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G-protein-coupled receptor dimers / Katharine Herrick-Davis, Graeme Milligan, Giuseppe Di Giovanni, editors.

Contributor(s): Di Giovanni, Giuseppe,, editor literario | Herrick-Davis, Katharine,, editor literario | Milligan, Graeme., editor literario
Material type: materialTypeLabelE-bookSeries: (The receptors ; v. 33).Publisher: Cham, Switzerland : Humana Press, 2017Copyright date: 2017Description: 1 recurso en línea.ISBN: 3319601741; 9783319601748.Subject: Biología molecularOnline resources: Acceso a este recurso digital (usuarios Universidad Europea de Madrid)Digital Resources
Contents:
Dedication; Foreword; On the Question of GPCR Oligomerization; References; Preface; Contents; Part I: Introduction; Chapter 1: Historical Perspectives: From Monomers to Dimers and Beyond, an Exciting Journey in the World of G Protein-Coupled Receptors; 1.1 Introduction; 1.2 The Birth of the Dimerization Concept; 1.3 Establishing the New Concept; 1.4 Oligomers Make the Picture More Complicated; 1.5 Receptor Homo- and Heteromers as New Pharmacological Targets; 1.6 Perspectives; References
2.1.6.1 Determining the Monomeric Quantal Brightness Value2.1.6.2 1 Population or 2 Population Mode; 2.1.6.3 When Does a QB Value Reflect Monomeric and When Dimeric/Oligomeric States?; 2.1.7 Determining the Quaternary Structure of GPCRs and How This May Be Affected by Ligand Binding; 2.1.8 Future Perspectives of SpIDA; References; Chapter 3: Advanced Microscopy Techniques; 3.1 Introduction; 3.2 FRET-Based Microscopy; 3.2.1 Definitions and the Principle of the Method; 3.2.2 Theoretical Basis of the Method; 3.2.3 Practical Implementation of FRET
3.2.3.1 General Requirements for Optical Microscopes Used in FRET Studies3.2.3.2 Two-Photon Absorption Optical Micro-spectroscopy; 3.2.3.3 Determination of FRET Efficiency from Optical Micro-­Spectroscopy Data; 3.2.4 Theoretical Models Used for Information Extraction from Experimental Data; 3.2.4.1 Prediction of FRET Efficiencies for Various Oligomer Configurations; 3.2.4.2 Computation of Average FRET Efficiencies for Mixtures of Oligomers; 3.2.5 Experimental Applications of FRET; 3.2.5.1 FRET Spectrometry; 3.2.5.2 Statistical-Ensemble Approach to FRET
3.2.5.3 Combination Between the Two FRET Approaches3.3 Spatial Fluorescence Correlation Spectroscopy; 3.3.1 Principle of the Method; 3.3.1.1 Generalized Spatial Correlation Function; 3.3.1.2 Spatial Auto-Correlation; 3.3.1.3 Spatial Cross-Correlation and Colocalization; 3.3.2 Practical Implementation of ICCS; 3.3.3 Experimental Applications of Spatial Fluorescence Correlation Spectroscopy; 3.4 Temporal Fluorescence Correlation Spectroscopy; 3.4.1 Principle of the Method; 3.4.2 Theoretical Background of the Method; 3.4.2.1 Generalized Temporal Correlation Function
Chapter 2: The Use of Spatial Intensity Distribution Analysis to Examine G Protein-Coupled Receptor Oligomerization2.1 Introduction; 2.1.1 SpIDA Procedure; 2.1.2 Choice of Fluorophore; 2.1.3 Selection of the Expression System; 2.1.4 Establishing Imaging Conditions for SpIDA; 2.1.4.1 Laser Power Intensity Measurement; 2.1.4.2 Laser Spot Beam Waist Radius Size; 2.1.4.3 Analog Detector Calibration; 2.1.4.4 Assessment of White Noise Level; 2.1.5 Laser Scanning Confocal Image Acquisition; 2.1.6 Spatial Intensity Distribution Analysis of Laser Scanning Confocal Images
Abstract: G-protein-coupled receptors (GPCRs) are believed to be the largest family of membrane proteins involved in signal transduction and cellular responses. They dimerize (form a pair of macromolecules) with a wide variety of other receptors. The proposed book will provide a comprehensive overview of GPCR dimers, starting with a historical perspective and including, basic information about the different dimers, how they synthesize, their signaling properties, and the many diverse physiological processes in which they are involved. In addition to presenting information about healthy GPCR dimer activity, the book will also include a section on their pathology and therapeutic potentials.
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Item type Current library Collection Call number Status Date due Barcode Item holds
LIBRO-E NO PRÉSTAMO LIBRO-E NO PRÉSTAMO Madrid Digital Acceso Electrónico (UEM) FCBS | FCAD QP552.G16 2017 EB (Browse shelf(Opens below)) Acceso electrónico eBook.20024091
Total holds: 0

Springer Biomedical and Life Sciences eBooks 2017 English+International

Incluye referencias bibliográficas

Dedication; Foreword; On the Question of GPCR Oligomerization; References; Preface; Contents; Part I: Introduction; Chapter 1: Historical Perspectives: From Monomers to Dimers and Beyond, an Exciting Journey in the World of G Protein-Coupled Receptors; 1.1 Introduction; 1.2 The Birth of the Dimerization Concept; 1.3 Establishing the New Concept; 1.4 Oligomers Make the Picture More Complicated; 1.5 Receptor Homo- and Heteromers as New Pharmacological Targets; 1.6 Perspectives; References

2.1.6.1 Determining the Monomeric Quantal Brightness Value2.1.6.2 1 Population or 2 Population Mode; 2.1.6.3 When Does a QB Value Reflect Monomeric and When Dimeric/Oligomeric States?; 2.1.7 Determining the Quaternary Structure of GPCRs and How This May Be Affected by Ligand Binding; 2.1.8 Future Perspectives of SpIDA; References; Chapter 3: Advanced Microscopy Techniques; 3.1 Introduction; 3.2 FRET-Based Microscopy; 3.2.1 Definitions and the Principle of the Method; 3.2.2 Theoretical Basis of the Method; 3.2.3 Practical Implementation of FRET

3.2.3.1 General Requirements for Optical Microscopes Used in FRET Studies3.2.3.2 Two-Photon Absorption Optical Micro-spectroscopy; 3.2.3.3 Determination of FRET Efficiency from Optical Micro-­Spectroscopy Data; 3.2.4 Theoretical Models Used for Information Extraction from Experimental Data; 3.2.4.1 Prediction of FRET Efficiencies for Various Oligomer Configurations; 3.2.4.2 Computation of Average FRET Efficiencies for Mixtures of Oligomers; 3.2.5 Experimental Applications of FRET; 3.2.5.1 FRET Spectrometry; 3.2.5.2 Statistical-Ensemble Approach to FRET

3.2.5.3 Combination Between the Two FRET Approaches3.3 Spatial Fluorescence Correlation Spectroscopy; 3.3.1 Principle of the Method; 3.3.1.1 Generalized Spatial Correlation Function; 3.3.1.2 Spatial Auto-Correlation; 3.3.1.3 Spatial Cross-Correlation and Colocalization; 3.3.2 Practical Implementation of ICCS; 3.3.3 Experimental Applications of Spatial Fluorescence Correlation Spectroscopy; 3.4 Temporal Fluorescence Correlation Spectroscopy; 3.4.1 Principle of the Method; 3.4.2 Theoretical Background of the Method; 3.4.2.1 Generalized Temporal Correlation Function

Chapter 2: The Use of Spatial Intensity Distribution Analysis to Examine G Protein-Coupled Receptor Oligomerization2.1 Introduction; 2.1.1 SpIDA Procedure; 2.1.2 Choice of Fluorophore; 2.1.3 Selection of the Expression System; 2.1.4 Establishing Imaging Conditions for SpIDA; 2.1.4.1 Laser Power Intensity Measurement; 2.1.4.2 Laser Spot Beam Waist Radius Size; 2.1.4.3 Analog Detector Calibration; 2.1.4.4 Assessment of White Noise Level; 2.1.5 Laser Scanning Confocal Image Acquisition; 2.1.6 Spatial Intensity Distribution Analysis of Laser Scanning Confocal Images

G-protein-coupled receptors (GPCRs) are believed to be the largest family of membrane proteins involved in signal transduction and cellular responses. They dimerize (form a pair of macromolecules) with a wide variety of other receptors. The proposed book will provide a comprehensive overview of GPCR dimers, starting with a historical perspective and including, basic information about the different dimers, how they synthesize, their signaling properties, and the many diverse physiological processes in which they are involved. In addition to presenting information about healthy GPCR dimer activity, the book will also include a section on their pathology and therapeutic potentials.

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