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1.

図書

図書
Brian R. Eggins
出版情報: Chichester, West Sussex : Wiley, c2002  xxi, 273 p. ; 23 cm
シリーズ名: Analytical Techniques in the Sciences(AnTS)
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Series Preface
Preface
Acronyms, Abbreviations and Symbols
About the Author
Introduction / 1:
Introduction to Sensors / 1.1:
What are Sensors? / 1.1.1:
The Nose as a Sensor / 1.1.2:
Sensors and Biosensors--Definitions / 1.2:
Aspects of Sensors / 1.3:
Recognition Elements / 1.3.1:
Transducers--the Detector Device / 1.3.2:
Methods of Immobilization / 1.3.3:
Performance Factors / 1.3.4:
Areas of Application / 1.3.5:
Transduction Elements / 2:
Electrochemical Transducers--Introduction / 2.1:
Potentiometry and Ion-Selective Electrodes: The Nernst Equation / 2.2:
Cells and Electrodes / 2.2.1:
Reference Electrodes / 2.2.2:
Quantitative Relationships: The Nernst Equation / 2.2.3:
Practical Aspects of Ion-Selective Electrodes / 2.2.4:
Measurement and Calibration / 2.2.5:
Voltammetry and Amperometry / 2.3:
Linear-Sweep Voltammetry / 2.3.1:
Cyclic Voltammetry / 2.3.2:
Chronoamperometry / 2.3.3:
Amperometry / 2.3.4:
Kinetic and Catalytic Effects / 2.3.5:
Conductivity / 2.4:
Field-Effect Transistors / 2.5:
Semiconductors--Introduction / 2.5.1:
Semiconductor--Solution Contact / 2.5.2:
Field-Effect Transistor / 2.5.3:
Modified Electrodes, Thin-Film Electrodes and Screen-Printed Electrodes / 2.6:
Thick-Film--Screen-Printed Electrodes / 2.6.1:
Microelectrodes / 2.6.2:
Thin-Film Electrodes / 2.6.3:
Photometric Sensors / 2.7:
Optical Techniques / 2.7.1:
Ultraviolet and Visible Absorption Spectroscopy / 2.7.3:
Fluorescence Spectroscopy / 2.7.4:
Luminescence / 2.7.5:
Optical Transducers / 2.7.6:
Device Construction / 2.7.7:
Solid-Phase Absorption Label Sensors / 2.7.8:
Applications / 2.7.9:
Further Reading
Sensing Elements / 3:
Ionic Recognition / 3.1:
Ion-Selective Electrodes--Introduction / 3.2.1:
Interferences / 3.2.2:
Conducting Devices / 3.2.3:
Modified Electrodes and Screen-Printed Electrodes / 3.2.4:
Molecular Recognition--Chemical Recognition Agents / 3.3:
Thermodynamic--Complex Formation / 3.3.1:
Kinetic--Catalytic Effects: Kinetic Selectivity / 3.3.2:
Molecular Size / 3.3.3:
Molecular Recognition--Spectroscopic Recognition / 3.4:
Infrared Spectroscopy--Molecular / 3.4.1:
Ultraviolet Spectroscopy--Less Selective / 3.4.3:
Nuclear Magnetic Resonance Spectroscopy--Needs Interpretation / 3.4.4:
Mass Spectrometry / 3.4.5:
Molecular Recognition--Biological Recognition Agents / 3.5:
Enzymes / 3.5.1:
Tissue Materials / 3.5.3:
Micro-Organisms / 3.5.4:
Mitochondria / 3.5.5:
Antibodies / 3.5.6:
Nucleic Acids / 3.5.7:
Receptors / 3.5.8:
Immobilization of Biological Components / 3.6:
Adsorption / 3.6.1:
Microencapsulation / 3.6.3:
Entrapment / 3.6.4:
Cross-Linking / 3.6.5:
Covalent Bonding / 3.6.6:
Selectivity / 4:
Ion-Selective Electrodes / 4.2.1:
Others / 4.2.2:
Sensitivity / 4.3:
Range, Linear Range and Detection Limits / 4.3.1:
Time Factors / 4.4:
Response Times / 4.4.1:
Recovery Times / 4.4.2:
Lifetimes / 4.4.3:
Precision, Accuracy and Repeatability / 4.5:
Different Biomaterials / 4.6:
Different Transducers / 4.7:
Urea Biosensors / 4.7.1:
Amino Acid Biosensors / 4.7.2:
Glucose Biosensors / 4.7.3:
Uric Acid / 4.7.4:
Some Factors Affecting the Performance of Sensors / 4.8:
Amount of Enzyme / 4.8.1:
Immobilization Method / 4.8.2:
pH of Buffer / 4.8.3:
Electrochemical Sensors and Biosensors / 5:
Potentiometric Sensors--Ion-Selective Electrodes / 5.1:
Concentrations and Activities / 5.1.1:
Calibration Graphs / 5.1.2:
Examples of Ion-Selective Electrodes / 5.1.3:
Gas Sensors--Gas-Sensing Electrodes / 5.1.4:
Potentiometric Biosensors / 5.2:
pH-Linked / 5.2.1:
Ammonia-Linked / 5.2.2:
Carbon Dioxide-Linked / 5.2.3:
Iodine-Selective / 5.2.4:
Silver Sulfide-Linked / 5.2.5:
Amperometric Sensors / 5.3:
Direct Electrolytic Methods / 5.3.1:
The Three Generations of Biosensors / 5.3.2:
First Generation--The Oxygen Electrode / 5.3.3:
Second Generation--Mediators / 5.3.4:
Third Generation--Directly Coupled Enzyme Electrodes / 5.3.5:
NADH/NAD[superscript +] / 5.3.6:
Examples of Amperometric Biosensors / 5.3.7:
Amperometric Gas Sensors / 5.3.8:
Conductometric Sensors and Biosensors / 5.4:
Chemiresistors / 5.4.1:
Biosensors Based on Chemiresistors / 5.4.2:
Semiconducting Oxide Sensors / 5.4.3:
Applications of Field-Effect Transistor Sensors / 5.5:
Chemically Sensitive Field-Effect Transistors (CHEMFETs) / 5.5.1:
Ion-Selective Field-Effect Transistors (ISFETs) / 5.5.2:
FET-Based Biosensors (ENFETs) / 5.5.3:
Photometric Applications / 6:
Techniques for Optical Sensors / 6.1:
Modes of Operation of Waveguides in Sensors / 6.1.1:
Immobilized Reagents / 6.1.2:
Visible Absorption Spectroscopy / 6.2:
Measurement of pH / 6.2.1:
Measurement of Carbon Dioxide / 6.2.2:
Measurement of Ammonia / 6.2.3:
Examples That Have Been Used in Biosensors / 6.2.4:
Fluorescent Reagents / 6.3:
Fluorescent Reagents for pH Measurements / 6.3.1:
Halides / 6.3.2:
Sodium / 6.3.3:
Potassium / 6.3.4:
Gas Sensors / 6.3.5:
Indirect Methods Using Competitive Binding / 6.4:
Reflectance Methods--Internal Reflectance Spectroscopy / 6.5:
Evanescent Waves / 6.5.1:
Reflectance Methods / 6.5.2:
Attenuated Total Reflectance / 6.5.3:
Total Internal Reflection Fluorescence / 6.5.4:
Surface Plasmon Resonance / 6.5.5:
Light Scattering Techniques / 6.6:
Types of Light Scattering / 6.6.1:
Quasi-Elastic Light Scattering Spectroscopy / 6.6.2:
Photon Correlation Spectroscopy / 6.6.3:
Laser Doppler Velocimetry / 6.6.4:
Mass-Sensitive and Thermal Sensors / 7:
The Piezo-Electric Effect / 7.1:
Principles / 7.1.1:
Gas Sensor Applications / 7.1.2:
Biosensor Applications / 7.1.3:
The Quartz Crystal Microbalance / 7.1.4:
Surface Acoustic Waves / 7.2:
Plate Wave Mode / 7.2.1:
Evanescent Wave Mode / 7.2.2:
Lamb Mode / 7.2.3:
Thickness Shear Mode / 7.2.4:
Thermal Sensors / 7.3:
Thermistors / 7.3.1:
Catalytic Gas Sensors / 7.3.2:
Thermal Conductivity Devices / 7.3.3:
Specific Applications / 8:
Determination of Glucose in Blood--Amperometric Biosensor / 8.1:
Survey of Biosensor Methods for the Determination of Glucose / 8.1.1:
Aim / 8.1.2:
Determination of Nanogram Levels of Copper(I) in Water Using Anodic Stripping Voltammetry, Employing an Electrode Modified with a Complexing Agent / 8.2:
Background to Stripping Voltammetry--Anodic and Cathodic / 8.2.1:
Determination of Several Ions Simultaneously--'The Laboratory on a Chip' / 8.2.2:
Sensor Arrays and 'Smart' Sensors / 8.3.1:
Background to Ion-Selective Field-Effect Transistors / 8.3.3:
Determination of Attomole Levels of a Trinitrotoluene--Antibody Complex with a Luminescent Transducer / 8.3.4:
Background to Immuno--Luminescent Assays / 8.4.1:
Determination of Flavanols in Beers / 8.4.2:
Background / 8.5.1:
Responses to Self-Assessment Questions / 8.5.2:
Bibliography
Glossary of Terms
SI Units and Physical Constants
Periodic Table
Index
Series Preface
Preface
Acronyms, Abbreviations and Symbols
2.

図書

図書
edited by Astrid Sigel and Helmut Sigel
出版情報: New York : Marcel Dekker, c2002  lix, 810 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 39
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Preface to the Series
Preface to Volume 39
In Memoriam of Professor Robert C. Bray
Contributors
Contents of Previous Volumes
Handbook on Toxicity of Inorganic Compounds
Handbook on Metals in Clinical and Analytical Chemistry
Handbook on Metalloproteins
The Biogeochemistry of Molybdenum and Tungsten / Edward I. StiefelChapter 1:
Introduction / 1.:
Molybdenum and Tungsten in the Environment / 2.:
The Nitrogen Cycle / 3.:
Sulfur Metabolism and the Sulfur Cycle / 4.:
Carbon Metabolism / 5.:
Arsenic, Selenium, and Chlorine Metabolism / 6.:
Conclusion / 7.:
Acknowledgment
Abbreviations
References
Transport, Homeostasis, Regulation, and Binding of Molybdate and Tungstate to Proteins / Richard N. Pau ; David M. LawsonChapter 2:
Competition with Iron(III)
Transport Systems
Cytoplasmic Molybdate-Binding Proteins
Conclusions
Acknowledgments
Abbreviations and Definitions
Molybdenum Nitrogenases: A Crystallographic and Mechanistic View / Barry E. SmithChapter 3:
The Nitrogenases
The Molybdenum-Iron Protein
The Iron Protein
Mechanistic Studies
The Nitrogenase Complex
The Active Site
Chemical Dinitrogen Fixation by Molybdenum and Tungsten Complexes: Insights From Coordination Chemistry / Masanobu Hidai ; Yasushi Mizobe8.:
Preparation and Structures of Dinitrogen Complexes
Reactions of Coordinated Dinitrogen
Biosynthesis of the Nitrogenase Iron-Molybdenum-Cofactor From Azotobacter Vinelandii / Jeverson Frazzon ; Dennis R. DeanChapter 5:
Biochemical Genetic Analysis of FeMo Cofactor Biosynthesis
A General Model for FeMo Cofactor Biosynthesis
Mobilization of Iron and Sulfur
NifB Cofactor
The NifEN Complex
Homocitrate Formation and Molybdenum Insertion
Role of Intermediate Carriers in FeMo Cofactor Biosynthesis
Role of the Iron Protein in Cofactor Assembly / 9.:
Summary and Future Prospects / 10.:
Molybdenum Enzymes Containing the Pyranopterin Cofactor: an Overview / Russ HilleChapter 6:
Classification of the Mononuclear Molybdenum Enzymes
Consideration of Selected Enzymes Not Covered in Other Chapters
Mechanistic Considerations
Concluding Remarks
The Molybdenum and Tungsten Cofactors: A Crystallographic View / Holger Dobbek ; Robert HuberChapter 7:
Structure of the Mo/W Cofactor
Moco-Containing Enzyme Families
Limitations of a Crystallographic Model
Models for the Pyranopterin-Containing Molybdenum and Tungsten Cofactors / Berthold Fischer ; Sharon J. Nieter BurgmayerChapter 8:
Early Models
Model Complexes of 1,2-Ene-Dithiolates
Metal Complexes of Pterins
Models with All Three Redox Sites
Biosynthesis and Molecular Biology of the Molybdenum Cofactor (Moco) / Ralf R. Mendel ; Gunter SchwarzChapter 9:
Genetics of the Molybdenum Cofactor
Biosynthesis of the Molybdenum Cofactor
Regulation of Molybdenum Cofactor Synthesis
Molybdenum in Nitrate Reductase and Nitrite Oxidoreductase / Peter M. H. Kroneck ; Dietmar J. AbtChapter 10:
Bacterial Respiratory Chains, Metalloenzymes, and Bioenergetics
Nitrate Reductase
Nitrite Oxidoreductase
Environmental Aspects and Biosensors
The Molybdenum-Containing Hydroxylases of Nicotinate, Isonicotinate, and Nicotine / Jan R. Andreesen ; Susanne FetznerChapter 11:
Hydroxylations of Nicotinate and Derivatives
Catabolism of Isonicotinate and Derivatives
Nicotine Catabolism: Enzymes and Genes Involved in Aerobic Transformations
Biotechnological Potentials and Medical Implications
The Molybdenum-Containing Xanthine Oxidoreductases and Picolinate Dehydrogenases / Emil F. Pai ; Takeshi NishinoChapter 12:
Xanthine Dehydrogenase/Xanthine Oxidase
Picolinate Dehydrogenase
Enzymes of the Xanthine Oxidase Family: the Role of Molybdenum / David J. LoweChapter 13:
The Reactions Catalyzed
Spectroscopic Investigations
Kinetic Studies
Theoretical Calculations
Discussion
The Molybdenum-Containing Hydroxylases of Quinoline, Isoquinoline, and Quinaldine / Reinhard Kappl ; Jurgen HuttermannChapter 14:
Biochemical and Genetic Characterization
Structural Features of Related Enzymes
EPR and ENDOR Characterization of Redox Centers
Molybdenum Enzymes in Reactions Involving Aldehydes and Acids / Maria Joao Romao ; Carlos A. Cunha ; Carlos D. Brondino ; Jose J. G. MouraChapter 15:
Enzymes of the Xanthine Oxidase Family
Enzymes of the Aldehyde Oxidoreductase Family
Molybdenum and Tungsten Enzymes in C1 Metabolism / Julia A. Vorholt ; Rudolf K. ThauerChapter 16:
Formate Dehydrogenase
Formylmethanofuran Dehydrogenase
Carbon Monoxide Dehydrogenase
Formaldehyde Dehydrogenases
Molybdenum Enzymes and Sulfur Metabolism / John H. Enemark ; Michele Mader CosperChapter 17:
Sulfite Oxidase
Dimethyl Sulfoxide Reductase
Biotin Sulfoxide Reductase
Polysulfide Reductase
Comparison of Selenium-Containing Molybdoenzymes / Vadim N. GladyshevChapter 18:
Overview of Selenium-Containing Molybdoenzymes
Incorporation of Selenium into Molybdoenzymes
Selenium Versus Sulfur in Catalysis
Evolution of Selenocysteine-Containing Molybdoenzymes
Tungsten-Dependent Aldehyde Oxidoreductase: A New Family of Enzymes Containing the Pterin Cofactor / Roopali Roy ; Michael W. W. AdamsChapter 19:
Classification of Tungstoenzymes
Aldehyde Ferredoxin Oxidoreductase
Carboxylic Acid Reductase and Aldehyde Dehydrogenase
Formaldehyde Ferredoxin Oxidoreductase
Glyceraldehyde-3-Phosphate Ferredoxin Oxidoreductase
Hypothetical Tungstoenzymes--WOR4 and WOR5
Tungsten Versus Molybdenum in the AOR Family
Tungsten-Substituted Molybdenum Enzymes / C. David Garner ; Lisa J. StewartChapter 20:
Molybdenum and Tungsten Chemistry: Similarities and Differences
Molybdenum and Tungsten Geochemistry and Link to Bioavailability
Early Attempts to Substitute Tungsten for Molybdenum
Molybdenum-Substituted Tungsten Acetylene Hydratase
Molybdenum Metabolism and Requirements in Humans / Judith R. TurnlundChapter 21:
Essentiality of Molybdenum in Humans
Dietary Intake and Bioavailability of Molybdenum
Molybdenum Deficiency and Toxicity
Stable Isotope Studies of Molybdenum Metabolism
Metabolism and Toxicity of Tungsten in Humans and Animals / Florence Lagarde ; Maurice LeroyChapter 22:
Metabolism of Tungsten
Toxicity of Tungsten
Subject Index
Preface to the Series
Preface to Volume 39
In Memoriam of Professor Robert C. Bray
3.

図書

図書
Ugo Testa
出版情報: Noca Raton : CRC Press, c2002  559 p. ; 25 cm
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Iron Absorption
Iron and Cell Proliferation: Mechanisms and Applications in Cancer Therapy
Lactoferin
Transferrin
Transferrin Receptors
Soluble Transferrin Receptor
Alternative Iron Uptake Systems
Iron-Responsive Elements and Iron Regulatory Proteins
Ferritin
Iron Absorption
Iron and Cell Proliferation: Mechanisms and Applications in Cancer Therapy
Lactoferin
4.

図書

図書
by Timo Koski
出版情報: Dordrecht : Kluwer Academic Publishers, c2001  xvii, 391 p. ; 25 cm
シリーズ名: Computational biology series ; vol. 2
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5.

図書

図書
edited by Stefan Hohmann, Soren Nielsen, Peter Agre
出版情報: San Diego : Academic Press, c2001  xvii, 390 p., [8] p. of plates ; 24 cm
シリーズ名: Current topics in membranes ; v. 51
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Contributors
Preface
Previous Volumes in Series
Discovery of the Aquaporins and Their Impact on Basic and Clinical Physiology / Peter Agre ; Mario J. Borgnia ; Masato Yasui ; John D. Neely ; Jennifer Carbrey ; David Kozono ; Eric Beitz ; Jason Hoffer ; Virginia Leitch ; Landon S. KingChapter 1:
Pre-Aquaporin Era / I.:
The First Recognized Water Channel Protein / II.:
Other Mammalian Aquaporins / III.:
Nonmammalian Homologs / IV.:
Perspective / V.:
References
The Aquaporin Superfamily: Structure and Function / Henning Stahlberg ; Bernard Heymann ; Kaoru Mitsuoka ; Yoshinori Fuyijoshi ; Andreas EngelChapter 2:
Introduction
Two-Dimensional Crystallization of Membrane Proteins
Electron Crystallography
Atomic Force Microscopy
AQP1, The Erythrocyte Water Channel
AQP0: The Major Intrinsic Protein of Lens Fiber Cells / VI.:
Water Channel of Escherichia coli: AqpZ / VII.:
Glycerol Channel of Escherichia coli: GlpF / VIII.:
Comparison of the High-Resolution Projection Structures of GlpF and AQP1 / IX.:
Conclusion and Perspectives / X.:
Physiological Roles of Aquaporins in the Kidney / Mark A. Knepper ; Soren Nielsen ; Chung-Lin ChouChapter 3:
Water Transport along the Renal Tubule
Water Permeability along the Renal Tubule
Aquaporin-1 Facilitates Isoosmotic Fluid Transport in Proximal Tubule
Aquaporin-1 Allows Osmotic Equilibration in the Thin Descending Limb of Henle Despite Rapid Flow of Tubule Fluid
Aquaporin-1 Allows Osmotic Equilibration in the Descending Vasa Recta
Aquaporins Provide Molecular Targets for Regulation of Water Transport in the Renal Collecting Duct
Pathophysiology of Renal Aquaporins / Tae-Hwan Kwon ; Henrik Hager ; David Marples ; Jorgen FrokiaerChapter 4:
Inherited NDI and CDI
Acquired NDI
Urinary Concentrating Defects
States of Water Retention
Conclusions
Genetic and Biophysical Approaches to Study Water Channel Biology / A. S. Verkman ; Baoxue Yang ; William R. Skach ; Alok Mitra ; Yuanlin Song ; Geoffrey T. Manley ; Tonghui MaChapter 5:
Lessons from Aquaporin Knockout Mice
Biophysical Analysis of Aquaporin Function
Aquaporin Structure and Function
New Directions in Aquaporin Physiology and Biophysics
Trafficking of Native and Mutant Mammalian MIP Proteins / Peter M. T. Deen ; Dennis BrownChapter 6:
Normal Routing of MIP Proteins
Disturbed Trafficking of MIP Proteins
Aquaporins of Plants: Structure, Function, Regulation, and Role in Plant Water Relations / Maarten J. Chrispeels ; Raphael Morillon ; Christophe Maurel ; Patricia Gerbeau ; Per Kjellbom ; Ingela JohanssonChapter 7:
The Transpiration Stream
Water Movement in and between Living Tissues
Molecular Characteristics and Transport Properties of Plant Aquaporins
Subcellular Location of Plant Aquaporins
What Do the Water and Solute Transport Properties of Membranes Tell Us about the Aquaporins in Those Membranes?
The Multiple Roles of Aquaporins: How to Link Water Transport Properties to Functions at the Cellular and Tissue Level
Regulation of Aquaporin Expression and Water Transport Activity
Microbial Water Channels and Glycerol Facilitators / Gerald Kayingo ; Roslyn M. Bill ; Guiseppe Calamita ; Stefan Hohmann ; Bernard A. PriorChapter 8:
Microbial Aquaporins and Glycerol Facilitators
Transport Properties and Channel Selectivity of Microbial MIP Channels
From Primary to Quaternary Structure in Microbial MIPs
Physiological Roles
Microbial MIP Channels in Osmoregulation
Control of the Function of Microbial MIP Channels
Conclusions and Future Perspectives
Future Directions of Aquaporin Research / Chapter 9:
Identification and Characterization of New MIP Channels
Why Have So Many MIP Channels?
Analysis of the Physiological Roles of Aquaporins
Structure and Function
Aquaporins as Targets for Treatment of Human Disease
Aquaporins as Possible Targets for Genetic Engineering and Crop Improvement
Metabolic Engineering with Aquaporins
The Aquaporin Research Community
Index
Contributors
Preface
Previous Volumes in Series
6.

図書

図書
edited by Astrid Sigel, Helmut Sigel and Roland K.O. Sigel
出版情報: Boca Raton, Fla. : Taylor & Francis, 2005  xlv, 298 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 44
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7.

図書

図書
Paul Bourgine, Annick Lesne, editors
出版情報: Heidelberg : Springer, c2011  xvii, 346 p. ; 25 cm
シリーズ名: Springer complexity
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8.

図書

図書
by Justus Liebig ; edited from the manuscript of the author, by William Gregory
出版情報: London : Taylor and Walton, 1847  xx, 156 p. ; 22 cm
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9.

図書

図書
edited by Stuart L. Schreiber, Tarun M. Kapoor and Günther Wess
出版情報: Weinheim : Wiley-VCH, 2007  3 v. ; 25 cm
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Introduction / Part I:
Chemistry and Biology -- Historial and Philosophical Aspects / Gerhard Quinkert
Using Small Molecules To Explore Biology / Part II:
Using Small Molecules to Unravel Biological Mechanisms / Tarun Kapoor
Using Natural Products to Unravel Cell Biology / Craig Crews
Engineering Control Over Protein Function Using Chemistry / Kevan Shokat
Controlling Protein Function by Caged Compounds / Carsten Schultz
Transcription Control by Small-Molecules / John Koh
Controlling Protein-Protein Interactions / Virginia Cornish ; Columbia University) Controlling Protein-Protein Interactions Using Chemical Inducers and Disrupters of Dimerization ; Tim Clackson
Protein Secondary Structure Mimetics as Modulators of Protein-Protein and Protein-Ligand Interactions / Andrew Hamilton
Expanding the Genetic Code / Masahiko Sisido
Discovering Small Molecule Probes For Biological Mechanisms / Part III:
Forward Chemical Genetics / Stuart Schreiber ; Steve Haggarty
Reverse Chemical Genetics -- An Important Strategy for the Study of Protein Function in Chemical and Drug Discovery / Herbert Waldmann
Chemical Biology and Enzymology: Protein Phosphorylation as a Case Study / Phil Cole
Chemical Strategies for Activity-based Proteomics / Ben Cravatt
The Biarsenical Tetracysteine Protein Tag: Chemistry and Biological Applications / Steve Adams
Chemical Approaches to Exploit Fusion Proteins for Functional Studies / Kai Johnsson
Expanding The Scope Of Chemical Synthesis / Part IV:
Diversity-oriented Synthesis / Derek Tan
Combinatorial Biosynthesis of Polyketides and Nonribosomal Peptides / Chaitan Khosla
Expressed Protein Ligation / Tom Muir
Chemical Synthesis of Proteins and Large Bioconjugates / Phil Dawson
New Methods for Protein Bioconjugation / Matt Francis
The Search for Chemical Probes to Illuminate Carbohydrate Function / Laura Kiessling
Chemical Clydomics as Basis for Drug Discovery / Peter Seeberger
The Bicyclid Depsipeptide Family of Histone Deacetylase / A. Ganesan
Chemical Informatics / Part V:
Wombat and Wombat-Pk / Paul Clemons
Bioactivity Databases for Lead and Drug Discovery / Tudor Oprea
Drug discovery / Part VI:
Managerial Challenges in Implementing Chemical Biology Platforms / Frank Douglas
The Molecular Basis of Predicting Druggability / Andrew Hopkins ; Pfizer)
The Target Family Approach / Peter Nestler ; Sanofi-Aventis)
Chemical Biology of Kinases Studied by NMR Spectroscopy / Harald Schwalbe
The Nuclear Receptor Superfamily and Drug Discovery / Kenneth Pearce
The GPCR-7TM Receptor Target Family / Edgar Jacoby
Drugs Targeting Protein-Protein Interactions / Patrick Chene ; Novartis)
Systems Biology / Part VII:
Prediction of ADMET properties / Ulf Norinder ; AstraZeneca)
Systems Biology of the JAK-STAT Signaling Pathway / Jens Timmer
Modeling Intracellular Signal Transduction Processes / Jason Haugh
Genome-wide Gene Expression and Application to the Analysis of T-Cell Subsets in Inflammatory Diseases / Lars Rogge
Scanning the Proteome for Targets of Organic Small Molecules Using Bifunctional Receptor Ligands / Nikolai Kley
Outlook / Part VIII:
Introduction / Part I:
Chemistry and Biology -- Historial and Philosophical Aspects / Gerhard Quinkert
Using Small Molecules To Explore Biology / Part II:
10.

図書

図書
Donald Voet, Judith G. Voet, Charlotte W. Pratt
出版情報: Hoboken, NJ : John Wiley & Sons, c2008  xxx, 1099, 31, 31, 48 p. ; 28 cm
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Introduction / Part I:
Introduction to the Chemistry of Life / Chapter 1:
Water / Chapter 2:
Biomolecules / Part II:
Nucleotides, Nucleic Acids, and Genetic Information / Chapter 3:
Amino Acids / Chapter 4:
Proteins: Primary Structure / Chapter 5:
Proteins: Three-Dimensional Structure / Chapter 6:
Protein Function Part I: Myoglobin and Hemoglobin / Chapter 7:
Carbohydrates / Chapter 8:
Lipids and Biological Membranes / Chapter 9:
Membrane Transport / Chapter 10:
ENZYMES / Part III:
Enzymatic Catalysis / Chapter 11:
Enzyme Kinetics, Inhibition, and Regulation / Chapter 12:
Metabolism / Part IV:
Biochemical Signaling / Chapter 13:
Introduction to Metabolism / Chapter 14:
Glucose Catabolism / Chapter 15:
Glycogen Metabolism and Gluconeogenesis / Chapter 16:
Citric Acid Cycle / Chapter 17:
Electron Transport and Oxidative Phosphorylation / Chapter 18:
Photosynthesis / Chapter 19:
Lipid Metabolism / Chapter 20:
Amino Acid Metabolism / Chapter 21:
Mammalian Fuel Metabolism: Integration and Regulation / Chapter 22:
Nucleotide Metabolism / Chapter 23:
Gene Expression and Replication / Part V:
Nucleic Acid Structure / Chapter 24:
DNA Replication, Repair, and Recombination / Chapter 25:
Transcription and RNA Processing / Chapter 26:
Translation / Chapter 27:
Regulation of Gene Expression / Chapter 28:
Protein Function Part II: Cytoskeletal and Motor Proteins and Antibodies / Chapter 29:
Appendix
Bioinformatics Exercises
Answers to Bioinformatics Exercises
Solutions to Problems
Glossary
Guide to Media Resources
Index
Introduction / Part I:
Introduction to the Chemistry of Life / Chapter 1:
Water / Chapter 2:
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