5 Label-Free Quantitation; 4.6 Conclusions; Acknowledgment; References; 5 Comparative Proteomics by Direct Tissue Analysis Using Imaging Mass Spectrometry; 5.1 Introduction; 5.2 Conventional Comparative Proteomics; 5.3 Comparative Proteomics Using Imaging MS; 5.3.1 Biomarker Discovery: Breast Cancer; 5.3.2 Biomarker Discovery: Toxicity; 5.3.3 Correlating Drug and Protein Distributions 5.4 Conclusions |
| Record Nr. | UNINA-9910141237703321 |
| Hoboken, NJ, : Wiley, c2012 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Protein and peptide mass spectrometry in drug discovery / / edited by Michael L. Gross, Guodong Chen, Birendra N. Pramanik
| Protein and peptide mass spectrometry in drug discovery / / edited by Michael L. Gross, Guodong Chen, Birendra N. Pramanik |
| Edizione | [1st ed.] |
| Pubbl/distr/stampa | Hoboken, NJ, : Wiley, c2012 |
| Descrizione fisica | 1 online resource (496 p.) |
| Disciplina | 615/.19 |
| Altri autori (Persone) |
GrossMichael L
ChenGuodong <1966-> PramanikBirendra N. <1944-> |
| Soggetto topico |
Drug development
Peptides - Spectra Proteins - Spectra |
| ISBN |
1-283-28278-X
9786613282781 1-118-11654-2 1-118-11655-0 1-118-11653-4 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Protein and Peptide Mass Spectrometry in Drug Discovery; CONTENTS; PREFACE; CONTRIBUTORS; PART I: METHODOLOGY; 1 Ionization Methods in Protein Mass Spectrometry; 1.1 History of the Development of Protein Mass Spectrometry; 1.2 Laser-Based Ionization Methods for Proteins; 1.2.1 Matrix-Assisted Laser Desorption/Ionization (MALDI); 1.2.2 Atmospheric Pressure Matrix-Assisted Laser Desorption/Ionization (AP-MALDI); 1.2.3 Surface-Enhanced Laser Desorption/Ionization (SELDI); 1.2.4 Nanostructure-Initiator Mass Spectrometry (NIMS); 1.3 Spray-Based Ionization Methods for Proteins
1.3.1 Electrospray Ionization (ESI)1.3.2 Sonic Spray Ionization (SSI); 1.3.3 Electrosonic Spray Ionization (ESSI); 1.4 Ambient Ionization Methods; 1.4.1 Desorption Electrospray Ionization (DESI); 1.4.2 Fused-Droplet Electrospray Ionization (FD-ESI); 1.4.3 Electrospray-Assisted Laser Desorption Ionization (ELDI); 1.4.4 Matrix-Assisted Laser Desorption Electrospray Ionization (MALDESI); 1.5 Conclusions; Acknowledgments; References; 2 Ion Activation and Mass Analysis in Protein Mass Spectrometry; 2.1 Introduction; 2.1.1 Mass Accuracy; 2.1.2 Mass Resolving Power; 2.1.3 Mass Range 2.1.4 Scan Speed2.1.5 Tandem MS Analysis; 2.2 Ion Activation and Tandem MS Analysis; 2.2.1 Introduction: Fragmentation in Protein MS; 2.2.2 Collisional Activation Methods; 2.2.3 Photodissociation; 2.2.4 Electron-Induced Dissociation; 2.2.5 Other Radical-Induced Fragmentation Methods; 2.3 Mass Analyzers; 2.3.1 Time-of-Flight Mass Analyzer; 2.3.2 Quadrupole Mass Analyzer and Quadrupole Ion Trap; 2.3.3 Fourier-Transform Ion Cyclotron Resonance Mass Spectrometer; 2.3.4 Orbitrap; 2.3.5 Ion-Mobility Instruments; References; 3 Target Proteins: Bottom-up and Top-down Proteomics 3.1 Mass Spectral Approaches to Targeted Protein Identification3.2 Bottom-up Proteomics; 3.2.1 Peptide Mass Fingerprinting; 3.2.2 Bottom-up Proteomics Using Tandem MS: GeLC-MS/MS and Shotgun Digests; 3.2.3 GeLC-MS/MS; 3.2.4 Shotgun Digest; 3.3 Top-down Approaches; 3.4 Next-Generation Approaches; References; 4 Quantitative Proteomics by Mass Spectrometry; 4.1 Introduction; 4.2 In-Cell Labeling; 4.2.1 15N Metabolic Labeling; 4.2.2 Stable Isotope Labeling by Amino Acid (SILAC); 4.3 Quantitation via Isotopic Labeling of Proteins; 4.3.1 2D PAGE-Based Quantitation 4.3.2 Proteolytic Labeling Using 18O Water4.3.3 Quantitative Labeling by Chemical Tagging; 4.4 Quantitation via Isotopic Labeling on Peptides; 4.4.1 ICAT; 4.4.2 iTRAQ; 4.4.3 SoPIL; 4.4.4 Absolute Quantitation; 4.5 Label-Free Quantitation; 4.6 Conclusions; Acknowledgment; References; 5 Comparative Proteomics by Direct Tissue Analysis Using Imaging Mass Spectrometry; 5.1 Introduction; 5.2 Conventional Comparative Proteomics; 5.3 Comparative Proteomics Using Imaging MS; 5.3.1 Biomarker Discovery: Breast Cancer; 5.3.2 Biomarker Discovery: Toxicity; 5.3.3 Correlating Drug and Protein Distributions 5.4 Conclusions |
| Record Nr. | UNINA-9910814257703321 |
| Hoboken, NJ, : Wiley, c2012 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
