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Part I Intercellular Communication. |
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Introduction (Claudia Anetzberger and Kirsten Jung). |
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1 Cell–Cell Communication and Biofilm Formation in Gram-Positive Bacteria (Christine Heilmann and Friedrich Götz). |
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1.2 Staphylococcal Infections and Biofilms. |
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1.3 Molecular Basis of Biofilm Formation in Staphylococci. |
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1.4 QS in Staphylococcal Biofilms. |
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2 Cell–Cell Communication in Biofilms of Gram-Negative Bacteria (Claudio Aguilar, Aurelien Carlier, Kathrin Riedel, and Leo Eberl). |
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2.2 QS in Gram-Negative Bacteria. |
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2.3 QS and Biofilm Formation. |
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2.4 QS-Regulated Factors Involved in Biofilm Formation. |
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2.5 QS as a Target for the Eradication of Biofilms. |
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2.6 Interspecies Signaling in Mixed Biofilms. |
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3 Cell Interactions Guide the Swarming and Fruiting Body Development of Myxobacteria (Dale Kaiser). |
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3.2 Motility of Myxobacteria. |
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3.4 Slime Secretion Engine. |
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3.5 Swarming of Myxobacteria. |
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3.6 Regulating Reversals. |
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3.7 Fruiting Body Development. |
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3.8 C-Signal and Fruiting Body Morphogenesis. |
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3.9 Managing the Reversal Frequency. |
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3.10 C-Signal Control of Gene Expression. |
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4 Communication Between Rhizobia and Plants (Michael Göttfert). |
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4.2 Nodulation (nod) Genes are Induced by Flavonoids and are Under Positive and Negative Regulation. |
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4.3 Activation of the nod Genes Results in the Synthesis and Export of Lipo-Chito-Oligosaccharide Signal Molecules. |
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4.4 Rhizobia use Secreted Proteins as Effector Molecules. |
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4.5 Microarray Studies Help in Elucidating the Flavonoid Stimulons. |
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4.6 nod Genes as Accessory Components of the Rhizobial Core Genome. |
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4.7 Conclusions and Outlook. |
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5 Communication Between Pathogens and Eukaryotic Cells (Jürgen Heesemann). |
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5.2 Long-Distance Communication. |
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5.3 Short-Distance Communication. |
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6 Identification of Bacterial Autoinducers – Methods Chapter (Agnes Fekete, Michael Rothballer, Anton Hartmann, and Philippe Schmitt-Kopplin). |
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6.3 Sample Preparation Prior to Analysis. |
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6.4 Techniques for the Structural Analysis of AIs. |
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6.5 Techniques for the Quantification of AIs. |
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6.6 Conclusions and Future Perspectives. |
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Part II Transmembrane Signaling. |
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Introduction (Reinhard Krämer). |
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7 Outer Membrane Signaling in Gram-Negative Bacteria (Volkmar Braun). |
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7.2 A Sophisticated Mechanism: A Signaling Cascade Across the Outer Membrane in Transcriptional Regulation of the Ferric Citrate Transport Genes. |
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7.3 Transfer of the Signal Across the Cytoplasmic Membrane. |
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7.4 Signal Transfer into the Cytoplasm. |
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7.5 FecI is an ECF Sigma Factor. |
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7.6 Mechanism of Ferric Citrate Transcription Regulation. |
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7.7 Transcription Regulation of the Fec Type in Pseudomonas putida. |
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7.8 Transcription Regulation of the Fec Type in Pseudomonas aeruginosa. |
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7.9 Transcriptional Regulation of the Fec Type in Bordetella. |
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7.10 ECF Signaling in Serratia marcescens. |
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7.11 ECF Signaling in Ralstonia solanacearum. |
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7.12 Signaling in Outer Membrane Transport. |
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7.13 Assumed Outer Membrane Signaling. |
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8 Stimulus Perception and Signaling in Histidine Kinases (Ralf Heermann and Kirsten Jung). |
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8.2 Histidine Kinase Family. |
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8.3 Stimulus Perception and Signaling by Histidine Kinases. |
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8.4 Accessory Proteins of Histidine Kinases. |
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8.5 Conclusions and Outlook. |
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9 Chemotaxis and Receptor Localization (Victor Sourjik). |
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9.2 Architecture of the Sensory Complex. |
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9.3 Clustering of Sensory Complexes. |
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9.4 Role of Clustering in Signal Processing. |
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9.5 Conclusions and Outlook. |
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10 Photoreception and Signal Transduction (Sonja Brandt and Nicole Frankenberg-Dinkel). |
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10.2 Bacterial Blue-Light Photoreceptors. |
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10.3 Red-Light Sensing – Phytochromes. |
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11 Transmembrane Signaling (Melinda D. Baker and Matthew B. Neiditch). |
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11.2 Transmembrane Receptor Domain Architecture. |
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11.3 Structural Analysis of Transmembrane Signaling. |
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12 Sensory Transport Proteins (Reinhard Krämer). |
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12.2 Sensing of Transport Activity. |
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12.3 Stress Sensing by Transport Proteins. |
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12.4 Conclusions and Perspective. |
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13 Regulated Intramembrane Proteolysis in Bacterial Transmembrane Signaling (Thomas Wiegert). |
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13.3 Regulation of ECF Sigma Factors by RIP. |
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13.4 Regulation of ToxR-Like Transcriptional Regulators via RIP. |
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13.5 Involvement of RIP in Regulation of Bacterial Cell Division and Differentiation. |
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13.6 Involvement of RIP in Cell–Cell Communication. |
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14 Protein Chemical and Electron Paramagnetic Resonance Spectroscopic Approaches to Monitor Membrane Protein Structure and Dynamics – Methods Chapter (Daniel Hilger and Heinrich Jung). |
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14.3 Site-Directed Spin Labeling and EPR Spectroscopy. |
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Part III Intracellular Signaling. |
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Introduction (Kirsten Jung, Michael Y. Galperin, and Reinhard Krämer). |
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15 Protein Domains Involved in Intracellular Signal Transduction (Michael Y. Galperin). |
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15.2 Computational Analysis of Signaling Domains. |
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15.3 Intracellular Sensory Domains. |
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15.4 Intracellular Signal-Transducing and Output Domains. |
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15.5 Diversity of Intracellular Signaling Pathways. |
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16 Sensing of Oxygen by Bacteria (Gottfried Unden, Martin Müllner, and Florian Reinhart). |
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16.4 Indirect O2 Sensors. |
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17 Microbial Sensor Systems for Dihydrogen, Nitric Oxide, and Carbon Monoxide (Rainer Cramm and Bärbel Friedrich). |
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17.2 Sensing of Molecular Hydrogen. |
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17.3 Sensing of Nitric Oxide and Carbon Monoxide. |
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18 Signal Transduction by Trigger Enzymes: Bifunctional Enzymes and Transporters Controlling Gene Expression (Fabian M. Commichau and Jörg Stülke). |
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18.2 Trigger Enzymes Active as DNA-Binding Transcription Factors. |
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18.3 Trigger Enzymes Involved in Post-Transcriptional Regulation via Protein–RNA Interaction. |
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18.4 Trigger Enzymes Controlling Gene Expression by Signal-Dependent Phosphorylation of Transcription Regulators. |
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18.5 Trigger Enzymes Controlling the Activity of Transcription Factors by Protein–Protein Interactions. |
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18.6 Evolution of Trigger Enzymes: From Enzymes via Trigger Enzymes to Regulators. |
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19 Regulation of Carbohydrate Utilization by Phosphotransferase System-Mediated Protein Phosphorylation (Boris Görke and Birte Reichenbach). |
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19.2 Unique Features of the Bacterial PTS. |
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19.3 Phosphorylation of the IIAGlc Subunit of the Glucose Transporter Triggers Global CCR in Enteric Bacteria. |
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19.4 A Second Key Mechanism of CCR: Phosphorylation of IIAGlc Controls Inducer Exclusion in Enteric Bacteria. |
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19.5 Phosphorylation of Ser46 of HPr Triggers CCR in Low-GC Gram-Positive Bacteria. |
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19.6 Phosphorylation of HPr by the Bifunctional Kinase/Phosphorylase Links CCR to the Metabolic State of the Cell in Gram-Positive Bacteria. |
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19.7 HPr Controls Inducer Exclusion in Low-GC Gram-Positive Bacteria. |
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19.8 Control of Transcription Regulators by EII. |
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19.9 Catabolite Control of PRD-Containing Regulators by HPr(His~P)-Mediated Phosphorylation. |
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19.10 PTS-Dependent Regulation of Chemotaxis. |
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19.11 Regulatory Functions of Paralogous PTSs. |
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20 cAMP Signaling in Prokaryotes (Knut Jahreis). |
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20.2 CCR – A Short Historical Account. |
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20.3 Regulation of Intracellular cAMP Levels: PTS as a Sensor and Signal Transduction System that Modulates AC Activity. |
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20.4 Another Extension of the Simple Model: Catabolite Repression by Non-PTS Substrates: The PEP: Pyruvate Ratio is a Key Node in Carbon and Energy Metabolism. |
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20.5 cAMP Excretion and Phosphodiesterase Activity. |
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20.6 Function of the cAMP–CRP Complex. |
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20.7 cAMP–CRP Modulon and the CFU ‘‘Carbohydrate Catabolism/Quest for Food’’. |
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20.8 Interactions with Other Regulatory Systems. |
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20.9 Mathematical and Computer-Assisted Modeling of Catabolite Repression. |
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21 c-di-GMP Signaling (Christina Pesavento and Regine Hengge). |
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21.2 Protein Domains Involved in c-di-GMP Signaling. |
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21.3 Signaling Specificity. |
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21.4 c-di-GMP Signaling in E. coli. |
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21.5 c-di-GMP signaling in V. cholerae. |
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21.6 c-di-GMP Signaling in C. crescentus. |
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21.7 Conclusions and Outlook. |
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22 ppGpp Signaling (Rolf Wagner). |
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22.2 Induction of the Effector (p)ppGpp Through Synthesis and Degradation. |
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22.3 ppGpp – A Bona Fide Global Regulator. |
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22.4 Effects on Macromolecular Synthesis. |
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22.5 Regulation of Transcription: RNA Polymerase is the Target. |
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23 Sensory RNAs (Franz Narberhaus). |
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23.2 RNA as a Regulatory Molecule. |
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24 Signal Transduction by Serine/Threonine Protein Kinases in Bacteria (Michael Bott). |
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24.2 Discovery and Distribution of STPKs in Prokaryotes. |
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24.3 Serine/Threonine Phosphorylation versus Histidine/Aspartate Phosphorylation. |
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24.4 Domain Architecture of STPKs. |
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24.5 Structural Studies on STPKs. |
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24.6 Signal Transduction by STPKs. |
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24.7 Control of Gene Expression by PknB via the Activity of Sigma Factors. |
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24.8 Control of Gene Expression by PknH via the Transcriptional Regulator EmbR. |
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24.9 Direct Control of Enzyme Activities by STPKs. |
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24.10 Indirect Control of Enzyme Activity by PknG and its Target Protein OdhI/GarA. |
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24.11 Conclusions and Outlook. |
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25 Regulatory Proteolysis and Signal Transduction in Bacteria (Kürşad Turgay). |
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25.2 Hsp100/Clp and other AAA+ Protease Systems in Bacteria. |
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25.3 Substrate Recognition and Adaptor Proteins. |
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25.4 Examples of Regulatory Proteolysis in B. subtilis. |
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26 Intracellular Signaling and Gene Target Analysis – Methods Chapter (Jörn Kalinowski). |
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26.2 Genome-Wide Expression Analysis. |
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26.3 Finding Unknown Target Genes. |
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26.4 Analyzing Known Targets. |
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26.5 Conclusions and Outlook. |
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