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  1. Book: Adhesion G protein-coupled receptors

    Langenhan, Tobias / Schöneberg, Torsten

    molecular, physiological and pharmacological principles in health and disease

    (Handbook of experimental pharmacology ; 234)

    2016  

    Author's details Tobias Langenhan, Torsten Schöneberg editors
    Series title Handbook of experimental pharmacology ; 234
    Collection
    Keywords Cell-cell interaction ; Cell-matrix interaction ; G protein-coupled receptors ; Mechanoreception ; Metabotropic pathways
    Language English
    Size xiv, 403 Seiten, Illustrationen, Diagramme, 23.5 cm x 15.5 cm, 0 g
    Publisher Springer
    Publishing place Cham
    Publishing country Switzerland
    Document type Book
    HBZ-ID HT019180581
    ISBN 978-3-319-41521-5 ; 9783319415239 ; 3-319-41521-2 ; 3319415239
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2016 A 2601 available for loan (reading room) Lesesaal EG

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  2. Article ; Online: The repertoire and structure of adhesion GPCR transcript variants assembled from publicly available deep-sequenced human samples.

    Kuhn, Christina Katharina / Stenzel, Udo / Berndt, Sandra / Liebscher, Ines / Schöneberg, Torsten / Horn, Susanne

    Nucleic acids research

    2024  Volume 52, Issue 7, Page(s) 3823–3836

    Abstract: Alternative splicing and multiple transcription start and termination sites can produce a diverse repertoire of mRNA transcript variants from a given gene. While the full picture of the human transcriptome is still incomplete, publicly available RNA ... ...

    Abstract Alternative splicing and multiple transcription start and termination sites can produce a diverse repertoire of mRNA transcript variants from a given gene. While the full picture of the human transcriptome is still incomplete, publicly available RNA datasets have enabled the assembly of transcripts. Using publicly available deep sequencing data from 927 human samples across 48 tissues, we quantified known and new transcript variants, provide an interactive, browser-based application Splice-O-Mat and demonstrate its relevance using adhesion G protein-coupled receptors (aGPCRs) as an example. On average, 24 different transcript variants were detected for each of the 33 human aGPCR genes, and several dominant transcript variants were not yet annotated. Variable transcription starts and complex exon-intron structures encode a flexible protein domain architecture of the N- and C termini and the seven-transmembrane helix domain (7TMD). Notably, we discovered the first GPCR (ADGRG7/GPR128) with eight transmembrane helices. Both the N- and C terminus of this aGPCR were intracellularly oriented, anchoring the N terminus in the plasma membrane. Moreover, the assessment of tissue-specific transcript variants, also for other gene classes, in our application may change the evaluation of disease-causing mutations, as their position in different transcript variants may explain tissue-specific phenotypes.
    MeSH term(s) Humans ; Receptors, G-Protein-Coupled/genetics ; Receptors, G-Protein-Coupled/metabolism ; Receptors, G-Protein-Coupled/chemistry ; Alternative Splicing ; High-Throughput Nucleotide Sequencing ; Transcriptome/genetics ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Messenger/chemistry ; Exons/genetics ; Protein Domains
    Chemical Substances Receptors, G-Protein-Coupled ; RNA, Messenger
    Language English
    Publishing date 2024-02-29
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkae145
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Stachel-mediated activation of adhesion G protein-coupled receptors: insights from cryo-EM studies.

    Liebscher, Ines / Schöneberg, Torsten / Thor, Doreen

    Signal transduction and targeted therapy

    2022  Volume 7, Issue 1, Page(s) 227

    MeSH term(s) Cryoelectron Microscopy ; Protein Binding ; Receptors, G-Protein-Coupled/genetics
    Chemical Substances Receptors, G-Protein-Coupled
    Language English
    Publishing date 2022-07-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 2886872-9
    ISSN 2059-3635 ; 2095-9907
    ISSN (online) 2059-3635
    ISSN 2095-9907
    DOI 10.1038/s41392-022-01083-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Mutations in G Protein-Coupled Receptors: Mechanisms, Pathophysiology and Potential Therapeutic Approaches.

    Schöneberg, Torsten / Liebscher, Ines

    Pharmacological reviews

    2020  Volume 73, Issue 1, Page(s) 89–119

    Abstract: There are approximately 800 annotated G protein-coupled receptor (GPCR) genes, making these membrane receptors members of the most abundant gene family in the human genome. Besides being involved in manifold physiologic functions and serving as important ...

    Abstract There are approximately 800 annotated G protein-coupled receptor (GPCR) genes, making these membrane receptors members of the most abundant gene family in the human genome. Besides being involved in manifold physiologic functions and serving as important pharmacotherapeutic targets, mutations in 55 GPCR genes cause about 66 inherited monogenic diseases in humans. Alterations of nine GPCR genes are causatively involved in inherited digenic diseases. In addition to classic gain- and loss-of-function variants, other aspects, such as biased signaling,
    MeSH term(s) Humans ; Mutation ; Phenotype ; Receptors, G-Protein-Coupled/genetics ; Signal Transduction
    Chemical Substances Receptors, G-Protein-Coupled
    Language English
    Publishing date 2020-11-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 209898-2
    ISSN 1521-0081 ; 0031-6997
    ISSN (online) 1521-0081
    ISSN 0031-6997
    DOI 10.1124/pharmrev.120.000011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  5. Book ; Online ; Thesis: Evolutionary analyses reveal immune cell receptor GPR84 as a conserved receptor for bacteria-derived molecules

    Schulze, Amadeus Samuel [Verfasser] / Stäubert, Claudia [Akademischer Betreuer] / Schöneberg, Torsten [Akademischer Betreuer]

    2024  

    Author's details Amadeus Samuel Schulze ; Claudia Stäubert, Torsten Schöneberg
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Universitätsbibliothek Leipzig
    Publishing place Leipzig
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

    Full text online

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  6. Article ; Online: Eignung von Offener Zucht und Blühstreifen zur Blattlausbekämpfung in Kopfsalat

    Schöneberg, Torsten / Sauer, Cornelia / Krauss, Jürgen

    2023  

    Keywords Text ; abstract_or_summary ; ddc:630
    Language German
    Publisher Julius Kühn-Institut
    Publishing country de
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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  7. Article ; Online: Translating the force-mechano-sensing GPCRs.

    Wilde, Caroline / Mitgau, Jakob / Suchý, Tomáš / Schöneberg, Torsten / Liebscher, Ines

    American journal of physiology. Cell physiology

    2022  Volume 322, Issue 6, Page(s) C1047–C1060

    Abstract: Incorporating mechanical cues into cellular responses allows us to experience our direct environment. Specialized cells can perceive and discriminate between different physical properties such as level of vibration, temperature, or pressure. Mechanical ... ...

    Abstract Incorporating mechanical cues into cellular responses allows us to experience our direct environment. Specialized cells can perceive and discriminate between different physical properties such as level of vibration, temperature, or pressure. Mechanical forces are abundant signals that also shape general cellular responses such as cytoskeletal rearrangement, differentiation, or migration and contribute to tissue development and function. The molecular structures that perceive and transduce mechanical forces are specialized cytoskeletal proteins, cell junction molecules, and membrane proteins such as ion channels and metabotropic receptors. G protein-coupled receptors (GPCRs) have attracted attention as metabotropic force receptors as they are among the most important drug targets. This review summarizes the function of mechano-sensitive GPCRs, specifically, the angiotensin II type 1 receptor and adrenergic, apelin, histamine, parathyroid hormone 1, and orphan receptors, focusing particularly on the advanced knowledge gained from adhesion-type GPCRs. We distinguish between shear stress and cell swelling/stretch as the two major types of mechano-activation of these receptors and contemplate the potential contribution of the force-from-lipid and force-from-tether models that have previously been suggested for ion channels.
    MeSH term(s) Ion Channels ; Mechanical Phenomena ; Membrane Proteins/metabolism ; Receptors, G-Protein-Coupled/metabolism ; Stress, Mechanical
    Chemical Substances Ion Channels ; Membrane Proteins ; Receptors, G-Protein-Coupled
    Language English
    Publishing date 2022-04-13
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 392098-7
    ISSN 1522-1563 ; 0363-6143
    ISSN (online) 1522-1563
    ISSN 0363-6143
    DOI 10.1152/ajpcell.00465.2021
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uc I Zs.89: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  8. Article ; Online: The Signaling Pathway of the ADP Receptor P2Y

    Entsie, Philomena / Kang, Ying / Amoafo, Emmanuel Boadi / Schöneberg, Torsten / Liverani, Elisabetta

    International journal of molecular sciences

    2023  Volume 24, Issue 7

    Abstract: ... ...

    Abstract P2Y
    MeSH term(s) Animals ; Humans ; Purinergic P2Y Receptor Antagonists/pharmacology ; Purinergic P2Y Receptor Antagonists/therapeutic use ; COVID-19/metabolism ; Blood Platelets/metabolism ; Signal Transduction ; Immune System ; Receptors, Purinergic P2/metabolism ; Receptors, Purinergic P2Y12/genetics ; Receptors, Purinergic P2Y12/metabolism ; Platelet Aggregation ; Platelet Aggregation Inhibitors/pharmacology ; Adenosine Diphosphate/metabolism
    Chemical Substances Purinergic P2Y Receptor Antagonists ; Receptors, Purinergic P2 ; Receptors, Purinergic P2Y12 ; Platelet Aggregation Inhibitors ; Adenosine Diphosphate (61D2G4IYVH)
    Language English
    Publishing date 2023-04-04
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms24076709
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Latrophilins and Teneurins in Invertebrates: No Love for Each Other?

    Schöneberg, Torsten / Prömel, Simone

    Frontiers in neuroscience

    2019  Volume 13, Page(s) 154

    Abstract: Transsynaptic connections enabling cell-cell adhesion and cellular communication are a vital part of synapse formation, maintenance and function. A recently discovered interaction between the Adhesion GPCRs Latrophilins and the type II single ... ...

    Abstract Transsynaptic connections enabling cell-cell adhesion and cellular communication are a vital part of synapse formation, maintenance and function. A recently discovered interaction between the Adhesion GPCRs Latrophilins and the type II single transmembrane proteins Teneurins at mammalian synapses is vital for synapse formation and dendrite branching. While the understanding of the effects and the molecular interplay of this Latrophilin-Teneurin partnership is not entirely understood, its significance is highlighted by behavioral and neurological phenotypes in various animal models. As both groups of molecules, Latrophilins and Teneurins, are generally highly conserved, have overlapping expression and often similar functions across phyla, it can be speculated that this interaction, which has been proven essential in mammalian systems, also occurs in invertebrates to control shaping of synapses. Knowledge of the generality of this interaction is especially of interest due to its possible involvement in neuropathologies. Further, several invertebrates serve as model organisms for addressing various neurobiological research questions. So far, an interaction of Latrophilins and Teneurins has not been observed in invertebrates, but our knowledge on both groups of molecules is by far not complete. In this review, we give an overview on existing experimental evidence arguing for as well as against a potential Latrophilin-Teneurin interaction beyond mammals. By combining these insights with evolutionary aspects on each of the interaction partners we provide and discuss a comprehensive picture on the functions of both molecules in invertebrates and the likeliness of an evolutionary conservation of their interaction.
    Language English
    Publishing date 2019-03-12
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2411902-7
    ISSN 1662-453X ; 1662-4548
    ISSN (online) 1662-453X
    ISSN 1662-4548
    DOI 10.3389/fnins.2019.00154
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: The Evolutionary History of Vertebrate Adhesion GPCRs and Its Implication on Their Classification.

    Wittlake, Aline / Prömel, Simone / Schöneberg, Torsten

    International journal of molecular sciences

    2021  Volume 22, Issue 21

    Abstract: Adhesion G protein-coupled receptors (aGPCRs) form a structurally separate class of GPCRs with an unresolved evolutionary history and classification. Based on phylogenetic relations of human aGPCRs, nine families (A-G, L, V) were distinguished. Taking ... ...

    Abstract Adhesion G protein-coupled receptors (aGPCRs) form a structurally separate class of GPCRs with an unresolved evolutionary history and classification. Based on phylogenetic relations of human aGPCRs, nine families (A-G, L, V) were distinguished. Taking advantage of available genome data, we determined the aGPCR repertoires in all vertebrate classes. Although most aGPCR families show a high numerical stability in vertebrate genomes, the full repertoire of family E, F, and G members appeared only after the fish-tetrapod split. We did not find any evidence for new aGPCR families in vertebrates which are not present in the human genome. Based on ortholog sequence alignments, selection analysis clearly indicated two types of tetrapod aGPCRs: (i) aGPCR under strong purifying selection in tetrapod evolution (families A, B, D, L, V); and (ii) aGPCR with signatures of positive selection in some tetrapod linages (families C, E, G, F). The alignments of aGPCRs also allowed for a revised definition of reference positions within the seven-transmembrane-helix domain (relative position numbering scheme). Based on our phylogenetic cluster analysis, we suggest a revised nomenclature of aGPCRs including their transcript variants. Herein, the former families E and L are combined to one family (L) and GPR128/ADGRG7 forms a separate family (E). Furthermore, our analyses provide valuable information about the (patho)physiological relevance of individual aGPCR members.
    MeSH term(s) Animals ; Evolution, Molecular ; Humans ; Phylogeny ; Protein Domains ; Receptors, G-Protein-Coupled/classification ; Receptors, G-Protein-Coupled/genetics ; Structure-Activity Relationship
    Chemical Substances Receptors, G-Protein-Coupled
    Language English
    Publishing date 2021-10-30
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms222111803
    Database MEDical Literature Analysis and Retrieval System OnLINE

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