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c-di-GMP Signaling

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Cover of 'c-di-GMP Signaling'

Table of Contents

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    Book Overview
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    Chapter 1 Discovery of the Second Messenger Cyclic di-GMP.
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    Chapter 2 Enzymatic Production of c-di-GMP Using a Thermophilic Diguanylate Cyclase.
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    Chapter 3 Synthesis of [(32)P]-c-di-GMP for Diguanylate Cyclase and Phosphodiesterase Activity Determinations.
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    Chapter 4 High-Performance Liquid Chromatography (HPLC)-Based Detection and Quantitation of Cellular c-di-GMP.
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    Chapter 5 Identification and Quantification of Cyclic Di-Guanosine Monophosphate and Its Linear Metabolites by Reversed-Phase LC-MS/MS.
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    Chapter 6 Detection of Cyclic Dinucleotides by STING
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    Chapter 7 Spectrophotometric and Mass Spectroscopic Methods for the Quantification and Kinetic Evaluation of In Vitro c-di-GMP Synthesis
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    Chapter 8 Gauging and Visualizing c-di-GMP Levels in Pseudomonas aeruginosa Using Fluorescence-Based Biosensors.
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    Chapter 9 Cyclic di-GMP-Responsive Transcriptional Reporter Bioassays in Pseudomonas aeruginosa.
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    Chapter 10 Live Flow Cytometry Analysis of c-di-GMP Levels in Single Cell Populations
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    Chapter 11 Experimental Detection and Visualization of the Extracellular Matrix in Macrocolony Biofilms.
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    Chapter 12 Congo Red Stain Identifies Matrix Overproduction and Is an Indirect Measurement for c-di-GMP in Many Species of Bacteria.
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    Chapter 13 Type IV Pili-Dependent Motility as a Tool to Determine the Activity of c-di-GMP Modulating Enzymes in Myxococcus xanthus.
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    Chapter 14 Using Light-Activated Enzymes for Modulating Intracellular c-di-GMP Levels in Bacteria
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    Chapter 15 Analysis of c-di-GMP Levels Synthesized by a Photoreceptor Protein in Response to Different Light Qualities Using an In Vitro Enzymatic Assay
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    Chapter 16 Probing the Role of Cyclic di-GMP Signaling Systems in Disease Using Chinese Radish.
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    Chapter 17 Contribution of Cyclic di-GMP in the Control of Type III and Type VI Secretion in Pseudomonas aeruginosa.
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    Chapter 18 Semiquantitative Analysis of the Red, Dry, and Rough Colony Morphology of Salmonella enterica Serovar Typhimurium and Escherichia coli Using Congo Red
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    Chapter 19 Fluorescent 2-Aminopurine c-di-GMP and GpG Analogs as PDE Probes
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    Chapter 20 Measuring Cyclic Diguanylate (c-di-GMP)-Specific Phosphodiesterase Activity Using the MANT-c-di-GMP Assay.
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    Chapter 21 Determining Phosphodiesterase Activity (Radioactive Assay).
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    Chapter 22 Determining Diguanylate Cyclase Activity (Radioactive Assay).
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    Chapter 23 Detection of c-di-GMP-Responsive DNA Binding.
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    Chapter 24 Use of Nonradiochemical DNAse Footprinting to Analyze c-di-GMP Modulation of DNA-Binding Proteins.
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    Chapter 25 Detection of Cyclic di-GMP Binding Proteins Utilizing a Biotinylated Cyclic di-GMP Pull-Down Assay.
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    Chapter 26 Probing Protein-Protein Interactions with Genetically Encoded Photoactivatable Cross-Linkers.
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    Chapter 27 Identification of c-di-AMP-Binding Proteins Using Magnetic Beads
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    Chapter 28 Pull-Down with a c-di-GMP-Specific Capture Compound Coupled to Mass Spectrometry as a Powerful Tool to Identify Novel Effector Proteins.
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    Chapter 29 Identification of c-di-GMP-Responsive Riboswitches.
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    Chapter 30 Isothermal Titration Calorimetry to Determine Apparent Dissociation Constants (K d) and Stoichiometry of Interaction (n) of C-di-GMP Binding Proteins
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    Chapter 31 Targeting c-di-GMP Signaling, Biofilm Formation, and Bacterial Motility with Small Molecules.
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    Chapter 32 Discovering Selective Diguanylate Cyclase Inhibitors: From PleD to Discrimination of the Active Site of Cyclic-di-GMP Phosphodiesterases.
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    Chapter 33 High-Throughput Screening for Compounds that Modulate the Cellular c-di-GMP Level in Bacteria
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    Chapter 34 Genetic Tools to Study c-di-GMP-Dependent Signaling in Pseudomonas aeruginosa.
Attention for Chapter 13: Type IV Pili-Dependent Motility as a Tool to Determine the Activity of c-di-GMP Modulating Enzymes in Myxococcus xanthus.
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Chapter title
Type IV Pili-Dependent Motility as a Tool to Determine the Activity of c-di-GMP Modulating Enzymes in Myxococcus xanthus.
Chapter number 13
Book title
c-di-GMP Signaling
Published in
Methods in molecular biology, January 2017
DOI 10.1007/978-1-4939-7240-1_13
Pubmed ID
Book ISBNs
978-1-4939-7239-5, 978-1-4939-7240-1

Skotnicka, Dorota, Søgaard-Andersen, Lotte, Dorota Skotnicka, Lotte Søgaard-Andersen


The nucleotide-based second messenger bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) regulates multiple processes in bacteria including cellular motility. The rod-shaped Myxococcus xanthus cells move in the direction of their long axis using two distinct motility systems: type IV pili (T4P)-dependent motility and gliding motility. Manipulation of the c-di-GMP level by expression of either an active, heterologous diguanylate cyclase or an active, heterologous phosphodiesterase causes defects in T4P-dependent motility without affecting gliding motility. As both an increased and a decreased level of c-di-GMP affect T4P-dependent motility, M. xanthus represents a good model system to assess enzyme activity of diguanylate cyclases and phosphodiesterases using T4P-dependent motility as a readout. Here, we describe the assay, which allows correlating diguanylate cyclase and phosphodiesterase activity with T4P-dependent motility in M. xanthus.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 6 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 6 100%

Demographic breakdown

Readers by professional status Count As %
Student > Master 2 33%
Unspecified 1 17%
Student > Bachelor 1 17%
Professor > Associate Professor 1 17%
Unknown 1 17%
Readers by discipline Count As %
Agricultural and Biological Sciences 2 33%
Unspecified 1 17%
Biochemistry, Genetics and Molecular Biology 1 17%
Immunology and Microbiology 1 17%
Unknown 1 17%