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2019 Journal Article Conformational transitions and the activation of heterotrimeric G proteins by G protein-coupled receptorsDraper-Joyce, Christopher and Furness, Sebastian George Barton (2019). Conformational transitions and the activation of heterotrimeric G proteins by G protein-coupled receptors. ACS Pharmacology and Translational Science, 2 (4), 285-290. doi: 10.1021/acsptsci.9b00054 |
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2019 Journal Article Deconvoluting the molecular control of binding and signaling at the amylin 3 receptor: RAMP3 alters signal propagation through extracellular loops of the calcitonin receptorPham, Vi, Zhu, Yue, Dal Maso, Emma, Reynolds, Christopher A., Deganutti, Giuseppe, Atanasio, Silvia, Hick, Caroline A., Yang, Dehua, Christopoulos, Arthur, Hay, Debbie L., Furness, Sebastian G. B., Wang, Ming-Wei, Wootten, Denise and Sexton, Patrick M. (2019). Deconvoluting the molecular control of binding and signaling at the amylin 3 receptor: RAMP3 alters signal propagation through extracellular loops of the calcitonin receptor. ACS Pharmacology and Translational Science, 2 (3), 183-197. doi: 10.1021/acsptsci.9b00010 |
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2019 Journal Article Expression and activity of the calcitonin receptor family in a sample of primary human high-grade gliomasOstrovskaya, Anna, Hick, Caroline, Hutchinson, Dana S., Stringer, Brett W., Wookey, Peter J., Wootten, Denise, Sexton, Patrick M. and Furness, Sebastian G.B. (2019). Expression and activity of the calcitonin receptor family in a sample of primary human high-grade gliomas. BMC Cancer, 19 (1) 157, 157. doi: 10.1186/s12885-019-5369-y |
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2019 Journal Article The molecular control of calcitonin receptor signalingdal Maso, Emma, Glukhova, Alisa, Zhu, Yue, Garcia-Nafria, Javier, Tate, Christopher G., Atanasio, Silvia, Reynolds, Christopher A., Ramírez-Aportela, Erney, Carazo, Jose-Maria, Hick, Caroline A., Furness, Sebastian G. B., Hay, Debbie L., Liang, Yi-Lynn, Miller, Laurence J., Christopoulos, Arthur, Wang, Ming-Wei, Wootten, Denise and Sexton, Patrick M. (2019). The molecular control of calcitonin receptor signaling. ACS Pharmacology and Translational Science, 2 (1), 31-51. doi: 10.1021/acsptsci.8b00056 |
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2018 Journal Article Differential engagement of polar networks in the glucagon-like peptide 1 receptor by endogenous variants of the glucagon-like peptide 1Furness, S. G. B., Christopoulos, A., Sexton, P. M. and Wootten, D. (2018). Differential engagement of polar networks in the glucagon-like peptide 1 receptor by endogenous variants of the glucagon-like peptide 1. Biochemical Pharmacology, 156, 223-240. doi: 10.1016/j.bcp.2018.08.033 |
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2018 Journal Article Dominant negative G proteins enhance formation and purification of agonist-GPCR-G protein complexes for structure determinationLiang, Yi-Lynn, Zhao, Peishen, Draper-Joyce, Christopher, Baltos, Jo-Anne, Glukhova, Alisa, Truong, Tin T., May, Lauren T., Christopoulos, Arthur, Wootten, Denise, Sexton, Patrick M. and Furness, Sebastian G. B. (2018). Dominant negative G proteins enhance formation and purification of agonist-GPCR-G protein complexes for structure determination. ACS Pharmacology and Translational Science, 1 (1), 12-20. doi: 10.1021/acsptsci.8b00017 |
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2018 Journal Article Structure of the adenosine-bound human adenosine A1 receptor–Gi complexDraper-Joyce, Christopher J., Khoshouei, Maryam, Thal, David M., Liang, Yi-Lynn, Nguyen, Anh T. N., Furness, Sebastian G. B., Venugopal, Hariprasad, Baltos, Jo-Anne, Plitzko, Jürgen M., Danev, Radostin, Baumeister, Wolfgang, May, Lauren T., Wootten, Denise, Sexton, Patrick M., Glukhova, Alisa and Christopoulos, Arthur (2018). Structure of the adenosine-bound human adenosine A1 receptor–Gi complex. Nature, 558 (7711), 559-563. doi: 10.1038/s41586-018-0236-6 |
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2018 Journal Article Extracellular loops 2 and 3 of the calcitonin receptor selectively modify agonist binding and efficacyDal Maso, Emma, Zhu, Yue, Pham, Vi, Reynolds, Christopher A., Deganutti, Giuseppe, Hick, Caroline A., Yang, Dehua, Christopoulos, Arthur, Hay, Debbie L., Wang, Ming-Wei, Sexton, Patrick M., Furness, Sebastian G.B. and Wootten, Denise (2018). Extracellular loops 2 and 3 of the calcitonin receptor selectively modify agonist binding and efficacy. Biochemical Pharmacology, 150, 214-244. doi: 10.1016/j.bcp.2018.02.005 |
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2018 Journal Article Phase-plate cryo-EM structure of a biased agonist-bound human GLP-1 receptor–Gs complexLiang, Yi-Lynn, Khoshouei, Maryam, Glukhova, Alisa, Furness, Sebastian G. B., Zhao, Peishen, Clydesdale, Lachlan, Koole, Cassandra, Truong, Tin T., Thal, David M., Lei, Saifei, Radjainia, Mazdak, Danev, Radostin, Baumeister, Wolfgang, Wang, Ming-Wei, Miller, Laurence J., Christopoulos, Arthur, Sexton, Patrick M. and Wootten, Denise (2018). Phase-plate cryo-EM structure of a biased agonist-bound human GLP-1 receptor–Gs complex. Nature, 555 (7694), 121-125. doi: 10.1038/nature25773 |
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2018 Journal Article Characterization of signalling and regulation of common calcitonin receptor splice variants and polymorphismsDal Maso, Emma, Just, Rasmus, Hick, Caroline, Christopoulos, Arthur, Sexton, Patrick M., Wootten, Denise and Furness, Sebastian G.B. (2018). Characterization of signalling and regulation of common calcitonin receptor splice variants and polymorphisms. Biochemical Pharmacology, 148, 111-129. doi: 10.1016/j.bcp.2017.12.016 |
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2017 Journal Article Coding GPCR-G protein specificityFurness, Sebastian G.B. and Sexton, Patrick M. (2017). Coding GPCR-G protein specificity. Cell Research, 27 (10), 1193-1194. doi: 10.1038/cr.2017.92 |
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2017 Journal Article Dianthin-30 or gelonin versus monomethyl auristatin E, each configured with an anti-calcitonin receptor antibody, are differentially potent in vitro in high-grade glioma cell lines derived from glioblastomaGilabert-Oriol, Roger, Furness, Sebastian G. B., Stringer, Brett W., Weng, Alexander, Fuchs, Hendrik, Day, Bryan W., Kourakis, Angela, Boyd, Andrew W., Hare, David L., Thakur, Mayank, Johns, Terrance G. and Wookey, Peter J. (2017). Dianthin-30 or gelonin versus monomethyl auristatin E, each configured with an anti-calcitonin receptor antibody, are differentially potent in vitro in high-grade glioma cell lines derived from glioblastoma. Cancer Immunology, Immunotherapy, 66 (9), 1217-1228. doi: 10.1007/s00262-017-2013-z |
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2017 Journal Article Phase-plate cryo-EM structure of a class B GPCR-G-protein complexLiang, Yi-Lynn, Khoshouei, Maryam, Radjainia, Mazdak, Zhang, Yan, Glukhova, Alisa, Tarrasch, Jeffrey, Thal, David M., Furness, Sebastian G. B., Christopoulos, George, Coudrat, Thomas, Danev, Radostin, Baumeister, Wolfgang, Miller, Laurence J., Christopoulos, Arthur, Kobilka, Brian K., Wootten, Denise, Skiniotis, Georgios and Sexton, Patrick M. (2017). Phase-plate cryo-EM structure of a class B GPCR-G-protein complex. Nature, 546 (7656), 118-123. doi: 10.1038/nature22327 |
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2017 Journal Article What determines the magnitude of cellular response for activation of G protein-coupled receptors?Furness, Sebastian G. B., Wootten, Denise and Sexton, Patrick M (2017). What determines the magnitude of cellular response for activation of G protein-coupled receptors?. Cell Cycle, 16 (5), 392-394. doi: 10.1080/15384101.2016.1271634 |
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2016 Journal Article Ligand-dependent modulation of G protein conformation alters drug efficacyFurness, Sebastian George Barton, Liang, Yi-Lynn, Nowell, Cameron James, Halls, Michelle Louise, Wookey, Peter John, Dal Maso, Emma, Inoue, Asuka, Christopoulos, Arthur, Wootten, Denise and Sexton, Patrick Michael (2016). Ligand-dependent modulation of G protein conformation alters drug efficacy. Cell, 167 (3), 739-749. doi: 10.1016/j.cell.2016.09.021 |
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2016 Journal Article Key interactions by conserved polar amino acids located at the transmembrane helical boundaries in Class B GPCRs modulate activation, effector specificity and biased signalling in the glucagon-like peptide-1 receptorWootten, Denise, Reynolds, Christopher A., Smith, Kevin J., Mobarec, Juan C., Furness, Sebastian G. B., Miller, Laurence J., Christopoulos, Arthur and Sexton, Patrick M. (2016). Key interactions by conserved polar amino acids located at the transmembrane helical boundaries in Class B GPCRs modulate activation, effector specificity and biased signalling in the glucagon-like peptide-1 receptor. Biochemical Pharmacology, 118, 68-87. doi: 10.1016/j.bcp.2016.08.015 |
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2016 Journal Article The extracellular surface of the GLP-1 receptor is a molecular trigger for biased agonismWootten, Denise, Reynolds, Christopher A, Smith, Kevin J, Mobarec, Juan C, Koole, Cassandra, Savage, Emilia E, Pabreja, Kavita, Simms, John, Sridhar, Rohan, Furness, Sebastian G B, Liu, Mengjie, Thompson, Philip E, Miller, Laurence J, Christopoulos, Arthur and Sexton, Patrick M (2016). The extracellular surface of the GLP-1 receptor is a molecular trigger for biased agonism. Cell, 165 (7), 1632-1643. doi: 10.1016/j.cell.2016.05.023 |
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2016 Journal Article A hydrogen-bonded polar network in the core of the glucagon-like peptide-1 receptor is a fulcrum for biased agonism: lessons from Class B crystal structuresWootten, Denise, Reynolds, Christopher A., Koole, Cassandra, Smith, Kevin J., Mobarec, Juan C., Simms, John, Quon, Tezz, Coudrat, Thomas, Furness, Sebastian G. B., Miller, Laurence J., Christopoulos, Arthur and Sexton, Patrick M. (2016). A hydrogen-bonded polar network in the core of the glucagon-like peptide-1 receptor is a fulcrum for biased agonism: lessons from Class B crystal structures. Molecular Pharmacology, 89 (3), 335-47. doi: 10.1124/mol.115.101246 |
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2016 Journal Article A novel ligand of calcitonin receptor reveals a potential new sensor that modulates programmed cell deathFurness, S.G.B., Hare, D.L., Kourakis, A., Turnley, A.M. and Wookey, P.J. (2016). A novel ligand of calcitonin receptor reveals a potential new sensor that modulates programmed cell death. Cell Death Discovery, 2 (1) 16062, 1-9. doi: 10.1038/cddiscovery.2016.62 |
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2015 Journal Article Biased allosteric modulation at the CaS receptor engendered by structurally diverse calcimimeticsCook, A. E., Mistry, S. N., Gregory, K. J., Furness, S. G. B., Sexton, P. M., Scammells, P. J., Conigrave, A. D., Christopoulos, A. and Leach, K. (2015). Biased allosteric modulation at the CaS receptor engendered by structurally diverse calcimimetics. British Journal of Pharmacology, 172 (1), 185-200. doi: 10.1111/bph.12937 |
