The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator

The adhesion G protein–coupled receptor (aGPCR) GPR126/ADGRG6 plays an important role in several physiological functions, such as myelination or peripheral nerve repair. This renders the receptor an attractive pharmacological target. GPR126 is a mechano-sensor that translates the binding of extracel...
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Autor*in:	Jakob Mitgau [verfasserIn] Julius Franke [verfasserIn] Camilla Schinner [verfasserIn] Gabriele Stephan [verfasserIn] Sandra Berndt [verfasserIn] Dimitris G. Placantonakis [verfasserIn] Hermann Kalwa [verfasserIn] Volker Spindler [verfasserIn] Caroline Wilde [verfasserIn] Ines Liebscher [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	adhesion GPCR mechano-activation signal transduction allosteric modulator activating antibody extracellular matrix ligand

Übergeordnetes Werk:	In: Frontiers in Cell and Developmental Biology - Frontiers Media S.A., 2014, 10(2022)
Übergeordnetes Werk:	volume:10 ; year:2022

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fcell.2022.873278

Katalog-ID:	DOAJ042650658

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allfields	10.3389/fcell.2022.873278 doi (DE-627)DOAJ042650658 (DE-599)DOAJ9d31dab5f98d48a9b7b8f662eb77a2f2 DE-627 ger DE-627 rakwb eng QH301-705.5 Jakob Mitgau verfasserin aut The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The adhesion G protein–coupled receptor (aGPCR) GPR126/ADGRG6 plays an important role in several physiological functions, such as myelination or peripheral nerve repair. This renders the receptor an attractive pharmacological target. GPR126 is a mechano-sensor that translates the binding of extracellular matrix (ECM) molecules to its N terminus into a metabotropic intracellular signal. To date, the structural requirements and the character of the forces needed for this ECM-mediated receptor activation are largely unknown. In this study, we provide this information by combining classic second-messenger detection with single-cell atomic force microscopy. We established a monoclonal antibody targeting the N terminus to stimulate GPR126 and compared it to the activation through its known ECM ligands, collagen IV and laminin 211. As each ligand uses a distinct mode of action, the N terminus can be regarded as an allosteric module that can fine-tune receptor activation in a context-specific manner. adhesion GPCR mechano-activation signal transduction allosteric modulator activating antibody extracellular matrix ligand Biology (General) Julius Franke verfasserin aut Camilla Schinner verfasserin aut Gabriele Stephan verfasserin aut Sandra Berndt verfasserin aut Dimitris G. Placantonakis verfasserin aut Hermann Kalwa verfasserin aut Volker Spindler verfasserin aut Caroline Wilde verfasserin aut Ines Liebscher verfasserin aut In Frontiers in Cell and Developmental Biology Frontiers Media S.A., 2014 10(2022) (DE-627)770398138 (DE-600)2737824-X 2296634X nnns volume:10 year:2022 https://doi.org/10.3389/fcell.2022.873278 kostenfrei https://doaj.org/article/9d31dab5f98d48a9b7b8f662eb77a2f2 kostenfrei https://www.frontiersin.org/articles/10.3389/fcell.2022.873278/full kostenfrei https://doaj.org/toc/2296-634X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2022
spelling	10.3389/fcell.2022.873278 doi (DE-627)DOAJ042650658 (DE-599)DOAJ9d31dab5f98d48a9b7b8f662eb77a2f2 DE-627 ger DE-627 rakwb eng QH301-705.5 Jakob Mitgau verfasserin aut The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The adhesion G protein–coupled receptor (aGPCR) GPR126/ADGRG6 plays an important role in several physiological functions, such as myelination or peripheral nerve repair. This renders the receptor an attractive pharmacological target. GPR126 is a mechano-sensor that translates the binding of extracellular matrix (ECM) molecules to its N terminus into a metabotropic intracellular signal. To date, the structural requirements and the character of the forces needed for this ECM-mediated receptor activation are largely unknown. In this study, we provide this information by combining classic second-messenger detection with single-cell atomic force microscopy. We established a monoclonal antibody targeting the N terminus to stimulate GPR126 and compared it to the activation through its known ECM ligands, collagen IV and laminin 211. As each ligand uses a distinct mode of action, the N terminus can be regarded as an allosteric module that can fine-tune receptor activation in a context-specific manner. adhesion GPCR mechano-activation signal transduction allosteric modulator activating antibody extracellular matrix ligand Biology (General) Julius Franke verfasserin aut Camilla Schinner verfasserin aut Gabriele Stephan verfasserin aut Sandra Berndt verfasserin aut Dimitris G. Placantonakis verfasserin aut Hermann Kalwa verfasserin aut Volker Spindler verfasserin aut Caroline Wilde verfasserin aut Ines Liebscher verfasserin aut In Frontiers in Cell and Developmental Biology Frontiers Media S.A., 2014 10(2022) (DE-627)770398138 (DE-600)2737824-X 2296634X nnns volume:10 year:2022 https://doi.org/10.3389/fcell.2022.873278 kostenfrei https://doaj.org/article/9d31dab5f98d48a9b7b8f662eb77a2f2 kostenfrei https://www.frontiersin.org/articles/10.3389/fcell.2022.873278/full kostenfrei https://doaj.org/toc/2296-634X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2022
allfields_unstemmed	10.3389/fcell.2022.873278 doi (DE-627)DOAJ042650658 (DE-599)DOAJ9d31dab5f98d48a9b7b8f662eb77a2f2 DE-627 ger DE-627 rakwb eng QH301-705.5 Jakob Mitgau verfasserin aut The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The adhesion G protein–coupled receptor (aGPCR) GPR126/ADGRG6 plays an important role in several physiological functions, such as myelination or peripheral nerve repair. This renders the receptor an attractive pharmacological target. GPR126 is a mechano-sensor that translates the binding of extracellular matrix (ECM) molecules to its N terminus into a metabotropic intracellular signal. To date, the structural requirements and the character of the forces needed for this ECM-mediated receptor activation are largely unknown. In this study, we provide this information by combining classic second-messenger detection with single-cell atomic force microscopy. We established a monoclonal antibody targeting the N terminus to stimulate GPR126 and compared it to the activation through its known ECM ligands, collagen IV and laminin 211. As each ligand uses a distinct mode of action, the N terminus can be regarded as an allosteric module that can fine-tune receptor activation in a context-specific manner. adhesion GPCR mechano-activation signal transduction allosteric modulator activating antibody extracellular matrix ligand Biology (General) Julius Franke verfasserin aut Camilla Schinner verfasserin aut Gabriele Stephan verfasserin aut Sandra Berndt verfasserin aut Dimitris G. Placantonakis verfasserin aut Hermann Kalwa verfasserin aut Volker Spindler verfasserin aut Caroline Wilde verfasserin aut Ines Liebscher verfasserin aut In Frontiers in Cell and Developmental Biology Frontiers Media S.A., 2014 10(2022) (DE-627)770398138 (DE-600)2737824-X 2296634X nnns volume:10 year:2022 https://doi.org/10.3389/fcell.2022.873278 kostenfrei https://doaj.org/article/9d31dab5f98d48a9b7b8f662eb77a2f2 kostenfrei https://www.frontiersin.org/articles/10.3389/fcell.2022.873278/full kostenfrei https://doaj.org/toc/2296-634X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2022
allfieldsGer	10.3389/fcell.2022.873278 doi (DE-627)DOAJ042650658 (DE-599)DOAJ9d31dab5f98d48a9b7b8f662eb77a2f2 DE-627 ger DE-627 rakwb eng QH301-705.5 Jakob Mitgau verfasserin aut The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The adhesion G protein–coupled receptor (aGPCR) GPR126/ADGRG6 plays an important role in several physiological functions, such as myelination or peripheral nerve repair. This renders the receptor an attractive pharmacological target. GPR126 is a mechano-sensor that translates the binding of extracellular matrix (ECM) molecules to its N terminus into a metabotropic intracellular signal. To date, the structural requirements and the character of the forces needed for this ECM-mediated receptor activation are largely unknown. In this study, we provide this information by combining classic second-messenger detection with single-cell atomic force microscopy. We established a monoclonal antibody targeting the N terminus to stimulate GPR126 and compared it to the activation through its known ECM ligands, collagen IV and laminin 211. As each ligand uses a distinct mode of action, the N terminus can be regarded as an allosteric module that can fine-tune receptor activation in a context-specific manner. adhesion GPCR mechano-activation signal transduction allosteric modulator activating antibody extracellular matrix ligand Biology (General) Julius Franke verfasserin aut Camilla Schinner verfasserin aut Gabriele Stephan verfasserin aut Sandra Berndt verfasserin aut Dimitris G. Placantonakis verfasserin aut Hermann Kalwa verfasserin aut Volker Spindler verfasserin aut Caroline Wilde verfasserin aut Ines Liebscher verfasserin aut In Frontiers in Cell and Developmental Biology Frontiers Media S.A., 2014 10(2022) (DE-627)770398138 (DE-600)2737824-X 2296634X nnns volume:10 year:2022 https://doi.org/10.3389/fcell.2022.873278 kostenfrei https://doaj.org/article/9d31dab5f98d48a9b7b8f662eb77a2f2 kostenfrei https://www.frontiersin.org/articles/10.3389/fcell.2022.873278/full kostenfrei https://doaj.org/toc/2296-634X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2022
allfieldsSound	10.3389/fcell.2022.873278 doi (DE-627)DOAJ042650658 (DE-599)DOAJ9d31dab5f98d48a9b7b8f662eb77a2f2 DE-627 ger DE-627 rakwb eng QH301-705.5 Jakob Mitgau verfasserin aut The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The adhesion G protein–coupled receptor (aGPCR) GPR126/ADGRG6 plays an important role in several physiological functions, such as myelination or peripheral nerve repair. This renders the receptor an attractive pharmacological target. GPR126 is a mechano-sensor that translates the binding of extracellular matrix (ECM) molecules to its N terminus into a metabotropic intracellular signal. To date, the structural requirements and the character of the forces needed for this ECM-mediated receptor activation are largely unknown. In this study, we provide this information by combining classic second-messenger detection with single-cell atomic force microscopy. We established a monoclonal antibody targeting the N terminus to stimulate GPR126 and compared it to the activation through its known ECM ligands, collagen IV and laminin 211. As each ligand uses a distinct mode of action, the N terminus can be regarded as an allosteric module that can fine-tune receptor activation in a context-specific manner. adhesion GPCR mechano-activation signal transduction allosteric modulator activating antibody extracellular matrix ligand Biology (General) Julius Franke verfasserin aut Camilla Schinner verfasserin aut Gabriele Stephan verfasserin aut Sandra Berndt verfasserin aut Dimitris G. Placantonakis verfasserin aut Hermann Kalwa verfasserin aut Volker Spindler verfasserin aut Caroline Wilde verfasserin aut Ines Liebscher verfasserin aut In Frontiers in Cell and Developmental Biology Frontiers Media S.A., 2014 10(2022) (DE-627)770398138 (DE-600)2737824-X 2296634X nnns volume:10 year:2022 https://doi.org/10.3389/fcell.2022.873278 kostenfrei https://doaj.org/article/9d31dab5f98d48a9b7b8f662eb77a2f2 kostenfrei https://www.frontiersin.org/articles/10.3389/fcell.2022.873278/full kostenfrei https://doaj.org/toc/2296-634X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2022
language	English
source	In Frontiers in Cell and Developmental Biology 10(2022) volume:10 year:2022
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topic_facet	adhesion GPCR mechano-activation signal transduction allosteric modulator activating antibody extracellular matrix ligand Biology (General)
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authorswithroles_txt_mv	Jakob Mitgau @@aut@@ Julius Franke @@aut@@ Camilla Schinner @@aut@@ Gabriele Stephan @@aut@@ Sandra Berndt @@aut@@ Dimitris G. Placantonakis @@aut@@ Hermann Kalwa @@aut@@ Volker Spindler @@aut@@ Caroline Wilde @@aut@@ Ines Liebscher @@aut@@
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callnumber-first	Q - Science
author	Jakob Mitgau
spellingShingle	Jakob Mitgau misc QH301-705.5 misc adhesion GPCR misc mechano-activation misc signal transduction misc allosteric modulator misc activating antibody misc extracellular matrix ligand misc Biology (General) The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator
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topic_title	QH301-705.5 The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator adhesion GPCR mechano-activation signal transduction allosteric modulator activating antibody extracellular matrix ligand
topic	misc QH301-705.5 misc adhesion GPCR misc mechano-activation misc signal transduction misc allosteric modulator misc activating antibody misc extracellular matrix ligand misc Biology (General)
topic_unstemmed	misc QH301-705.5 misc adhesion GPCR misc mechano-activation misc signal transduction misc allosteric modulator misc activating antibody misc extracellular matrix ligand misc Biology (General)
topic_browse	misc QH301-705.5 misc adhesion GPCR misc mechano-activation misc signal transduction misc allosteric modulator misc activating antibody misc extracellular matrix ligand misc Biology (General)
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title	The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator
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title_full	The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator
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title_sort	n terminus of adhesion g protein–coupled receptor gpr126/adgrg6 as allosteric force integrator
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title_auth	The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator
abstract	The adhesion G protein–coupled receptor (aGPCR) GPR126/ADGRG6 plays an important role in several physiological functions, such as myelination or peripheral nerve repair. This renders the receptor an attractive pharmacological target. GPR126 is a mechano-sensor that translates the binding of extracellular matrix (ECM) molecules to its N terminus into a metabotropic intracellular signal. To date, the structural requirements and the character of the forces needed for this ECM-mediated receptor activation are largely unknown. In this study, we provide this information by combining classic second-messenger detection with single-cell atomic force microscopy. We established a monoclonal antibody targeting the N terminus to stimulate GPR126 and compared it to the activation through its known ECM ligands, collagen IV and laminin 211. As each ligand uses a distinct mode of action, the N terminus can be regarded as an allosteric module that can fine-tune receptor activation in a context-specific manner.
abstractGer	The adhesion G protein–coupled receptor (aGPCR) GPR126/ADGRG6 plays an important role in several physiological functions, such as myelination or peripheral nerve repair. This renders the receptor an attractive pharmacological target. GPR126 is a mechano-sensor that translates the binding of extracellular matrix (ECM) molecules to its N terminus into a metabotropic intracellular signal. To date, the structural requirements and the character of the forces needed for this ECM-mediated receptor activation are largely unknown. In this study, we provide this information by combining classic second-messenger detection with single-cell atomic force microscopy. We established a monoclonal antibody targeting the N terminus to stimulate GPR126 and compared it to the activation through its known ECM ligands, collagen IV and laminin 211. As each ligand uses a distinct mode of action, the N terminus can be regarded as an allosteric module that can fine-tune receptor activation in a context-specific manner.
abstract_unstemmed	The adhesion G protein–coupled receptor (aGPCR) GPR126/ADGRG6 plays an important role in several physiological functions, such as myelination or peripheral nerve repair. This renders the receptor an attractive pharmacological target. GPR126 is a mechano-sensor that translates the binding of extracellular matrix (ECM) molecules to its N terminus into a metabotropic intracellular signal. To date, the structural requirements and the character of the forces needed for this ECM-mediated receptor activation are largely unknown. In this study, we provide this information by combining classic second-messenger detection with single-cell atomic force microscopy. We established a monoclonal antibody targeting the N terminus to stimulate GPR126 and compared it to the activation through its known ECM ligands, collagen IV and laminin 211. As each ligand uses a distinct mode of action, the N terminus can be regarded as an allosteric module that can fine-tune receptor activation in a context-specific manner.
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title_short	The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator
url	https://doi.org/10.3389/fcell.2022.873278 https://doaj.org/article/9d31dab5f98d48a9b7b8f662eb77a2f2 https://www.frontiersin.org/articles/10.3389/fcell.2022.873278/full https://doaj.org/toc/2296-634X
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author2	Julius Franke Camilla Schinner Gabriele Stephan Sandra Berndt Dimitris G. Placantonakis Hermann Kalwa Volker Spindler Caroline Wilde Ines Liebscher
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up_date	2024-07-04T01:45:24.583Z
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The N Terminus of Adhesion G Protein–Coupled Receptor GPR126/ADGRG6 as Allosteric Force Integrator

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