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Library | Materyal Türü | Barkod | Yer Numarası | Durum |
|---|---|---|---|---|
Searching... Pamukkale Merkez Kütüphanesi | Kitap | 0039686 | QH 604.2K73 2005 | Searching... Unknown |
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Özet
Özet
This all-new edition of a classic text has been thoroughly revised to keep pace with the rapid progress in signal transduction research. With didactic skill and clarity, the author relates the observed biological phenomena to the underlying biochemical processes.
Directed at advanced students, teachers, and researchers in biochemistry and molecular biology, this book describes the molecular basis of signal transduction, regulated gene expression, the cell cycle, tumorigenesis and apoptosis.
From the reviews of the previous edition:
"Provides a comprehensive account of cell signaling and signal transduction and, where possible, explains these processes at the molecular level"
- Angewandte Chemie
"The clear and didactic presentation makes it a textbook very useful for students and researchers not familiar with all aspects of cell regulation."
- Biochemistry
"This book is actually two books: Regulation and Signal Transduction."
- Drug Research
Author Notes
Gerhard Krauss is Professor of Biochemistry at the University of Bayreuth (Germany). His resarch is centered on the mechanism of interaction of DNA binding proteins and their target DNA. He is specifically interested in transcription factor, DNA methyl transferases and nucleotide excision repair.
The idea for a textbook on Signal Transduction and Gene Regulation originated from a lecture course that he has been teaching at Bayreuth since the middle of the 1990s.
Table of Contents
| Preface | p. VI |
| 1 The Regulation of Gene Expression | p. 1 |
| 1.1 Regulation of Gene Expression: How and Where? A Schematic Overview | p. 1 |
| 1.2 Protein-Nucleic Acid Interactions as a Basis for Specific Gene Regulation | p. 3 |
| 1.2.1 Structural Motifs of DNA-binding Proteins | p. 3 |
| 1.2.2 The Nature of the Specific Interactions in Protein-Nucleic Acid Complexes | p. 9 |
| 1.2.3 The Role of the DNA Conformation in Protein-DNA Interactions | p. 11 |
| 1.2.4 Structure of the Recognition Sequence and Quaternary Structure of DNA-binding Proteins | p. 13 |
| 1.3 The Principles of Transcription Regulation | p. 17 |
| 1.3.1 Elements of Transcription Regulation | p. 17 |
| 1.3.2 Functional Requirements for Repressors and Transcriptional Activators | p. 19 |
| 1.3.3 Mechanisms for the Control of the Activity of DNA-binding Proteins | p. 20 |
| 1.3.3.1 Binding of Effector Molecules | p. 21 |
| 1.3.3.2 Binding of Inhibitory Proteins | p. 23 |
| 1.3.3.3 Modification of Regulatory Proteins | p. 23 |
| 1.3.3.4 Changes in the Concentration of Regulatory DNA-binding Proteins | p. 24 |
| 1.4 Regulation of Transcription in Eucaryotes | p. 25 |
| 1.4.1 Overview of Transcription Initiation in Procaryotes | p. 26 |
| 1.4.2 The Basic Features of Eukaryotic Transcription | p. 28 |
| 1.4.3 The Eucaryotic Transcription Apparatus | p. 30 |
| 1.4.3.1 Structure of the Transcription Start Site and Regulatory Sequences | p. 30 |
| 1.4.3.2 Elementary Steps of Eucaryotic Transcription | p. 32 |
| 1.4.3.3 Formation of a Basal Transcription Apparatus from General Transcription Factors and RNA Polymerase | p. 33 |
| 1.4.3.4 Phosphorylation of RNA Polymerase II and the Onset of Transcription | p. 36 |
| 1.4.3.5 TFIIH--a Pivotal Regulatory Protein Complex | p. 38 |
| 1.4.4 Regulation of Eucaryotic Transcription by DNA-binding Proteins | p. 39 |
| 1.4.4.1 The Structure of Eucaryotic Transcriptional Activators | p. 39 |
| 1.4.4.2 Concerted Action of Transcriptional Activators and Coactivators in the Regulation of Transcription | p. 41 |
| 1.4.4.3 Interactions with the Transcription Apparatus | p. 45 |
| 1.4.5 Regulation of the Activity of Transcriptional Activators | p. 45 |
| 1.4.5.1 The Principal Pathways for the Regulation of Transcriptional Activators | p. 46 |
| 1.4.5.2 Phosphorylation of Transcriptional Activators | p. 46 |
| 1.4.5.3 Heterotypic Dimerization | p. 50 |
| 1.4.5.4 Regulation by Binding of Effector Molecules | p. 52 |
| 1.4.6 Specific Repression of Transcription | p. 52 |
| 1.4.7 Chromatin Structure and Transcription Activation | p. 55 |
| 1.4.7.1 Transcriptional Activity and Histone Acetylation | p. 58 |
| 1.4.7.2 Transcriptional Activity and Histone Methylation | p. 62 |
| 1.4.7.3 Enhanceosomes | p. 63 |
| 1.4.8 Methylation of DNA | p. 65 |
| 1.5 Post-transcriptional Regulation of Gene Expression | p. 68 |
| 1.5.1 Modifications at the 5' and 3' Ends of the Pre-mRNA | p. 69 |
| 1.5.2 Formation of Alternative mRNA by Alternative Polyadenylation and by Alternative Splicing | p. 70 |
| 1.5.3 Regulation via Transport and Splicing of Pre-mRNA | p. 73 |
| 1.5.4 Stability of the mRNA | p. 75 |
| 1.5.5 Regulation at the Level of Translation | p. 78 |
| 1.5.5.1 Regulation by binding of protein to the 5' end of the mRNA | p. 79 |
| 1.5.5.2 Regulation by Modification of Initiation Factors | p. 80 |
| 2 The Regulation of Enzyme Activity | p. 89 |
| 2.1 Enzymes as Catalysts | p. 90 |
| 2.2 Regulation of Enzymes by Effector Molecules | p. 91 |
| 2.3 Principal Features of Allosteric Regulation | p. 93 |
| 2.4 Regulation of Enzyme Activity by Binding of Inhibitor and Activator Proteins | p. 94 |
| 2.5 Regulation of Enzyme Activity by Phosphorylation | p. 95 |
| 2.5.1 Regulation of Glycogen Phosphorylase by Phosphorylation | p. 97 |
| 2.5.2 Regulation of Isocitrate Dehydrogenase (E. coli) by Phosphorylation | p. 100 |
| 2.6 Regulation via the Ubiquitin-Proteasome Pathway | p. 101 |
| 2.6.1 Components of the Ubiquitin System | p. 102 |
| 2.6.2 Degradation in the Proteasome | p. 107 |
| 2.6.3 Recognition of the Substrate in the Ubiquitin-Proteasome Degradation Pathway | p. 108 |
| 2.6.4 Regulatory Function of Ubiquitin Conjugation and the Targeted Degradation of Proteins | p. 110 |
| 2.7 Regulation of Proteins by Sumoylation | p. 113 |
| 3 Structure and Function of Signal Pathways | p. 115 |
| 3.1 General Function of Signal Pathways | p. 115 |
| 3.2 Structure of Signaling Pathways | p. 117 |
| 3.2.1 The Mechanisms of Intercellular Communication | p. 117 |
| 3.2.2 Principles of Intracellular Signal Transduction | p. 119 |
| 3.2.3 Components of Intracellular Signal Transduction | p. 120 |
| 3.2.4 Coupling of Proteins in Signaling Chains | p. 122 |
| 3.2.4.1 Coupling by Specific Protein-Protein Interactions | p. 122 |
| 3.2.4.2 Coupling by Protein Modules | p. 122 |
| 3.2.4.3 Coupling by Reversible Docking Sites | p. 123 |
| 3.2.4.4 Coupling by Colocalization | p. 123 |
| 3.2.4.5 Linearity, Branching and Crosstalk | p. 124 |
| 3.2.4.6 Variability and Specificity of Receptors and Signal Responses | p. 126 |
| 3.3 Extracellular Signaling Molecules | p. 128 |
| 3.3.1 The Chemical Nature of Hormones | p. 128 |
| 3.3.2 Hormone Analogs: Agonists and Antagonists | p. 131 |
| 3.3.3 Endocrine, Paracrine and Autocrine Signaling | p. 133 |
| 3.3.4 Direct Modification of Protein by Signaling Molecules | p. 133 |
| 3.4 Hormone Receptors | p. 135 |
| 3.4.1 Recognition of Hormones by Receptors | p. 135 |
| 3.4.2 The Interaction between Hormone and Receptor | p. 135 |
| 3.5 Signal Amplification | p. 139 |
| 3.6 Regulation of Inter- and Intracellular Signaling | p. 141 |
| 3.7 Membrane Anchoring and Signal Transduction | p. 142 |
| 3.7.1 Myristoylation | p. 144 |
| 3.7.2 Palmitoylation | p. 145 |
| 3.7.3 Farnesylation and Geranylation | p. 146 |
| 3.7.4 The Glycosyl-Phosphatidyl-Inositol Anchor (GPI Anchor) | p. 147 |
| 3.7.5 The Switch Function of Lipid Anchors | p. 148 |
| 4 Signaling by Nuclear Receptors | p. 151 |
| 4.1 Ligands of Nuclear Receptors | p. 151 |
| 4.2 Principles of Signaling by Nuclear Receptors | p. 153 |
| 4.3 Classification and Structure of Nuclear Receptors | p. 156 |
| 4.3.1 DNA-Binding Elements of Nuclear Receptors, HREs | p. 156 |
| 4.3.2 The DNA-Binding Domain of Nuclear Receptors | p. 159 |
| 4.3.3 HRE Recognition and Structure of the HRE-Receptor Complex | p. 161 |
| 4.3.4 Ligand-binding Domains | p. 162 |
| 4.3.5 Transactivating Elements of the Nuclear Receptors | p. 164 |
| 4.4 Mechanisms of Transcriptional Regulation by Nuclear Receptors | p. 165 |
| 4.5 Regulation and Variability of Signaling by Nuclear Receptors | p. 169 |
| 4.6 The Signaling Pathway of the Steroid Hormone Receptors | p. 171 |
| 4.7 Signaling by Retinoids, Vitamin D3, and the T3-Hormone | p. 173 |
| 4.7.1 Structure of the HREs of RXR Heterodimers | p. 175 |
| 4.7.2 Complexity of the Interaction between HRE, Receptor and Hormone | p. 175 |
| 5 G Protein-Coupled Signal Transmission Pathways | p. 179 |
| 5.1 Transmembrane Receptors: General Structure and Classification | p. 179 |
| 5.2 Structural Principles of Transmembrane Receptors | p. 181 |
| 5.2.1 The Extracellular Domain of Transmembrane Receptors | p. 181 |
| 5.2.2 The Transmembrane Domain | p. 183 |
| 5.2.3 The Intracellular Domain of Membrane Receptors | p. 185 |
| 5.2.4 Regulation of Receptor Activity | p. 186 |
| 5.3 G Protein-Coupled Receptors | p. 187 |
| 5.3.1 Structure of G Protein-Coupled Receptors | p. 188 |
| 5.3.2 Ligand Binding | p. 191 |
| 5.3.3 Mechanism of Signal Transmission | p. 192 |
| 5.3.4 Switching Off and Desensitization of 7-Helix Transmembrane Receptors | p. 192 |
| 5.3.5 Dimerization of GPCRs | p. 196 |
| 5.4 Regulatory GTPases | p. 197 |
| 5.4.1 The GTPase Superfamily: General Functions and Mechanism | p. 197 |
| 5.4.2 Inhibition of GTPases by GTP Analogs | p. 200 |
| 5.4.3 The G-domain as Common Structural Element of the GTPases | p. 200 |
| 5.4.4 The Different GTPase Families | p. 201 |
| 5.5 The Heterotrimeric G Proteins | p. 202 |
| 5.5.1 Classification of the Heterotrimeric G Proteins | p. 203 |
| 5.5.2 Toxins as Tools in the Characterization of Heterotrimeric G Proteins | p. 205 |
| 5.5.3 The Functional Cycle of Heterotrimeric G Proteins | p. 206 |
| 5.5.4 Structural and Mechanistic Aspects of the Switch Function of G Proteins | p. 208 |
| 5.5.5 Structure and Function of the [beta gamma]-Complex | p. 215 |
| 5.5.6 Membrane Association of the G Proteins | p. 217 |
| 5.5.7 Regulators of G Proteins: Phosducin and RGS Proteins | p. 218 |
| 5.6 Effector Molecules of G Proteins | p. 220 |
| 5.6.1 Adenylyl Cyclase and cAMP as Second Messenger | p. 220 |
| 5.6.2 Phospholipase C | p. 225 |
| 6 Intracellular Messenger Substances: Second Messengers | p. 231 |
| 6.1 General Functions of Intracellular Messenger Substances | p. 231 |
| 6.2 cAMP | p. 233 |
| 6.3 cGMP | p. 235 |
| 6.4 Metabolism of Inositol Phospholipids and Inositol Phosphates | p. 237 |
| 6.5 Inositol 1,4,5-Triphosphate and Release of Ca[superscript 2+] | p. 240 |
| 6.5.1 Release of Ca[superscript 2+] from Ca[superscript 2+] Storage | p. 241 |
| 6.5.2 Influx of Ca[superscript 2+] from the Extracellular Region | p. 245 |
| 6.5.3 Removal and Storage of Ca[superscript 2+] | p. 246 |
| 6.5.4 Temporal and Spatial Changes in Ca[superscript 2+] Concentration | p. 246 |
| 6.6 Phosphatidyl Inositol Phosphates and PI3-Kinase | p. 248 |
| 6.6.1 PI3-Kinases | p. 249 |
| 6.6.2 The Messenger Substance PtdIns(3,4,5)P[subscript 3] | p. 250 |
| 6.6.3 Akt Kinase and PtdIns(3,4,5)P[subscript 3] Signaling | p. 252 |
| 6.6.4 Functions of PtIns(4,5)P[subscript 2] | p. 253 |
| 6.7 Ca[superscript 2+] as a Signal Molecule | p. 253 |
| 6.7.1 Calmodulin as a Ca[superscript 2+] Receptor | p. 256 |
| 6.7.2 Target Proteins of Ca[superscript 2+]/Calmodulin | p. 257 |
| 6.7.3 Other Ca[superscript 2+] Receptors | p. 258 |
| 6.8 Diacylglycerol as a Signal Molecule | p. 259 |
| 6.9 Other Lipid Messengers | p. 260 |
| 6.10 The NO Signaling Molecule | p. 261 |
| 6.10.1 Reactivity and Stability of NO | p. 262 |
| 6.10.2 Synthesis of NO | p. 263 |
| 6.10.3 Physiological Functions and Attack Points of NO | p. 264 |
| 7 Ser/Thr-specific Protein Kinases and Protein Phosphatases | p. 269 |
| 7.1 Classification, Structure and Characteristics of Protein Kinases | p. 269 |
| 7.1.1 General Classification and Function of Protein Kinases | p. 269 |
| 7.1.2 Classification of Ser/Thr-specific Protein Kinases | p. 272 |
| 7.2 Structure and Regulation of Protein Kinases | p. 273 |
| 7.2.1 Main Structural Elements of Protein Kinases | p. 274 |
| 7.2.2 Substrate Binding and Recognition | p. 276 |
| 7.2.3 Control of Protein Kinase Activity | p. 277 |
| 7.3 Protein Kinase A | p. 280 |
| 7.3.1 Structure and Substrate Specificity of Protein Kinase A | p. 280 |
| 7.3.2 Regulation of Protein Kinase A | p. 281 |
| 7.4 Protein Kinase C | p. 283 |
| 7.4.1 Characterization and Classification | p. 283 |
| 7.4.2 Structure and Activation of Protein Kinase C | p. 286 |
| 7.4.3 Regulation of Protein Kinase C | p. 288 |
| 7.4.4 Functions and Substrates of Protein Kinase C | p. 290 |
| 7.5 Ca[superscript 2+]/Calmodulin-dependent Protein Kinases | p. 292 |
| 7.5.1 Importance and General Function | p. 292 |
| 7.5.2 Structure and Autoregulation of CaM Kinase II | p. 293 |
| 7.6 Ser/Thr-specific Protein Phosphatases | p. 296 |
| 7.6.1 Structure and Classification of Ser/Thr Protein Phosphatases | p. 296 |
| 7.6.2 Regulation of Ser/Thr Protein Phosphatases | p. 297 |
| 7.6.3 Protein Phosphatase I, PPI | p. 299 |
| 7.6.4 Protein Phosphatase 2A, PP2A | p. 301 |
| 7.6.5 Protein Phosphatase 2B, Calcineurin | p. 302 |
| 7.7 Regulation of Protein Phosphorylation by Subcellular Localization | p. 305 |
| 8 Signal Transmission via Transmembrane Receptors with Tyrosine-Specific Protein Kinase Activity | p. 311 |
| 8.1 Structure and Function of Receptor Tyrosine Kinases | p. 311 |
| 8.1.1 General Structure and Classification | p. 313 |
| 8.1.2 Ligand Binding and Activation | p. 314 |
| 8.1.3 Structure and Activation of the Tyrosine Kinase Domain | p. 319 |
| 8.1.4 Effector Proteins of the Receptor Tyrosine Kinases | p. 323 |
| 8.1.5 Attenuation and Termination of RTK Signaling | p. 326 |
| 8.2 Protein Modules as Coupling Elements of Signal Proteins | p. 328 |
| 8.2.1 SH2 Domains | p. 329 |
| 8.2.2 Phosphotyrosine-binding Domain (PTB Domain) | p. 332 |
| 8.2.3 SH3 Domains | p. 332 |
| 8.2.4 Membrane-targeting Domains: Pleckstrin Homology (PH) Domains and FYVE Domains | p. 334 |
| 8.2.5 Phosphoserine/Threonine-binding Domains | p. 335 |
| 8.2.6 PDZ Domains | p. 336 |
| 8.3 Nonreceptor Tyrosine-specific Protein Kinases | p. 337 |
| 8.3.1 Structure and General Function of Nonreceptor Tyrosine Kinases | p. 337 |
| 8.3.2 Src Tyrosine Kinase and Abl Tyrosine Kinase | p. 338 |
| 8.4 Protein Tyrosine Phosphatases | p. 342 |
| 8.4.1 Structure and Classification of Protein Tyrosine Phosphatases | p. 343 |
| 8.4.2 Cooperation of Protein Tyrosine Phosphatases and Protein Tyrosine Kinases | p. 346 |
| 8.4.3 Regulation of Protein Tyrosine Phosphatases | p. 348 |
| 8.5 Adaptor Molecules of Intracellular Signal Transduction | p. 351 |
| 9 Signal Transmission via Ras Proteins | p. 355 |
| 9.1 The Ras Superfamily of Monomeric GTPases | p. 355 |
| 9.2 General Importance of Ras Protein | p. 358 |
| 9.3 Structure and Biochemical Properties of Ras Protein | p. 360 |
| 9.3.1 Structure of the GTP- and GDP-bound Forms of Ras Protein | p. 361 |
| 9.3.2 GTP Hydrolysis: Mechanism and Stimulation by GAP Proteins | p. 363 |
| 9.3.3 Structure and Biochemical Properties of Transforming Mutants of Ras Protein | p. 366 |
| 9.4 Membrane Localization of Ras Protein | p. 366 |
| 9.5 GTPase-activating Protein (GAP) in Ras Signal Transduction | p. 368 |
| 9.6 Guanine Nucleotide Exchange Factors (GEFs) in Signal Transduction via Ras Proteins | p. 369 |
| 9.6.1 General Function of GEFs | p. 369 |
| 9.6.2 Structure and Activation of GEFs | p. 369 |
| 9.7 Raf Kinase as an Effector of Signal Transduction by Ras Proteins | p. 373 |
| 9.7.1 Structure of Raf Kinase | p. 373 |
| 9.7.2 Interaction of Raf Kinase with Ras Protein | p. 374 |
| 9.7.3 Mechanism of Activation and Regulation of Raf Kinase | p. 374 |
| 9.8 Reception and Transmission of Multiple Signals by Ras Protein | p. 375 |
| 10 Intracellular Signal Transduction: the Protein Cascades of the MAP Kinase Pathways | p. 383 |
| 10.1 Components of MAPK Pathways | p. 385 |
| 10.2 The Major MAPK Pathways of Mammals | p. 388 |
| 10.2.1 The ERK Pathway | p. 388 |
| 10.2.2 The JNK/SAPK, p38 and ERK5 MAPK Pathways | p. 391 |
| 11 Membrane Receptors with Associated Tyrosine Kinase Activity | p. 395 |
| 11.1 Cytokines and Cytokine Receptors | p. 395 |
| 11.2 Structure and Activation of Cytokine Receptors | p. 396 |
| 11.2.1 Activation of Cytoplasmic Tyrosine Kinases | p. 401 |
| 11.2.2 The Jak-Stat Pathway | p. 405 |
| 11.2.2.1 The Janus Kinases | p. 405 |
| 11.2.2.2 The Stat Proteins | p. 406 |
| 11.3 T and B Cell Antigen Receptors | p. 409 |
| 11.3.1 Receptor Structure | p. 410 |
| 11.3.2 Intracellular Signal Molecules of the T and B Cell Antigen Receptors | p. 411 |
| 11.4 Signal Transduction via Integrins | p. 413 |
| 12 Other Receptor Classes | p. 417 |
| 12.1 Receptors with Intrinsic Ser/Thr Kinase Activity: the TGF[beta] Receptor and the Smad Proteins | p. 417 |
| 12.1.1 TGF[beta] Receptor | p. 417 |
| 12.1.2 Smad Proteins | p. 418 |
| 12.2 Receptor Regulation by Intramembrane Proteolysis | p. 422 |
| 12.3 Signal Transduction via the Two-Component Pathway | p. 424 |
| 13 Regulation of the Cell Cycle | p. 429 |
| 13.1 Overview of the Cell Cycle | p. 429 |
| 13.1.1 Principles of Cell Cycle Control | p. 429 |
| 13.1.2 Intrinsic Control Mechanisms | p. 431 |
| 13.1.3 External Control Mechanisms | p. 433 |
| 13.1.4 Critical Cell Cycle Events and Cell Cycle Transitions | p. 434 |
| 13.2 Key Elements of the Cell Cycle Apparatus | p. 434 |
| 13.2.1 Cyclin-dependent Protein Kinases, CDKs | p. 435 |
| 13.2.2 Structure of CDKs and Regulation by Phosphorylation | p. 437 |
| 13.2.3 Cyclins | p. 439 |
| 13.2.4 Regulation of Cyclin Concentration | p. 440 |
| 13.2.5 Structural Basis for CDK Activation | p. 442 |
| 13.2.6 Inhibitors of CDKs: the CKIs | p. 445 |
| 13.2.7 Substrates of CDKs | p. 447 |
| 13.2.8 Multiple Regulation of CDKs | p. 449 |
| 13.3 Regulation of the Cell Cycle by Proteolysis | p. 449 |
| 13.3.1 Targeted Proteolysis by the SCF Complex | p. 451 |
| 13.3.2 Proteolysis during Mitosis: the Anaphase-promoting Complex/Cyclosome | p. 452 |
| 13.4 The G[subscript 1]/S Phase Transition | p. 453 |
| 13.4.1 Function of the D-type Cyclins | p. 454 |
| 13.4.2 Function of pRb in the Cell Cycle | p. 456 |
| 13.5 Cell Cycle Control of DNA Replication | p. 461 |
| 13.6 The G[subscript 2]/M Transition and Cdc25 Phosphatase | p. 463 |
| 13.7 Summary of Cell Cycle Progression | p. 465 |
| 13.8 The DNA Damage Checkpoints | p. 466 |
| 14 Malfunction of Signaling Pathways and Tumorigenesis: Oncogenes and Tumor Suppressor Genes | p. 469 |
| 14.1 General Aspects of Tumor Formation | p. 469 |
| 14.1.1 Characteristics of Tumor Cells | p. 469 |
| 14.1.2 Genetic Changes in Tumor Cells | p. 471 |
| 14.1.3 Epigenetic Changes in Tumor Cells | p. 472 |
| 14.1.4 Causes of Oncogenic Mutations | p. 473 |
| 14.1.5 DNA Repair, DNA Damage Checkpoints, and Tumor Formation | p. 474 |
| 14.1.6 Cell Division and Tumor Formation | p. 475 |
| 14.2 Cell Division Activity, Errors in Function of Signal Proteins, and Tumor Formation | p. 475 |
| 14.2.1 The Fate of a Cell: Quiescence, Division, or Death | p. 476 |
| 14.3 Definition and General Function of Oncogenes and Tumor Suppressor Genes | p. 477 |
| 14.3.1 Oncogenes and Proto-Oncogenes | p. 478 |
| 14.3.2 Mechanisms of Activation of Proto-Oncogenes | p. 479 |
| 14.3.3 Examples of the Functions of Oncogenes | p. 482 |
| 14.4 Tumor Suppressor Genes: General Functions | p. 487 |
| 14.5 DNA Repair, DNA Integrity and Tumor Suppression | p. 488 |
| 14.6 The Retinoblastoma Protein pRb in Cancer | p. 490 |
| 14.7 The p16[superscript INK4a] Gene Locus and ARF | p. 493 |
| 14.8 The Tumor Suppressor Protein p53 | p. 494 |
| 14.8.1 Structure and Biochemical Properties of the p53 Protein | p. 495 |
| 14.8.2 Sequence-Specific DNA Binding of p53 | p. 496 |
| 14.8.3 Genes Regulated by p53 | p. 498 |
| 14.8.4 Activation, Regulation and Modulation of the Function of p53 | p. 500 |
| 14.8.5 Overview of p53 Regulation | p. 502 |
| 14.8.6 The MDM2-p53 Network and Cancer | p. 505 |
| 14.9 The Tumor Suppressor APC and Wnt/[beta]-Catenin Signaling | p. 507 |
| 15 Apoptosis | p. 511 |
| 15.1 Basic Functions of Apoptosis | p. 511 |
| 15.2 Overview of Apoptosis | p. 513 |
| 15.3 Caspases: Death by Proteolysis | p. 515 |
| 15.4 The Family of Bcl-2 Proteins: Gatekeepers of Apoptosis | p. 520 |
| 15.5 The Mitochondrial Pathway of Apoptosis | p. 522 |
| 15.6 Death Receptor-triggered Apoptosis | p. 524 |
| 15.6.1 The Fas/CD95 Signaling Pathway | p. 525 |
| 15.6.2 Tumor Necrosis Factor-Receptor 1 and Apoptosis | p. 527 |
| 15.7 Links of Apoptosis and Cellular Signaling Pathways | p. 528 |
| 15.7.1 P13-Kinase/Akt Kinase and Apoptosis | p. 529 |
| 15.7.2 The Protein p53 and Apoptosis | p. 530 |
| Index | p. 533 |
