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An introduction to molecular biotechnology : fundamentals, methods, and applications / edited by Michael Wink.
Van Pelt Library TP248.2 .I6813 2021
By Request
- Format:
- Book
- Language:
- English
- Subjects (All):
- Biotechnology.
- Genetic engineering.
- Molecular biology.
- Genetic Engineering.
- Molecular Biology.
- Cell Biology.
- bioengineering.
- molecular biology.
- Medical Subjects:
- Genetic Engineering.
- Biotechnology.
- Molecular Biology.
- Cell Biology.
- Physical Description:
- xxiv, 518 pages : illustrations (some color) ; 28 cm
- Edition:
- Third, completely revised edition.
- Place of Publication:
- Weinheim, Germany : Wiley-VCH, [2021]
- Contents:
- Machine generated contents note: pt. I Fundamentals of Cellular and Molecular Biology
- 1. The Cell as the Basic Unit of Life / Michael Wink
- References
- Further Reading
- 2. Structure and Function of Cellular Macromolecules / Michael Wink
- 2.1. Structure and Function of Sugars
- 2.2. Structure of Membrane Lipids
- 2.3. Structure and Function of Proteins
- 2.4. Structure of Nucleotides and Nucleic Acids (DNA and RNA)
- 3. Structure and Functions of a Cell / Michael Wink
- 3.1. Structure of a Eukaryotic Cell
- 3.1.1. Structure and Function of the Cytoplasmic Membrane
- 3.1.1.1. Membrane Permeability
- 3.1.1.2. Transport Processes Across Biomembranes
- 3.1.1.3. Receptors and Signal Transduction at Biomembranes
- 3.1.2. Endomembrane System in a Eukaryotic Cell
- 3.1.3. Mitochondria and Chloroplasts
- 3.1.4. Cytoplasm
- 3.1.5. Cytoskeleton
- 3.1.6. Cell Walls
- 3.2. Structure of Bacteria
- 3.3. Structure of Viruses
- 3.4. Differentiation of Cells
- 3.5. Cell Death
- 4. Biosynthesis and Function of Macromolecules (DNA, RNA, and Proteins) / Michael Wink
- 4.1. Genomes, Chromosomes, and Replication
- 4.1.1. Genome Size
- 4.1.2. Composition and Function of Chromosomes
- 4.1.3. Mitosis and Meiosis
- 4.1.4. Replication
- 4.1.5. Mutations and Repair Mechanisms
- 4.2. Transcription: From Gene to Protein
- 4.3. Protein Biosynthesis (Translation)
- 5. Distributing Proteins in the Cell (Protein Sorting) / Michael Wink
- 5.1. Import and Export of Proteins via the Nuclear Pore
- 5.2. Import of Proteins in Mitochondria, Chloroplasts, and Peroxisomes
- 5.3. Protein Transport into the Endoplasmic Reticulum
- 5.4. Vesicle Transport from the ER via the Golgi Apparatus to the Cytoplasmic Membrane
- 6. Evolution and Diversity of Organisms / Michael Wink
- 6.1. Prokaryotes
- 6.2. Eukaryotes
- pt. II Standard Methods in Molecular Biotechnology
- 7. Isolation and Purification of Proteins / Thomas Wieland
- 7.1. Introduction
- 7.2. Producing a Protein Extract
- 7.3. Gel Electrophoretic Separation Methods
- 7.3.1. Principles of Electrophoresis
- 7.3.2. Native Gel Electrophoresis
- 7.3.3. Discontinuous Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE)
- 7.3.4. Two-Dimensional (2D) Gel Electrophoresis and Isoelectric Focusing (IEF)
- 7.3.5. Detecting Proteins in Gels
- 7.4. Methods of Protein Precipitation
- 7.5. Column Chromatography Methods
- 7.5.1. General Principles of Separation
- 7.5.1.1. Size Exclusion Chromatography (Gel Filtration)
- 7.5.1.2. Hydrophobic Interaction Chromatography
- 7.5.1.3. Ion Exchange Chromatography
- 7.5.1.4. Hydroxyapatite Chromatography
- 7.5.2. Group-Specific Separation Techniques
- 7.5.2.1. Chromatography on Protein A or Protein G
- 7.5.2.2. Chromatography on Cibacron Blue (Blue Gel)
- 7.5.2.3. Chromatography on Lectins
- 7.5.2.4. Chromatography on Heparin
- 7.5.3. Purification of Recombinant Fusion Proteins
- 7.5.3.1. Chromatography on Chelating Agents
- 7.5.3.2. Chromatography on Glutathione Matrices
- 7.6. Examples
- 7.6.1. Example 1: Purification of Nucleoside Diphosphate Kinase from the Cytosol of Bovine Retina Rod Cells
- 7.6.2. Example 2: Purification of Recombinant His6-RGS16 After Expression in E. coli
- 8. Mass Spectrometry and Applications in Proteomics and Microbial Identification / Wolf D. Lehmann
- 8.1. Principles of ESI and MALDI Mass Spectrometry
- 8.2. Instrumental Setup
- 8.3. Intact Protein Analysis
- 8.3.1. Protein Digestion
- 8.3.2. Peptide Fragmentation
- 8.3.3. Protein Identification with MS/MS Spectra
- 8.4. Protein and Proteome Quantification
- 8.4.1. Label-Free Quantification
- 8.4.2. Chemical Stable Isotope Labeling
- 8.4.3. Metabolic Stable Isotope Labeling
- 8.5. Protein-Protein Interaction Analysis
- 8.6. Analysis of Posttranslational Modifications
- 8.7. Microbial Identification and Resistance Detection
- 9. Isolation of DNA and RNA / Hans Weiher
- 9.1. Introduction
- 9.2. DNA Isolation
- 9.3. RNA Isolation
- 9.3.1. Enrichment of mRNA
- Reference
- 10. Chromatography and Electrophoresis of Nucleic Acids / Hans Weiher
- 10.1. Introduction
- 10.2. Chromatographic Separation of Nucleic Acids
- 10.3. Electrophoresis
- 10.3.1. Agarose Gel Electrophoresis: Submarine Electrophoresis
- 10.3.2. Pulsed-Field Agarose Gel Electrophoresis
- 10.3.3. Polyacrylamide Gel Electrophoresis (PAGE)
- 11. Hybridization of Nucleic Acids / Hans Weiher
- 11.1. Significance of Base Pairing
- 11.2. Experimental Hybridization: Kinetic and Thermodynamic Control
- 11.3. Analytical Techniques
- 11.3.1. Clone Detection, Southern Blotting, Northern Blotting, and Gene Diagnosis
- 11.3.2. Systematic Gene Diagnosis and Expression Screening Based on Gene Arrays
- 11.3.3. In Situ Hybridization
- 12. Use of Enzymes in the Modification of Nucleic Acids / Michael Wink
- 12.1. Restriction Enzymes (Restriction Endonucleases)
- 12.2. Ligases
- 12.3. Methyltransferases
- 12.4. DNA Polymerases
- 12.5. RNA Polymerases and Reverse Transcriptase
- 12.6. Nucleases
- 12.7. T4 Polynucleotide Kinase
- 12.8. Phosphatases
- 13. Polymerase Chain Reaction / Hans Weiher
- 13.1. Introduction
- 13.2. PCR Methods
- 13.2.1. Basic Principle
- 13.2.2. Primer Design and Hot Start PCR
- 13.2.3. Multiplex PCR
- 13.2.4. RT-PCR
- 13.2.5. Qualitative Analysis of the PCR Products
- 13.3. PCR as a Quantitative Method
- 13.3.1. PCR Phases and PCR Efficiency
- 13.3.2. Quantitative Real-Time PCR
- 13.3.3. Digital PCR
- 13.4. Areas of Application
- 13.4.1. Genome Analysis
- 13.4.2. Cloning Techniques
- 13.4.3. Gene Expression Studies
- 14. DNA Sequencing / Hans Weiher
- 14.1. Introduction
- 14.2. The Sanger Method
- 14.3. Pyrosequencing
- 14.4. Second-Generation Sequencing: Illumina and Ion Torrent
- 14.4.1. Overview
- 14.4.2. The Illumina Sequencing System
- 14.4.3. The Ion Torrent Sequencing System
- 14.5. Third-Generation Sequencing Techniques
- 14.5.1. Overview
- 14.5.2. SMRT Sequencing
- 14.5.3. Nanopore Sequencing
- 14.6. The Impact of the DNA Sequencing Technology
- Websites
- 15. Cloning Procedures / Susanne Lutz
- 15.1. Introduction
- 15.2. Construction of Recombinant Vectors
- 15.2.1. Insert
- 15.2.2. Vector
- 15.2.3. Essential Components of Vectors
- 15.2.3.1. Bacterial Origin of Replication (ori)
- 15.2.3.2. Antibiotic Resistance
- 15.2.3.3. Polylinkers
- 15.2.4. Cloning Using Recombination Systems
- 15.2.5. Further Components of Vectors for Prokaryotic Expression Systems
- 15.2.5.1. Promoter
- 15.2.5.2. Ribosome-Binding Site
- 15.2.5.3. Termination Sequence
- 15.2.5.4. Fusion Sequence
- 15.2.6. Further Components of Eukaryotic Expression Vectors
- 15.2.6.1. Eukaryotic Expression Vectors: Yeast
- 15.2.6.2. Eukaryotic Expression Vectors for Mammal Cells
- 15.2.6.3. Viral Expression Systems for Mammalian Cells
- 15.2.7. Nonviral Introduction of Heterologous DNA to Host Organisms (Transformation, Transfection)
- 15.2.7.1. Transformation of Prokaryotes
- 15.2.7.2. Transformation of Yeast Cells
- 15.2.7.3. Transfection of Mammal Cells
- 16. Expression of Recombinant Proteins / Thomas Wieland
- 16.1. Introduction
- 16.2. Expression of Recombinant Proteins in Host Organisms
- 16.2.1. Expression in E. coli
- 16.2.2. Expression in Yeasts
- 16.2.3. Expression in Insect Cells
- 16.2.3.1. Expression Based on Recombinant Baculoviruses
- 16.2.3.2. Expression of Proteins in Stably Transfected Insect Cells
- 16.2.4. Expression of Proteins in Mammalian Cells
- 16.3. Expression in Cell-Free Systems
- 16.3.1. Expression of Proteins in Reticulocyte Lysates
- 16.3.2. Protein Expression Using E. coli Extracts
- 17. Patch Clamp Method / Robert Kraft
- 17.1. Ion Channels
- 17.2. Technical Requirements of the Patch Clamp Method
- 17.3. Patch Clamp Configurations
- 17. A Applications of the Patch Clamp Method
- 18. Cell Cycle Analysis / Stefan Wolfl
- 18.1. Introduction
- 18.2. Analyzing the Cell Cycle
- 18.3. Experimental Analysis of the Cell Cycle
- 18.3.1. Preparing Synchronized Cell Cultures of S. cerevisiae
- 18.3.1.1. Centrifugal Elutriation
- 18.3.1.2. Cell Cycle Arrest Using ot-Factor
- 18.3.2. Identification of Cell Cycle Stages
- 18.3.2.1. Budding Index
- 18.3.2.2. Fluorescent Staining of the Nucleus
- 18.3.2.3. Detection of Cell Cycle Phases Using Fluorescent Proteins as Reporters
- Acknowledgments
- 19. Microscopic Techniques / Stephan Diekmann
- 19.1. Introduction
- 19.2. Electron Microscopy
- 19.2.1. Cryo-electron Microscopy
- 19.2.2. Electron Tomography
- 19.3. Atomic or Scanning Force Microscopy
- 19.3.1. Force Spectroscopy
- 19.3.2. Advantages and Disadvantages
- 19. A Light Microscopy
- 19.4.1. Deconvolution
- 19.4.2. Confocal Microscopy
- 19.4.3. Why Fluorescence?
- 19.4.4. Nanoscopy
- 19.5. Microscopy in the Living Cell
- Contents note continued: 19.5.1. Analysis of Fluorescently Labeled Proteins In Vivo
- 19.5.2. Fluorescence Recovery After Photobleaching
- 19.5.3. Fluorescence Correlation Spectroscopy
- 19.5.4. Forster Resonance Energy Transfer and Fluorescence Lifetime Imaging Microscopy
- 19.5.5. Single-Molecule Fluorescence
- 20. Laser Applications / Rainer Fink
- 20.1. Laser Development: A Historical Perspective
- 20.2. Types of Lasers and Setups
- 20.3. Properties of Laser Radiation
- 20.4. Applications
- 20.4.1. Laser Scanning Microscopy
- 20.4.2. Optical Tweezers
- 20.4.3. Laser Microdissection and Laser Therapy
- 20.4.4. Manufacturing of Products in Medical Technology and Biotechnology Products
- pt. III Key Topics
- 21. Sequencing the Universe of Life / Stefan Wiemann
- 21.1. What to Sequence?
- 21.1.1. Whole-Genome Sequencing
- 21.1.2. Exome Sequencing
- 21.1.3. (Gene) Panel Sequencing
- 21.1.4. RNA Sequencing
- 21.1.4.1. Tag- vs. Full-Length Sequencing
- 21.1.4.2. Sequencing of RNA Species and Modifications
- 21.1.4.3. Sequencing of Single Cells
- 21.1.4.4. In Situ Sequencing
- 21.1.5. (Whole-Genome) Bisulfite Sequencing of DNA
- 21.1.6. Sequencing to Characterize Chromatin Structure and Beyond
- 21.2. Sequencing Projects: Human
- 21.2.1. Initial Sequencing of the Human Genome
- 21.2.2. The 1000 Genomes Project: Assessing Natural Variation
- 21.2.3. Screening for Genetic Disease
- 21.2.4. Sequencing of Populations
- 21.2.5. TCGA and ICGC: Screening for Cancer Driver Mutations
- 21.3. Sequencing Other Species, Environments
- 21.4. Sequencing in the Clinics: Personalizing Oncology
- 21.5. Sequencing in the Private Sector: Direct to Consumer Testing (DTC)
- 21.6. The Information Content of a Genome Sequence and Ethical Consequences
- 22. Cellular Systems Biology / Rainer Konig
- 22.1. Introduction
- 22.2. Analysis of Cellular Networks by Top-Down Approaches
- 22.2.1. Motivation
- 22.2.2. Definitions and Construction of the Networks
- 22.2.3. Gene Set Enrichment Tests
- 22.2. A Inferring Gene Regulators Employing Gene Regulatory Models
- 22.2.5. Network Descriptors
- 22.2.5.1. Scale-Free Networks
- 22.2.5.2. Centrality
- 22.2.5.3. The Clustering Coefficient
- 22.2.6. Detecting Essential Enzymes with a Machine Learning Approach
- 22.2.7. Elementary Flux Modes
- 22.3. Overview over Bottom-Up Modeling of Biochemical Networks
- 22.3.1. Motivation
- 22.3.2. Choosing Model Complexity and Model Building
- 22.3.3. Model Simulation
- 22.3.4. Model Calibration
- 22.3.5. Model Verification and Analysis
- 22.3.6. Examples
- 23. Protein-Protein and Protein-DNA Interactions / Ehmke Pohl
- 23.1. Protein-Protein Interactions
- 23.1.1. Classification and Specificity: Protein Domains
- 23.1.2. Protein Networks and Complexes
- 23.1.3. Structural Properties of Interacting Proteins
- 23.1.4. Which Forces Mediate Protein-Protein Interactions?
- 23.1.4.1. Thermodynamics
- 23.1.4.2. Energetics
- 23.1.5. Methods to Examine Protein-Protein Interactions
- 23.1.6. Theoretical Prediction of Protein-Protein Interactions
- 23.1.7. Regulation of Protein-Protein Interactions
- 23.1.8. Biotechnological and Medical Applications of Protein-Protein Interactions
- 23.2. Protein-DNA Interactions
- 23.2.1. Specific Protein-DNA Interaction
- 23.2.2. Thermodynamic Consideration
- 23.2.3. Methods to Study Protein-DNA Interactions
- 23.2.3.1. Structural Classification of Protein-DNA Complexes
- 23.2.4. Regulatory Networks and System Biology
- 23.2.5. Medical Importance of Protein-DNA Interactions
- 23.2.6. Biotechnological Applications
- 24. Bioinformatics / Benedikt Brors
- 24.1. Introduction
- 24.2. Data Sources
- 24.2.1. Primary Databases: EMBL/GenBank/DDBJ, PIR, and Swiss-Prot
- 24.2.2. Genome Databases: Ensembl and GoldenPath
- 24.2.3. Motif Databases: BLOCKS, PROSITE, Pfam, ProDom, and SMART
- 24.2.4. Molecular Structure Databases: PDB and SCOP
- 24.2.5. Transcriptome Databases: SAGE, ArrayExpress, and GEO
- 24.2.6. Reference Databases: PubMed, OMIM, and GeneCards
- 24.2.7. Pathway Databases and Gene Ontology
- 24.3. Sequence Analysis
- 24.3.1. Kyte-Doolittle Plot, Helical Wheel Analysis, and Signal Sequence Analysis
- 24.3.2. Pairwise Alignment
- 24.3.2.1. Local/Global
- 24.3.2.2. Optimal/Heuristic
- 24.3.3. Alignment Statistics
- 24.3.4. Multiple Alignment
- 24.4. Evolutionary Bioinformatics
- 24.4.1. Statistical Models of Evolution
- 24.4.2. Relation to Score Matrices
- 24.4.3. Phylogenetic Analysis
- 24.5. Gene Prediction
- 24.5.1. Neural Networks or HMMs Based on Hexanucleotide Composition
- 24.5.2. Comparison with Expressed Sequence Tags or Other Genomes (Fugu, Mouse)
- 24.6. Bioinformatics in Transcriptome and Proteome Analysis
- 24.6.1. Preprocessing and Normalization
- 24.6.2. Feature Selection
- 24.6.3. Similarity Measures: Euclidean Distance, Correlation, Manhattan Distance, Mahalanobis Distance, and Entropy Measures
- 24.6.4. Unsupervised Learning Procedures: Clustering, Principal Component Analysis, Multidimensional Scaling, and Correspondence Analysis
- 24.6.5. Supervised Learning Procedures: Linear Discriminant Analysis, Decision Trees, Support Vector Machines, and ANNs
- 24.6.6. Analysis of Overrepresentation of Functional Categories
- 24.7. Analysis of Ultraparallel Sequencing Data
- 24.7.1. Mapping of Ultraparallel Sequencing Data
- 24.7.2. Genome (Re-)sequencing
- 24.7.3. Transcriptome Sequencing
- 24.7.4. ChlP-seq
- 24.7.5. Epigenetic Analysis
- 24.7.6. Single-Cell Analysis
- 24.7.7. Bioethics of Human Sequencing Data
- 24.8. Bioinformatic Software
- 25. Drug Research / Michael Wink
- 25.1. Introduction
- 25.2. Active Compounds and Their Targets
- 25.2.1. Identification of Potential Targets in the Human Genome
- 25.2.2. Comparative Genome Analysis
- 25.2.3. Experimental Target Identification: In Vitro Methods
- 25.2.4. Experimental Identification of Targets: Model Organisms
- 25.2.5. Experimental Target Identification in Humans
- 25.2.6. Difference Between Target Candidates and Genuine Targets
- 25.2.7. Biologicals
- 25.2.8. DNA and RNA in New Therapeutic Approaches
- 25.2.9. Patent Protection for Targets
- 25.2.10. Compound Libraries as a Source of Drug Discovery
- 25.2.11. High-Throughput Screening
- 25.2.12. High-Quality Paramounts in Screening Assays
- 25.2.13. Virtual Ligand Screening
- 25.2.14. Activity of Drugs Described in Terms of Efficacy and Potency
- 25.2.15. Chemical Optimization of Lead Structures
- 25.3. Preclinical Pharmacology and Toxicology
- 25. A Clinical Development
- 25.5. Clinical Testing
- 26. Drug Targeting and Prodrugs / Gert Fricker
- 26.1. Drug Targeting
- 26.1.1. Passive Targeting by Exploiting Special Physiological Properties of the Target Tissue
- 26.1.2. Physical Targeting
- 26.1.3. Active Targeting
- 26.1. A Cellular Carrier Systems
- 26.2. Prodrugs
- 26.2.1. Prodrugs to Improve Drug Solubility
- 26.2.2. Prodrugs to Increase Stability
- 26.3. Penetration of Drugs Through Biological Membranes
- 26. A Prodrugs to Extend Duration of Effect
- 26.5. Prodrugs for the Targeted Release of a Drug
- 26.6. Prodrugs to Minimize Side Effects
- 27. Molecular Diagnostics in Medicine / Reinhard Cessner
- 27.1. Introduction
- 27.2. Uses of Molecular Diagnostics
- 27.2.1. Introduction
- 27.2.2. Monogenic and Polygenic Diseases
- 27.2.3. Individual Variability in the Genome: Forensics
- 27.2.4. Individual Variability in the Genome: HLA Typing
- 27.2.5. Individual Variability in the Genome: Pharmacogenomics
- 27.2.6. Individual Variability in the Genome: Susceptibility to Infectious Diseases
- 27.2.7. Viral Diagnosis
- 27.2.8. Microbial Diagnosis and Resistance Diagnosis
- 27.3. Which Molecular Variations Should be Detected
- 27.3.1. Point Mutations
- 27.3.2. Insertions and Deletions
- 27.3.3. Nucleotide Repeats
- 27.3.4. Deletion or Duplication of Genes
- 27.3.5. Recombination Between Chromosomes
- 27.3.6. Epigenetic Changes
- 27.4. Molecular Diagnostic Methods
- 27.4.1. DNA/RNA Purification
- 27.4.2. Detection of Target Sequence and Known Sequence Variations
- 27.4.2.1. Nucleic Acid Tests
- 27.4.2.2. Quantitative PCR
- 27.4.2.3. Multiplexing of Nucleic Acid Detection: Nucleic Acid Microarrays
- 27.4.2.4. Production and Manufacture of Microarrays
- 27.4.2.5. Applications of Fragment Length Analysis
- 27.4.2.6. Minisequencing
- 27.4.2.7. Determination of Unknown Mutations
- 27.5. Oudook
- Historic Article: "News & Views"
- Reviews
- Web Link
- Textbooks
- 28. Recombinant Antibodies and Phage Display / Stefan Dubel
- 28.1. Introduction
- 28.2. Generation of Specific Recombinant Antibodies
- 28.2.1. Generation of Antibody Gene Libraries
- 28.2.2. Selection Systems for Recombinant Antibodies
- 28.2.2.1. Transgenic Mice with Human IgG Genes
- 28.2.2.2. In Vitro Selection Systems
- 28.3. Production and Purification of Recombinant Antibodies
- 28.4. Features and Applications of Recombinant Antibodies
- 28.4.1. Advantages of Recombinant Antibodies
- 28.4.2. Formats and Applications of Recombinant Antibodies
- Contents note continued: 28.4.2.1. Camelid Antibodies and VH Domains
- 28.4.2.2. scFvanddsFv
- 28.4.2.3. scFv-Fc Fusions, Fc Engineering, and the Addition of Constant Domains
- 28.4.2.4. IgG, Fusion Proteins, and Derivatives for Therapy
- 28.4.2.5. Bispecific Antibodies
- 28.4.2.6. Chimeric Antigen Receptors (CARs)
- 28.4.3. The Future of Therapeutic Antibodies
- 28.4.4. Research and In Vitro Diagnostics
- 28.4.5. Intracellular and Cell-Penetrating Antibodies
- 28.5. Outlook
- 29. Genetically Modified Mice and Their Impact in Medical Research / Mazahir T. Hasan
- 29.1. Overview
- 29.2. Transgenic Mice
- 29.2.1. Retroviral Infection
- 29.2.2. Pronuclear Injection
- 29.3. Homologous Recombination: Knockout (Knock-In) Mice
- 29.4. Endonuclease-Based Knockout Mice
- 29.5. Endonuclease-Based Knock-In Mice
- 29.6. Conditionally Regulated Gene Expression
- 29.7. Gene Transfer to Subpopulations of Cells
- 29.7.1. Electroporation of Mouse Embryos (Plasmid DNA)
- 29.7.2. Virus-Mediated Gene Transfer (Lentivirus, rAAVs)
- 29.7.3. Virus-Mediated Gene Deletion (Cre/lox)
- 29.7.4. Virus-Mediated Gene Knockdown (shRNA, Antagomirs)
- 29.8. Impact of Genetically Modified Mice in Biomedicine
- 29.8.1. Alzheimer's Disease
- 29.8.2. Amyotrophic Lateral Sclerosis (ALS)
- 29.8.3. Psychological and Cognitive Disorders
- 29.8.4. Autism Spectrum Disorder (ASD)
- 29.8.5. Chemogenetics, Optogenetics, and Magnetogenetics
- 29.9. Outiook
- 30. Plant Biotechnology / Rudiger Hell
- 30.1. Introduction
- 30.1.1. Green Genetic Engineering: A New Method Toward Traditional Goals
- 30.1.2. Challenges in Plant Biotechnology
- 30.2. Gene Expression Control and Genome Editing
- 30.2.1. Gene Expression Control
- 30.2.2. Genome Editing
- 30.3. Production of Transgenic Plants
- 30.3.1. Transformation Systems
- 30.3.1.1. Agrobacterium as a Natural Transformation System
- 30.3.1.2. Biolistic Method: Gene Gun
- 30.3.1.3. Plastid Transformation
- 30.3.1.4. Viral Systems
- 30.4. Selection of Transformed Plant Cells
- 30.4.1. Requirements for an Optimal Selection Marker System
- 30.4.2. Negative Selection Marker Systems
- 30.4.3. Positive Selection Marker Systems
- 30.4.4. Selection Systems, Genetic Engineering Safety, and Marker-Free Plants
- 30.5. Regeneration of Transgenic Plants
- 30.5.1. Regeneration Procedures
- 30.5.2. Composition of Regeneration Media
- 30.6. Plant Analysis: Identification and Characterization of Genetically Engineered Plants
- 30.6.1. DNA and RNA Verification
- 30.6.2. Protein Analysis
- 30.6.3. Genetic and Molecular Maps
- 30.6.4. Stability of Transgenic Plants
- 31. Biocatalysis in the Chemical Industry / Bernhard Hauer
- 31.1. Introduction
- 31.2. Bioconversion/Enzymatic Procedures
- 31.3. Development of an Enzyme for Industrial Biocatalysis
- 31.3.1. Identification of Novel Biocatalysts
- 31.3.2. Improvement of Biocatalysts
- 31.3.3. Production of Biocatalysts
- 31.3.4. Oudook
- 31.3.5. Case Study 1: Screening for New Nitrilases
- 31.3.6. Case Study 2: Use of Known Enzymes for New Reactions: Lipases for the Production of Optically Active Amines and Alcohols
- 31.3.7. Case Study 3: Enzyme Optimization with Rational and Evolutive Methods
- 31.4. Fermentative Procedures
- 31.4.1. Improvement of Fermentation Processes
- 31.4.2. Classical Strain Optimization
- 31.4.3. Metabolic Engineering
- 31.4.4. Case Study 4: Fermentative Production of w-Butanol
- 31.4.5. Case Study 5: Production of Glutamic Acid with C. glutamicum
- 31.4.5.1. Molecular Mechanism of Glutamate Overproduction
- 31.4.6. Case Study 6: Production of Lysine with C. glutamicum
- 31.4.6.1. Molecular Mechanism of Lysine Biosynthesis
- 31.4.6.2. Deregulation of the Key Enzyme Aspartate Kinase
- 31.4.7. Genomic Research and Functional Genomics
- 31.4.8. Case Study 7: Fermentative Penicillin Production
- 31.4.9. Case Study 8: Vitamin B2 Production
- 31.4.9.1. Riboflavin Biosynthesis
- 31.4.9.2. Classical Strain Development
- pt. IV Biotechnology in Industry
- 32. Industrial Application: Biotech Industry, Markets, and Opportunities / Julia Schuler
- 32.1. Historical Overview and Definitions of Concepts
- 32.2. Areas of Industrial Application of Molecular Biotechnology
- 32.2.1. Red Biotechnology
- 32.2.1.1. Biopharmaceutical Drug Development
- 32.2.1.2. Gene and Cell Therapy
- 32.2.1.3. Tissue Engineering/Regenerative Medicine
- 32.2.1.4. Pharmacogenomics and Personalized Medicine
- 32.2.1.5. Molecular Diagnostic Agents
- 32.2.1.6. Systems Biology
- 32.2.1.7. Synthetic Biology
- 32.2.2. Green Biotechnology
- 32.2.2.1. Transgenic Plants
- 32.2.2.2. Genomic Approaches in Green Biotechnology
- 32.2.2.3. Novel Food and Functional Food
- 32.2.2.4. Livestock Breeding
- 32.2.3. White Biotechnology
- 32.3. Status Quo of the Biotech Industry Worldwide
- 32.3.1. Global Overview
- 32.3.2. United States
- 32.3.3. Europe
- 33. Patents in the Molecular Biotechnology Industry: Legal and Ethical Issues / David Resnik
- 33.1. Patent Law
- 33.1.1. What is a Patent?
- 33.1.2. How Does One Obtain a Patent?
- 33.1.3. What is the Proper Subject Matter for a Patent?
- 33.1.4. Types of Patents in Pharmaceutical and Molecular Biotechnology
- 33.1.5. Patent Infringement
- 33.1.6. International Patent Law
- 33.2. Ethical and Policy Issues in Biotechnology Patents
- 33.2.1. No Patents on Nature
- 33.2.2. Threats to Human Dignity
- 33.2.3. Problems with Access to Technology
- 33.2.4. Benefit Sharing
- 33.3. Conclusions
- 34. Drug Approval in the European Union and United States / Gary Walsh
- 34.1. Introduction
- 34.2. Regulation Within the European Union
- 34.2.1. The EU Regulatory Framework
- 34.2.2. The EMA and National Competent Authorities
- 34.2.3. New Drug Approval Routes
- 34.2.3.1. The Centralized Procedure
- 34.2.3.2. Decentralized Procedure and Mutual Recognition
- 34.3. Regulation in the United States
- 34.3.1. CDER and CBER
- 34.3.2. The Approvals Procedure
- 34.4. The Advent and Regulation of Biosimilars
- 34.5. International Regulatory Harmonization
- 35. Emergence of a Biotechnology Industry / Claus Kremoser
- 36. The 101 of Founding a Biotech Company / Michael Wink
- 36.1. First Steps Toward Your Own Company
- 36.2. Employees: Recruitment, Remuneration, and Participation
- 37. Marketing / Michael Wink
- 37.1. Introduction
- 37.2. What Types of Deals Are Possible?
- 37.3. What Milestone or License Fees Are Effectively Paid in a Biotech/Pharma Cooperation?
- 37. A PR and IR in Biotech Companies
- Websites.
- Notes:
- Includes bibliographical references and index.
- ISBN:
- 9783527344147
- 3527344144
- OCLC:
- 1057233444
- Publisher Number:
- 99990663521
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