Adhesion GPCR-Related Protein Networks
- Publikationstyp:
- Kapitel
- Metadaten:
-
- Autoren
- Barbara Knapp
- Uwe Wolfrum
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000402032600009&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1007/978-3-319-41523-9_8
- ISBN-13
- 978-3-319-41521-5
- Schlüsselwörter
- Protein networks
- Adhesion complexes
- Adhesion GPCR
- Affinity proteomics
- Brain-specific angiogenesis inhibitor
- Latrophillin
- VLGR1
- GPR98
- ADGR
- Signaling pathways
- Paginierung
- 147 - 178
- Buchtitel
- ADHESION G PROTEIN-COUPLED RECEPTORS: MOLECULAR, PHYSIOLOGICAL AND PHARMACOLOGICAL PRINCIPLES IN HEALTH AND DISEASE
- Datum der Veröffentlichung
- 2016
- Status
- Published
- Titel
- Adhesion GPCR-Related Protein Networks
- Ausgabe der Zeitschrift
- 234
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Autoren
- Barbara Knapp
- Uwe Wolfrum
- DOI
- 10.1007/978-3-319-41523-9_8
- ISBN-13
- 9783319415215
- Online publication date
- 2016
- Paginierung
- 147 - 178
- Buchtitel
- Adhesion G Protein-coupled Receptors
- Datum der Veröffentlichung
- 2016
- Status
- Published
- Herausgeber
- Springer International Publishing
- Herausgeber URL
- http://dx.doi.org/10.1007/978-3-319-41523-9_8
- Datum der Datenerfassung
- 2019
- Titel
- Adhesion GPCR-Related Protein Networks
Datenquelle: Crossref
- Abstract
- Adhesion G protein-coupled receptors (aGPCRs/ADGRs) are unique receptors that combine cell adhesion and signaling functions. Protein networks related to ADGRs exert diverse functions, e.g., in tissue polarity, cell migration, nerve cell function, or immune response, and are regulated via different mechanisms. The large extracellular domain of ADGRs is capable of mediating cell-cell or cell-matrix protein interactions. Their intracellular surface and domains are coupled to downstream signaling pathways and often bind to scaffold proteins, organizing membrane-associated protein complexes. The cohesive interplay between ADGR-related network components is essential to prevent severe disease-causing damage in numerous cell types. Consequently, in recent years, attention has focused on the decipherment of the precise molecular composition of ADGR protein complexes and interactomes in various cellular modules. In this chapter, we discuss the affiliation of ADGR networks to cellular modules and how they can be regulated, pinpointing common features in the networks related to the diverse ADGRs. Detailed decipherment of the composition of protein networks should provide novel targets for the development of novel therapies with the aim to cure human diseases related to ADGRs.
- Addresses
- Cell and Matrix Biology, Institute of Zoology, Johannes Gutenberg University of Mainz, Johannes von Muellerweg 6, Mainz, 55099, Germany.
- Autoren
- Barbara Knapp
- Uwe Wolfrum
- DOI
- 10.1007/978-3-319-41523-9_8
- Open access
- false
- Schlüsselwörter
- Cell Membrane
- Animals
- Humans
- Receptors, G-Protein-Coupled
- Protein Interaction Mapping
- Proteomics
- Cell Adhesion
- Signal Transduction
- Binding Sites
- Protein Binding
- Structure-Activity Relationship
- Models, Molecular
- Protein Interaction Domains and Motifs
- Protein Interaction Maps
- Medium
- Paginierung
- 147 - 178
- Datum der Veröffentlichung
- 2016
- Status
- Published
- Datum der Datenerfassung
- 2016
- Titel
- Adhesion GPCR-Related Protein Networks.
- Ausgabe der Zeitschrift
- 234
Datenquelle: Europe PubMed Central
- Abstract
- Adhesion G protein-coupled receptors (aGPCRs/ADGRs) are unique receptors that combine cell adhesion and signaling functions. Protein networks related to ADGRs exert diverse functions, e.g., in tissue polarity, cell migration, nerve cell function, or immune response, and are regulated via different mechanisms. The large extracellular domain of ADGRs is capable of mediating cell-cell or cell-matrix protein interactions. Their intracellular surface and domains are coupled to downstream signaling pathways and often bind to scaffold proteins, organizing membrane-associated protein complexes. The cohesive interplay between ADGR-related network components is essential to prevent severe disease-causing damage in numerous cell types. Consequently, in recent years, attention has focused on the decipherment of the precise molecular composition of ADGR protein complexes and interactomes in various cellular modules. In this chapter, we discuss the affiliation of ADGR networks to cellular modules and how they can be regulated, pinpointing common features in the networks related to the diverse ADGRs. Detailed decipherment of the composition of protein networks should provide novel targets for the development of novel therapies with the aim to cure human diseases related to ADGRs.
- Autoren
- Barbara Knapp
- Uwe Wolfrum
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/27832488
- DOI
- 10.1007/978-3-319-41523-9_8
- Schlüsselwörter
- ADGR
- Adhesion GPCR
- Adhesion complexes
- Affinity proteomics
- Brain-specific angiogenesis inhibitor
- GPR98
- Latrophillin
- Protein networks
- Signaling pathways
- VLGR1
- Animals
- Binding Sites
- Cell Adhesion
- Cell Membrane
- Humans
- Models, Molecular
- Protein Binding
- Protein Interaction Domains and Motifs
- Protein Interaction Mapping
- Protein Interaction Maps
- Proteomics
- Receptors, G-Protein-Coupled
- Signal Transduction
- Structure-Activity Relationship
- Paginierung
- 147 - 178
- Datum der Veröffentlichung
- 2016
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2017
- Titel
- Adhesion GPCR-Related Protein Networks.
- Ausgabe der Zeitschrift
- 234
Datenquelle: PubMed
- Beziehungen:
- Eigentum von