Mass spectrometry-based chemical proteomics / / edited by W. Andy Tao (Purdue University, West Lafayette, IN, US), Ying Zhang (Fudan University, Shanghai, China) |
Pubbl/distr/stampa | Hoboken, New Jersey : , : Wiley, , [2019] |
Descrizione fisica | 1 online resource (448 pages) |
Disciplina | 572.6 |
Collana | THEi Wiley ebooks. |
Soggetto topico |
Proteins - Spectra
Proteomics Molecular biology Spectrum analysis |
ISBN |
1-118-97020-9
1-118-97021-7 1-118-97019-5 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Record Nr. | UNINA-9910555173403321 |
Hoboken, New Jersey : , : Wiley, , [2019] | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Mass spectrometry-based chemical proteomics / / edited by W. Andy Tao (Purdue University, West Lafayette, IN, US), Ying Zhang (Fudan University, Shanghai, China) |
Pubbl/distr/stampa | Hoboken, New Jersey : , : Wiley, , [2019] |
Descrizione fisica | 1 online resource (448 pages) |
Disciplina | 572.6 |
Collana | THEi Wiley ebooks. |
Soggetto topico |
Proteins - Spectra
Proteomics Molecular biology Spectrum analysis |
ISBN |
1-118-97020-9
1-118-97021-7 1-118-97019-5 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Record Nr. | UNINA-9910825182803321 |
Hoboken, New Jersey : , : Wiley, , [2019] | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
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 |
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 | ||
|
Proteomics today [[electronic resource] ] : protein assessment and biomarkers using mass spectrometry, 2D electrophoresis, and microarray technology / / Mahmoud Hamdan, Pier Giorgio Righetti |
Autore | Hamdan Mahmoud <1947-> |
Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, 2005 |
Descrizione fisica | 1 online resource (446 p.) |
Disciplina |
572.6
572.636 |
Altri autori (Persone) | RighettiP. G |
Collana | Wiley-Interscience series in mass spectrometry |
Soggetto topico |
Proteins - Spectra
Mass spectrometry Proteomics |
Soggetto genere / forma | Electronic books. |
ISBN |
1-280-27548-0
9786610275489 0-470-24684-7 0-471-70910-7 0-471-70915-8 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
PROTEOMICS TODAY; CONTENTS; PREFACE TO PART I; ACKNOWLEDGMENT; I INTRODUCTION TO PART I; 1 INSTRUMENTATION AND DEVELOPMENTS; 1.1 Introduction; 1.2 Ionization Techniques for Macromolecules; 1.2.1 (252)Cf Plasma Desorption Ionization; 1.2.2 Fast Atom/Ion Bombardment; 1.2.3 Type of Fragment Ions and Nomenclature; 1.3 Examples on Analytical Solutions Based on FAB-MS; 1.3.1 Detection of Abnormalities in Hemoglobin; 1.3.2 Glycoprotein Structure Determination; 1.3.3 Early Scanning Functions on Sector Machines; 1.4 Electrospray Ionization; 1.5 Matrix-Assisted Laser Desorption Ionization
1.5.1 MALDI at High Pressure1.5.2 Desorption Ionization on Silicon (DIOS); 1.5.3 Delayed Extraction; 1.6 Ion Detection; 1.6.1 Microchannel Plates (MCPs); 1.6.2 Cryogenic Detectors; 1.6.2.1 Superconducting Tunnel Junction; 1.6.2.2 Thermal Detectors; 1.7 Types of Analyzers; 1.7.1 Quadrupole Mass Filter; 1.7.2 Three-Dimensional Quadrupole Ion Trap; 1.7.3 Linear Ion Trap; 1.7.4 Time of Flight; 1.7.5 Fourier Transform Ion Cyclotron Resonance; 1.8 Hybrid Analyzers; 1.8.1 Quadrupole Time of Flight; 1.8.2 Ion Mobility-TOF; 1.8.3 Linear Ion Trap-FT-ICR; 1.8.4 Ion Trap-TOF; 1.9 Tandem Mass Spectrometry 1.9.1 Postsource Decay1.9.2 MS-MS Measurements; 1.9.3 Collisional Activation; 1.10 Current MS Instrumentation in Proteome Analyses; 1.10.1 MALDI-TOF; 1.10.2 MALDI-TOF-TOF; 1.10.3 FT-ICR-MS; 1.10.4 ION Mobility-MS; 1.11 Current MS-Based Proteomics; 1.11.1 Delivering Peptides to Ion Source; 1.11.2 Peptide Sequencing and Database Searching; 1.11.3 Peptide Mass Fingerprinting; 1.11.4 Searching with MS-MS Data; 1.11.5 Databases for MS Data Search; 1.12 Recent Achievements and Future Challenges; 1.12.1 Current Applications; 1.12.2 Signal Transduction Pathways; 1.13 Concluding Remarks; References 2 PROTEOMICS IN CANCER RESEARCH2.1 Introduction; 2.1.1 Two-Dimensional Gel Electrophoresis; 2.1.2 Surface-Enhanced Laser Desorption Ionization; 2.1.3 Protein Microarrays; 2.1.4 Getting More Than Just Simple Change in Protein Expression; 2.1.5 Laser Capture Microdissection; 2.2 Pancreatic Ductal Adenocarcinoma; 2.2.1 Analyses Based on Chip Technology; 2.2.2 SELDI Analysis of Pancreatic Ductal Adenocarcinoma; 2.2.3 Protein Profiling Following Treatment with DNA Methylation/Histone Deacetylation Inhibitors; 2.2.4 Proteomic Profiling of PDAC Following Treatment with Trichostatin A 2.2.5 Proteomic Profiling of PDAC Following Treatment with 5 ́-aza-2 ́-deoxycytidine2.3 Proteomic Analysis of Human Breast Carcinoma; 2.3.1 Two-DE Analysis in Breast Cancer; 2.3.2 Proteomic Profiling of Breast Cancer Cell Membranes; 2.3.3 Proteomic Analysis on Selected Tissue Samples; 2.4 Proteomic Profiling of Chemoresistant Cancer Cells; 2.4.1 Protein Alterations in Pancreas Carcinoma Cells Exposed to Anticancer Drug; 2.4.2 Proteomic Profiling of Cervix Squamous Cell Carcinoma Treated with Cisplatin; 2.5 Signal Pathway Profiling of Prostate Cancer 2.6 Emerging Role of Functional and Activity-Based Proteomics in Disease Understanding |
Record Nr. | UNINA-9910144639903321 |
Hamdan Mahmoud <1947-> | ||
Hoboken, N.J., : John Wiley & Sons, 2005 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Proteomics today [[electronic resource] ] : protein assessment and biomarkers using mass spectrometry, 2D electrophoresis, and microarray technology / / Mahmoud Hamdan, Pier Giorgio Righetti |
Autore | Hamdan Mahmoud <1947-> |
Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, 2005 |
Descrizione fisica | 1 online resource (446 p.) |
Disciplina |
572.6
572.636 |
Altri autori (Persone) | RighettiP. G |
Collana | Wiley-Interscience series in mass spectrometry |
Soggetto topico |
Proteins - Spectra
Mass spectrometry Proteomics |
ISBN |
1-280-27548-0
9786610275489 0-470-24684-7 0-471-70910-7 0-471-70915-8 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
PROTEOMICS TODAY; CONTENTS; PREFACE TO PART I; ACKNOWLEDGMENT; I INTRODUCTION TO PART I; 1 INSTRUMENTATION AND DEVELOPMENTS; 1.1 Introduction; 1.2 Ionization Techniques for Macromolecules; 1.2.1 (252)Cf Plasma Desorption Ionization; 1.2.2 Fast Atom/Ion Bombardment; 1.2.3 Type of Fragment Ions and Nomenclature; 1.3 Examples on Analytical Solutions Based on FAB-MS; 1.3.1 Detection of Abnormalities in Hemoglobin; 1.3.2 Glycoprotein Structure Determination; 1.3.3 Early Scanning Functions on Sector Machines; 1.4 Electrospray Ionization; 1.5 Matrix-Assisted Laser Desorption Ionization
1.5.1 MALDI at High Pressure1.5.2 Desorption Ionization on Silicon (DIOS); 1.5.3 Delayed Extraction; 1.6 Ion Detection; 1.6.1 Microchannel Plates (MCPs); 1.6.2 Cryogenic Detectors; 1.6.2.1 Superconducting Tunnel Junction; 1.6.2.2 Thermal Detectors; 1.7 Types of Analyzers; 1.7.1 Quadrupole Mass Filter; 1.7.2 Three-Dimensional Quadrupole Ion Trap; 1.7.3 Linear Ion Trap; 1.7.4 Time of Flight; 1.7.5 Fourier Transform Ion Cyclotron Resonance; 1.8 Hybrid Analyzers; 1.8.1 Quadrupole Time of Flight; 1.8.2 Ion Mobility-TOF; 1.8.3 Linear Ion Trap-FT-ICR; 1.8.4 Ion Trap-TOF; 1.9 Tandem Mass Spectrometry 1.9.1 Postsource Decay1.9.2 MS-MS Measurements; 1.9.3 Collisional Activation; 1.10 Current MS Instrumentation in Proteome Analyses; 1.10.1 MALDI-TOF; 1.10.2 MALDI-TOF-TOF; 1.10.3 FT-ICR-MS; 1.10.4 ION Mobility-MS; 1.11 Current MS-Based Proteomics; 1.11.1 Delivering Peptides to Ion Source; 1.11.2 Peptide Sequencing and Database Searching; 1.11.3 Peptide Mass Fingerprinting; 1.11.4 Searching with MS-MS Data; 1.11.5 Databases for MS Data Search; 1.12 Recent Achievements and Future Challenges; 1.12.1 Current Applications; 1.12.2 Signal Transduction Pathways; 1.13 Concluding Remarks; References 2 PROTEOMICS IN CANCER RESEARCH2.1 Introduction; 2.1.1 Two-Dimensional Gel Electrophoresis; 2.1.2 Surface-Enhanced Laser Desorption Ionization; 2.1.3 Protein Microarrays; 2.1.4 Getting More Than Just Simple Change in Protein Expression; 2.1.5 Laser Capture Microdissection; 2.2 Pancreatic Ductal Adenocarcinoma; 2.2.1 Analyses Based on Chip Technology; 2.2.2 SELDI Analysis of Pancreatic Ductal Adenocarcinoma; 2.2.3 Protein Profiling Following Treatment with DNA Methylation/Histone Deacetylation Inhibitors; 2.2.4 Proteomic Profiling of PDAC Following Treatment with Trichostatin A 2.2.5 Proteomic Profiling of PDAC Following Treatment with 5 ́-aza-2 ́-deoxycytidine2.3 Proteomic Analysis of Human Breast Carcinoma; 2.3.1 Two-DE Analysis in Breast Cancer; 2.3.2 Proteomic Profiling of Breast Cancer Cell Membranes; 2.3.3 Proteomic Analysis on Selected Tissue Samples; 2.4 Proteomic Profiling of Chemoresistant Cancer Cells; 2.4.1 Protein Alterations in Pancreas Carcinoma Cells Exposed to Anticancer Drug; 2.4.2 Proteomic Profiling of Cervix Squamous Cell Carcinoma Treated with Cisplatin; 2.5 Signal Pathway Profiling of Prostate Cancer 2.6 Emerging Role of Functional and Activity-Based Proteomics in Disease Understanding |
Record Nr. | UNINA-9910831066403321 |
Hamdan Mahmoud <1947-> | ||
Hoboken, N.J., : John Wiley & Sons, 2005 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Proteomics today : protein assessment and biomarkers using mass spectrometry, 2D electrophoresis, and microarray technology / / Mahmoud Hamdan, Pier Giorgio Righetti |
Autore | Hamdan Mahmoud <1947-> |
Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, 2005 |
Descrizione fisica | 1 online resource (446 p.) |
Disciplina | 572/.6 |
Altri autori (Persone) | RighettiP. G |
Collana | Wiley-Interscience series in mass spectrometry |
Soggetto topico |
Proteins - Spectra
Mass spectrometry Proteomics |
ISBN |
1-280-27548-0
9786610275489 0-470-24684-7 0-471-70910-7 0-471-70915-8 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
PROTEOMICS TODAY; CONTENTS; PREFACE TO PART I; ACKNOWLEDGMENT; I INTRODUCTION TO PART I; 1 INSTRUMENTATION AND DEVELOPMENTS; 1.1 Introduction; 1.2 Ionization Techniques for Macromolecules; 1.2.1 (252)Cf Plasma Desorption Ionization; 1.2.2 Fast Atom/Ion Bombardment; 1.2.3 Type of Fragment Ions and Nomenclature; 1.3 Examples on Analytical Solutions Based on FAB-MS; 1.3.1 Detection of Abnormalities in Hemoglobin; 1.3.2 Glycoprotein Structure Determination; 1.3.3 Early Scanning Functions on Sector Machines; 1.4 Electrospray Ionization; 1.5 Matrix-Assisted Laser Desorption Ionization
1.5.1 MALDI at High Pressure1.5.2 Desorption Ionization on Silicon (DIOS); 1.5.3 Delayed Extraction; 1.6 Ion Detection; 1.6.1 Microchannel Plates (MCPs); 1.6.2 Cryogenic Detectors; 1.6.2.1 Superconducting Tunnel Junction; 1.6.2.2 Thermal Detectors; 1.7 Types of Analyzers; 1.7.1 Quadrupole Mass Filter; 1.7.2 Three-Dimensional Quadrupole Ion Trap; 1.7.3 Linear Ion Trap; 1.7.4 Time of Flight; 1.7.5 Fourier Transform Ion Cyclotron Resonance; 1.8 Hybrid Analyzers; 1.8.1 Quadrupole Time of Flight; 1.8.2 Ion Mobility-TOF; 1.8.3 Linear Ion Trap-FT-ICR; 1.8.4 Ion Trap-TOF; 1.9 Tandem Mass Spectrometry 1.9.1 Postsource Decay1.9.2 MS-MS Measurements; 1.9.3 Collisional Activation; 1.10 Current MS Instrumentation in Proteome Analyses; 1.10.1 MALDI-TOF; 1.10.2 MALDI-TOF-TOF; 1.10.3 FT-ICR-MS; 1.10.4 ION Mobility-MS; 1.11 Current MS-Based Proteomics; 1.11.1 Delivering Peptides to Ion Source; 1.11.2 Peptide Sequencing and Database Searching; 1.11.3 Peptide Mass Fingerprinting; 1.11.4 Searching with MS-MS Data; 1.11.5 Databases for MS Data Search; 1.12 Recent Achievements and Future Challenges; 1.12.1 Current Applications; 1.12.2 Signal Transduction Pathways; 1.13 Concluding Remarks; References 2 PROTEOMICS IN CANCER RESEARCH2.1 Introduction; 2.1.1 Two-Dimensional Gel Electrophoresis; 2.1.2 Surface-Enhanced Laser Desorption Ionization; 2.1.3 Protein Microarrays; 2.1.4 Getting More Than Just Simple Change in Protein Expression; 2.1.5 Laser Capture Microdissection; 2.2 Pancreatic Ductal Adenocarcinoma; 2.2.1 Analyses Based on Chip Technology; 2.2.2 SELDI Analysis of Pancreatic Ductal Adenocarcinoma; 2.2.3 Protein Profiling Following Treatment with DNA Methylation/Histone Deacetylation Inhibitors; 2.2.4 Proteomic Profiling of PDAC Following Treatment with Trichostatin A 2.2.5 Proteomic Profiling of PDAC Following Treatment with 5 ́-aza-2 ́-deoxycytidine2.3 Proteomic Analysis of Human Breast Carcinoma; 2.3.1 Two-DE Analysis in Breast Cancer; 2.3.2 Proteomic Profiling of Breast Cancer Cell Membranes; 2.3.3 Proteomic Analysis on Selected Tissue Samples; 2.4 Proteomic Profiling of Chemoresistant Cancer Cells; 2.4.1 Protein Alterations in Pancreas Carcinoma Cells Exposed to Anticancer Drug; 2.4.2 Proteomic Profiling of Cervix Squamous Cell Carcinoma Treated with Cisplatin; 2.5 Signal Pathway Profiling of Prostate Cancer 2.6 Emerging Role of Functional and Activity-Based Proteomics in Disease Understanding |
Record Nr. | UNINA-9910877867003321 |
Hamdan Mahmoud <1947-> | ||
Hoboken, N.J., : John Wiley & Sons, 2005 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|