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Adhesion G Protein-coupled Receptors

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Cover of 'Adhesion G Protein-coupled Receptors'

Table of Contents

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    Book Overview
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    Chapter 1 Introduction: History of the Adhesion GPCR Field.
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    Chapter 2 Classification, Nomenclature, and Structural Aspects of Adhesion GPCRs.
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    Chapter 3 7TM Domain Structure of Adhesion GPCRs.
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    Chapter 4 Understanding the Structural Basis of Adhesion GPCR Functions.
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    Chapter 5 Control of Adhesion GPCR Function Through Proteolytic Processing.
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    Chapter 6 Tethered Agonism: A Common Activation Mechanism of Adhesion GPCRs.
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    Chapter 7 Versatile Signaling Activity of Adhesion GPCRs.
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    Chapter 8 Adhesion G Protein-coupled Receptors
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    Chapter 9 The Relevance of Genomic Signatures at Adhesion GPCR Loci in Humans.
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    Chapter 10 Adhesion GPCRs as a Putative Class of Metabotropic Mechanosensors.
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    Chapter 11 Adhesion GPCRs Govern Polarity of Epithelia and Cell Migration.
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    Chapter 12 Adhesion GPCRs as Novel Actors in Neural and Glial Cell Functions: From Synaptogenesis to Myelination.
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    Chapter 13 Control of Skeletal Muscle Cell Growth and Size Through Adhesion GPCRs.
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    Chapter 14 Adhesion GPCR Function in Pulmonary Development and Disease.
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    Chapter 15 Adhesion GPCRs as Modulators of Immune Cell Function.
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    Chapter 16 Heart Development, Angiogenesis, and Blood-Brain Barrier Function Is Modulated by Adhesion GPCRs.
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    Chapter 17 Adhesion GPCRs in Tumorigenesis.
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    Chapter 18 Erratum to: 7TM Domain Structure of Adhesion GPCRs
Attention for Chapter 4: Understanding the Structural Basis of Adhesion GPCR Functions.
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Chapter title
Understanding the Structural Basis of Adhesion GPCR Functions.
Chapter number 4
Book title
Adhesion G Protein-coupled Receptors
Published in
Handbook of experimental pharmacology, November 2016
DOI 10.1007/978-3-319-41523-9_4
Pubmed ID
Book ISBNs
978-3-31-941521-5, 978-3-31-941523-9
Authors

Demet Araç, Norbert Sträter, Elena Seiradake

Editors

Tobias Langenhan, Torsten Schöneberg

Abstract

Unlike conventional G-protein-coupled receptors (GPCRs), adhesion GPCRs (aGPCRs) have large extracellular regions that are autoproteolytically cleaved from their membrane-embedded seven-pass transmembrane helices. Autoproteolysis occurs within the conserved GPCR-Autoproteolysis INducing (GAIN) domain that is juxtaposed to the transmembrane domain and cleaves the last beta strand of the GAIN domain. The other domains of the extracellular region are variable and specific to each aGPCR and are likely involved in adhering to various ligands. Emerging evidence suggest that extracellular regions may modulate receptor function and that ligand binding to the extracellular regions may induce receptor activation via multiple mechanisms. Here, we summarize current knowledge about the structural understanding for the extracellular regions of aGPCRs and discuss their possible functional roles that emerge from the available structural information.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 26 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 4%
Unknown 25 96%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 5 19%
Student > Master 4 15%
Student > Ph. D. Student 4 15%
Other 2 8%
Researcher 2 8%
Other 1 4%
Unknown 8 31%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 9 35%
Agricultural and Biological Sciences 5 19%
Neuroscience 4 15%
Pharmacology, Toxicology and Pharmaceutical Science 1 4%
Unknown 7 27%