Principles and practice of pharmaceutical medicine / / edited by Lionel D. Edwards, Anthony W. Fox, Peter D. Stonier |
Edizione | [3rd ed.] |
Pubbl/distr/stampa | Oxford, U.K., : Wiley-Blackwell, 2011 |
Descrizione fisica | 1 online resource (801 p.) |
Disciplina | 615/.19 |
Altri autori (Persone) |
EdwardsLionel D
FoxAnthony W. <1956-> StonierP. D |
Soggetto topico |
Drug development
Drugs - Research Pharmacology |
ISBN |
1-4443-4812-4
1-282-88432-8 9786612884320 1-4443-2526-4 1-4443-2527-2 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | section 1. Overview of pharmaceutical medicine -- section 2. Drug discovery and development -- section 3. Special populations and required special studies -- section 4. Applied aspects -- section 5. Drug regulation -- section 6. Medical services -- section 7. Legal and ethical aspects of pharmaceutical medicine -- section 8. Business aspects. |
Record Nr. | UNINA-9910140911403321 |
Oxford, U.K., : Wiley-Blackwell, 2011 | ||
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Lo trovi qui: Univ. Federico II | ||
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Principles of organic medicinal chemistry [[electronic resource] /] / Rama Rao Nadendla |
Autore | Nadendla Rama Rao |
Pubbl/distr/stampa | New Delhi, : New Age International, 2005 |
Descrizione fisica | 1 online resource (331 p.) |
Disciplina | 615/.19 |
Soggetto topico |
Pharmaceutical chemistry
Chemistry, Organic |
Soggetto genere / forma | Electronic books. |
ISBN |
1-281-78890-2
9786611788902 81-224-2485-6 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Cover; Preface; Contents; Chapter 1 Introduction to Medicinal Chemistry; Chapter 2 General Principles of Drug Action; Chapter 3 Physico-chemical Properties of Organic Medicinal Agents; Chapter 4 Chemistry of Prodrugs; Chapter 5 Drug Metabolism; Chapter 6 General Anesthetics; Chapter 7 Sedative-Hypnotic Drugs; Chapter 8 Phychoactive Drugs; Chapater 9 Antiepileptic Agents; Chapter 10 Cholinergic and Anticholinergic Drugs; Chapter 11 Adrenergic Drugs; Chapter 12 Adrenoreceptor Blocking Agents; Chapter 13 Skeletal Muscle Relaxants; Chapter 14 Antihistamines; Chapter 15 Narcotic Analgesics
Chapter 16 Narcotic AntagonistsChapter 17 Antitussives; Chapter 18 Non-Steroidal Antiinflammatory Drugs (NSAIDs); Chapter 19 Local Anesthetics; Chapter 20 Diuretics; Chapter 21 Hypoglycemic Agents; Chapter 22 Thyroid and Antithyroid Drugs; Practice Questions; References; Index |
Record Nr. | UNINA-9910454544503321 |
Nadendla Rama Rao
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New Delhi, : New Age International, 2005 | ||
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Lo trovi qui: Univ. Federico II | ||
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Principles of organic medicinal chemistry / / Rama Rao Nadendla |
Autore | Nadendla Rama Rao |
Pubbl/distr/stampa | New Delhi, : New Age International, 2005 |
Descrizione fisica | 1 online resource (322 pages) : illustrations |
Disciplina | 615/.19 |
Soggetto topico |
Pharmaceutical chemistry
Chemistry, Organic |
ISBN |
1-281-78890-2
9786611788902 81-224-2485-6 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Cover; Preface; Contents; Chapter 1 Introduction to Medicinal Chemistry; Chapter 2 General Principles of Drug Action; Chapter 3 Physico-chemical Properties of Organic Medicinal Agents; Chapter 4 Chemistry of Prodrugs; Chapter 5 Drug Metabolism; Chapter 6 General Anesthetics; Chapter 7 Sedative-Hypnotic Drugs; Chapter 8 Phychoactive Drugs; Chapater 9 Antiepileptic Agents; Chapter 10 Cholinergic and Anticholinergic Drugs; Chapter 11 Adrenergic Drugs; Chapter 12 Adrenoreceptor Blocking Agents; Chapter 13 Skeletal Muscle Relaxants; Chapter 14 Antihistamines; Chapter 15 Narcotic Analgesics
Chapter 16 Narcotic Antagonists; Chapter 17 Antitussives; Chapter 18 Non-Steroidal Antiinflammatory Drugs (NSAIDs); Chapter 19 Local Anesthetics; Chapter 20 Diuretics; Chapter 21 Hypoglycemic Agents; Chapter 22 Thyroid and Antithyroid Drugs; Practice Questions; References; Index |
Record Nr. | UNINA-9910782798403321 |
Nadendla Rama Rao
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||
New Delhi, : New Age International, 2005 | ||
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Lo trovi qui: Univ. Federico II | ||
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Principles of organic medicinal chemistry / / Rama Rao Nadendla |
Autore | Nadendla Rama Rao |
Edizione | [1st ed.] |
Pubbl/distr/stampa | New Delhi, : New Age International, 2005 |
Descrizione fisica | 1 online resource (322 pages) : illustrations |
Disciplina | 615/.19 |
Soggetto topico |
Pharmaceutical chemistry
Chemistry, Organic |
ISBN |
1-281-78890-2
9786611788902 81-224-2485-6 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Cover; Preface; Contents; Chapter 1 Introduction to Medicinal Chemistry; Chapter 2 General Principles of Drug Action; Chapter 3 Physico-chemical Properties of Organic Medicinal Agents; Chapter 4 Chemistry of Prodrugs; Chapter 5 Drug Metabolism; Chapter 6 General Anesthetics; Chapter 7 Sedative-Hypnotic Drugs; Chapter 8 Phychoactive Drugs; Chapater 9 Antiepileptic Agents; Chapter 10 Cholinergic and Anticholinergic Drugs; Chapter 11 Adrenergic Drugs; Chapter 12 Adrenoreceptor Blocking Agents; Chapter 13 Skeletal Muscle Relaxants; Chapter 14 Antihistamines; Chapter 15 Narcotic Analgesics
Chapter 16 Narcotic Antagonists; Chapter 17 Antitussives; Chapter 18 Non-Steroidal Antiinflammatory Drugs (NSAIDs); Chapter 19 Local Anesthetics; Chapter 20 Diuretics; Chapter 21 Hypoglycemic Agents; Chapter 22 Thyroid and Antithyroid Drugs; Practice Questions; References; Index |
Record Nr. | UNINA-9910809824103321 |
Nadendla Rama Rao
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New Delhi, : New Age International, 2005 | ||
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Lo trovi qui: Univ. Federico II | ||
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Process scale purification of antibodies [[electronic resource] /] / edited by Uwe Gottschalk |
Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, c2009 |
Descrizione fisica | 1 online resource (458 p.) |
Disciplina | 615/.19 |
Altri autori (Persone) | GottschalkUwe |
Soggetto topico |
Monoclonal antibodies - Purification
Biochemical engineering |
ISBN |
1-118-21074-3
1-282-00919-2 9786612009198 0-470-44489-4 0-470-44488-6 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
PROCESS SCALE PURIFICATION OF ANTIBODIES; CONTENTS; Preface; About the Author; Contributors; 1 Downstream Processing of Monoclonal Antibodies: Current Practices and Future Opportunities; 1.1 Introduction; 1.2 A Brief History of cGMP mAb and Intravenous Immunoglobulin (IgIV) Purification; 1.3 Current Approaches in Purification Process Development: Impact of Platform Processes; 1.4 Typical Unit Operations and Processing Alternatives; 1.5 VLS Processes: Ton-Scale Production and Beyond; 1.6 Process Validation; 1.7 Product Life Cycle Management; 1.8 Future Opportunities; 1.9 Conclusions
1.10 Acknowledgments1.11 References; 2 The Development of Antibody Purification Technologies; 2.1 Introduction; 2.2 Chromatographic Purification of Antibodies before Protein A; 2.3 Antibody Purification after 1975; 2.4 Additional Technologies for Antibody Purification; 2.5 Purification of mAbS Approved in North America and in Europe; 2.6 Acknowledgments; 2.7 References; 3 Harvest and Recovery of Monoclonal Antibodies: Cell Removal and Clarification; 3.1 Introduction; 3.2 Centrifugation; 3.3 Microfiltration; 3.4 Depth Filtration; 3.5 Flocculation; 3.6 Absolute Filtration 3.7 Expanded-Bed Chromatography3.8 Comparison of Harvest and Clarification Unit Operations; 3.9 Acknowledgments; 3.10 References; 4 Protein A-Based Affinity Chromatography; 4.1 Introduction; 4.2 Properties of Protein A and Commercially Available Protein A Resins; 4.2.1 Protein A Structure; 4.2.2 Protein A-Immunoglobulin G (IgG) Interaction; 4.2.3 Stoichiometry of Protein A-IgG Binding; 4.2.4 Protein A Stability; 4.2.5 Commercial Protein A Resins; 4.2.6 Static Capacity; 4.2.7 DBC; 4.2.8 Leaching; 4.2.9 Production Rates; 4.3 Protein A Chromatography Step Development; 4.3.1 Loading/Binding 4.3.2 Wash Development4.3.3 Elution; 4.3.4 Stripping; 4.3.5 Regeneration and CIP; 4.4 Additional Considerations During Development and Scale-Up; 4.4.1 Controlling HMW Formation; 4.4.2 Removal of Soluble HMW Contaminants; 4.4.3 Turbidity; 4.5 Virus Removal/Inactivation; 4.5.1 Virus Removal; 4.5.2 Low-pH Inactivation; 4.5.3 Bovine/Transmissible Spongiform Encephalopathy (BSE/TSE) Clearance; 4.6 Validation and Robustness; 4.6.1 Validation; 4.6.2 Robustness; 4.7 Conclusions; 4.8 Acknowledgments; 4.9 References; 5 Purification of Human Monoclonal Antibodies: Non-Protein A Strategies 5.1 Introduction5.2 Integrated Process Designs for Human Monoclonal Antibody (HuMab) Production; 5.3 Purification Process Designs for HuMabs; 5.3.1 Protein A Purification Schemes; 5.3.2 Non-Protein A Purification Schemes; 5.3.3 Host Cell Protein (HCP) Exclusion Approach for Ion-Exchange Purification Schemes; 5.4 Conclusions; 5.5 Acknowledgments; 5.6 References; 6 Purification of Monoclonal Antibodies by Mixed-Mode Chromatography; 6.1 Introduction; 6.2 A Brief History; 6.3 Prerequisites for Industrial Implementation; 6.4 Mechanisms, Screening, and Method Development; 6.5 Capture Applications 6.6 Polishing Applications |
Record Nr. | UNINA-9910782895903321 |
Hoboken, N.J., : John Wiley & Sons, c2009 | ||
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Lo trovi qui: Univ. Federico II | ||
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Process scale purification of antibodies / / edited by Uwe Gottschalk |
Edizione | [1st ed.] |
Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, c2009 |
Descrizione fisica | 1 online resource (458 p.) |
Disciplina | 615/.19 |
Altri autori (Persone) | GottschalkUwe |
Soggetto topico |
Monoclonal antibodies - Purification
Biochemical engineering |
ISBN |
1-118-21074-3
1-282-00919-2 9786612009198 0-470-44489-4 0-470-44488-6 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
PROCESS SCALE PURIFICATION OF ANTIBODIES; CONTENTS; Preface; About the Author; Contributors; 1 Downstream Processing of Monoclonal Antibodies: Current Practices and Future Opportunities; 1.1 Introduction; 1.2 A Brief History of cGMP mAb and Intravenous Immunoglobulin (IgIV) Purification; 1.3 Current Approaches in Purification Process Development: Impact of Platform Processes; 1.4 Typical Unit Operations and Processing Alternatives; 1.5 VLS Processes: Ton-Scale Production and Beyond; 1.6 Process Validation; 1.7 Product Life Cycle Management; 1.8 Future Opportunities; 1.9 Conclusions
1.10 Acknowledgments1.11 References; 2 The Development of Antibody Purification Technologies; 2.1 Introduction; 2.2 Chromatographic Purification of Antibodies before Protein A; 2.3 Antibody Purification after 1975; 2.4 Additional Technologies for Antibody Purification; 2.5 Purification of mAbS Approved in North America and in Europe; 2.6 Acknowledgments; 2.7 References; 3 Harvest and Recovery of Monoclonal Antibodies: Cell Removal and Clarification; 3.1 Introduction; 3.2 Centrifugation; 3.3 Microfiltration; 3.4 Depth Filtration; 3.5 Flocculation; 3.6 Absolute Filtration 3.7 Expanded-Bed Chromatography3.8 Comparison of Harvest and Clarification Unit Operations; 3.9 Acknowledgments; 3.10 References; 4 Protein A-Based Affinity Chromatography; 4.1 Introduction; 4.2 Properties of Protein A and Commercially Available Protein A Resins; 4.2.1 Protein A Structure; 4.2.2 Protein A-Immunoglobulin G (IgG) Interaction; 4.2.3 Stoichiometry of Protein A-IgG Binding; 4.2.4 Protein A Stability; 4.2.5 Commercial Protein A Resins; 4.2.6 Static Capacity; 4.2.7 DBC; 4.2.8 Leaching; 4.2.9 Production Rates; 4.3 Protein A Chromatography Step Development; 4.3.1 Loading/Binding 4.3.2 Wash Development4.3.3 Elution; 4.3.4 Stripping; 4.3.5 Regeneration and CIP; 4.4 Additional Considerations During Development and Scale-Up; 4.4.1 Controlling HMW Formation; 4.4.2 Removal of Soluble HMW Contaminants; 4.4.3 Turbidity; 4.5 Virus Removal/Inactivation; 4.5.1 Virus Removal; 4.5.2 Low-pH Inactivation; 4.5.3 Bovine/Transmissible Spongiform Encephalopathy (BSE/TSE) Clearance; 4.6 Validation and Robustness; 4.6.1 Validation; 4.6.2 Robustness; 4.7 Conclusions; 4.8 Acknowledgments; 4.9 References; 5 Purification of Human Monoclonal Antibodies: Non-Protein A Strategies 5.1 Introduction5.2 Integrated Process Designs for Human Monoclonal Antibody (HuMab) Production; 5.3 Purification Process Designs for HuMabs; 5.3.1 Protein A Purification Schemes; 5.3.2 Non-Protein A Purification Schemes; 5.3.3 Host Cell Protein (HCP) Exclusion Approach for Ion-Exchange Purification Schemes; 5.4 Conclusions; 5.5 Acknowledgments; 5.6 References; 6 Purification of Monoclonal Antibodies by Mixed-Mode Chromatography; 6.1 Introduction; 6.2 A Brief History; 6.3 Prerequisites for Industrial Implementation; 6.4 Mechanisms, Screening, and Method Development; 6.5 Capture Applications 6.6 Polishing Applications |
Record Nr. | UNINA-9910819255503321 |
Hoboken, N.J., : John Wiley & Sons, c2009 | ||
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Lo trovi qui: Univ. Federico II | ||
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Prokaryotic toxin-antitoxins / / Kenn Gerdes, editor |
Pubbl/distr/stampa | Heidelberg, : Springer, 2013 |
Descrizione fisica | 1 online resource (362 p.) |
Disciplina | 615/.19 |
Altri autori (Persone) | GerdesKenn |
Soggetto topico |
Toxins
Medical microbiology |
ISBN | 3-642-33253-6 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | Introduction -- Type I Toxin – Antitoxin Systems: Hok/Sok and Fst -- Novel Type I Toxin – Antitoxin Systems -- Type II TA Loci: The Ccdab and Parde Families -- Type II TA Loci: The Relbe Family -- Type II TA Loci: The Unusual Mqsra Locus -- Type II TA Loci: The Mazef Family -- Type II TA Loci: Vapbc and Other TA Loci In Mycobacteria -- Type II TA Loci: Phd Doc Family -- Type II TA Loci: The Fic Family -- Type II TA Loci, Hipab And Persisters -- Type II TA Loci: Zeta/Pezt Family -- Type II Loci: Phylogeny -- Type III TA Loci -- TA Loci Encoded By Plasmids -- TA Loci in Archaea -- TA Loci in Mycobacterium Tuberculosis -- TA Loci in Streptococcus Pneumoniae -- Biotechnological and Medical Exploitations Of TA Genes and Their Components. |
Record Nr. | UNINA-9910437845303321 |
Heidelberg, : Springer, 2013 | ||
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Lo trovi qui: Univ. Federico II | ||
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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 | ||
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Lo trovi qui: Univ. Federico II | ||
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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 | ||
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Lo trovi qui: Univ. Federico II | ||
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Protein crystallography in drug discovery [[electronic resource] /] / edited by R.E. Babine and S.S. Abdel-Meguid |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2004 |
Descrizione fisica | 1 online resource (280 p.) |
Disciplina | 615/.19 |
Altri autori (Persone) |
BabineR. E (Robert E.)
Abdel-MeguidS. S |
Collana | Methods and principles in medicinal chemistry |
Soggetto topico |
Proteins
X-ray crystallography Drug development |
Soggetto genere / forma | Electronic books. |
ISBN |
1-280-56064-9
9786610560646 3-527-60635-1 3-527-60187-2 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Protein Crystallography in Drug Discovery; Contents; Preface; A Personal Foreword; List of Contributors; 1 Molecular Recognition of Nuclear Hormone Receptor-Ligand Complexes; 1.1 Introduction; 1.1.1 Nuclear Hormone Receptors: Ligand Binding Domains; 1.1.2 Dimerization and Interactions with Co-activators and Co-repressors; 1.2 Steroid Receptors; 1.2.1 The Role of the Ligand; 1.2.1.1 Estradiol Estrogen Receptor Complex; 1.2.1.2 Other Estrogen Receptor Agonists Complexes; 1.2.1.3 Estrogen Receptor Antagonists Complexes; 1.2.1.4 Genistein - An ER-β Partial Agonist
1.2.1.5 R,R-5,11-cis-Diethyl-5,6,11,12-tetrahydrochrysene-2,8-diol: An ER-α Agonist and ER-β Antagonist1.2.2 Structural Basis for Agonism and Antagonism and Partial Agonism: The Role of the Ligand; 1.2.3 Progesterone/Progesterone Receptor Complex; 1.2.4 Androgen Receptor Complexes; 1.2.5 Glucocorticoid Receptor; 1.2.6 Steroid Ligand Selectivity; 1.3 The Vitamin D Receptor-Ligand Complexes; 1.4 The Retinoic Acid Receptors RAR and RXR; 1.4.1 Introduction; 1.4.2 RAR-γ and RXR-α Retinoid Complexes; 1.4.3 Selectivity of RAR Ligands and RAR Isotypes; 1.4.4 RXR Complexes with Unnatural Ligands 1.5 PPAR: Isotype-Selective Ligands1.6 Summary; 1.7 Acknowledgements; 1.8 References; 2 Kinases; 2.1 Introduction; 2.2 Structure and Function; 2.2.1 Tertiary Structure; 2.2.2 Catalysis and Substrate Binding; 2.2.3 Regulation and Conformational Flexibility; 2.2.3.1 Activation Loop Conformation; 2.2.3.2 Glycine Rich Loop; 2.2.3.3 C-Helix Orientation; 2.2.3.4 Lobe Orientation; 2.2.3.5 Solvent Channel; 2.3 Crystallization; 2.3.1 Defining the Construct; 2.3.2 Mutagenesis; 2.3.3 Phosphorylation; 2.4 Inhibitor Design; 2.4.1 Binding in ATP Cleft; 2.4.1.1 ATP Binding Sites 2.4.1.2 Gatekeeper-Dependent Binding Pocket2.4.1.3 Lipophilic Plug; 2.4.1.4 Polar Surface Site; 2.4.2 Conformational Considerations; 2.4.2.1 Inhibitor-Induced Binding; 2.4.2.2 What is the Most Appropriate Enzyme Form for Crystallography?; 2.4.2.3 Homology Models and Surrogate Kinases; 2.4.3 Paradigms for Kinase Drug Discovery; 2.4.3.1 High Throughput Screening; 2.4.3.2 Structure-Based Design; 2.4.3.3 Mechanism-Based and Ligand Mimetic Design; 2.4.3.4 Computational Chemistry and Virtual Screening; 2.4.4 Selectivity; 2.5 Conclusion; 2.6 References; 3 The Proteasome as a Drug Target 3.1 Introduction3.2 The Ubiquitin-Proteasome System; 3.2.1 Role of the Ubiquitin-Proteasome System; 3.2.2 26S Proteasome; 3.2.3 20S Proteasome; 3.3 Structure of the 20S Proteasome; 3.3.1 Active Sites of Eukaryotic 20S Proteasomes; 3.3.2 Novel Ntn-Hydrolase Active Site of the β7 Subunit; 3.3.3 Predicted Structure of Immunoproteasome and Substrate Specificities; 3.4 Proteasome Inhibitors; 3.4.1 Structure of Proteasome Inhibitor Complexes; 3.5 Conclusions; 3.6 Acknowledgements; 3.7 References; 4 Antibiotics and the Ribosome; 4.1 Introduction; 4.2 The Ribosome; 4.2.1 Introduction 4.2.2 Binding of tRNA |
Record Nr. | UNINA-9910146237403321 |
Weinheim, : Wiley-VCH, c2004 | ||
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Lo trovi qui: Univ. Federico II | ||
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