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1. SARS-CoV-2 Mpro responds to oxidation by forming disulfide and NOS/SONOS bonds

Author

Reinke, Patrick Y. A., Schubert, Robin, Oberthür, Dominik, Galchenkova, Marina, Rahmani Mashhour, Aida, Günther, Sebastian, Chretien, Anaïs, Round, Adam, Seychell, Brandon Charles, Norton-Baker, Brenna, Kim, Chan, Schmidt, Christina, Koua, Faisal H. M., Tolstikova, Alexandra, Ewert, Wiebke, Peña Murillo, Gisel Esperanza, Mills, Grant, Kirkwood, Henry, Brognaro, Hévila, Han, Huijong, Koliyadu, Jayanath, Schulz, Joachim, Bielecki, Johan, Lieske, Julia, Maracke, Julia, Knoska, Juraj, Lorenzen, Kristina, Brings, Lea, Sikorski, Marcin, Kloos, Marco, Vakili, Mohammad, Vagovic, Patrik, Middendorf, Philipp, de Wijn, Raphael, Bean, Richard, Letrun, Romain, Han, Seonghyun, Falke, Sven, Geng, Tian, Sato, Tokushi, Srinivasan, Vasundara, Kim, Yoonhee, Yefanov, Oleksandr M., Gelisio, Luca, Beck, Tobias, Doré, Andrew S., Mancuso, Adrian P., Betzel, Christian, Bajt, Saša, Redecke, Lars, Chapman, Henry N., Meents, Alke, Turk, Dušan, Hinrichs, Winfried, and Lane, Thomas J.

Published
2024
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10. Extra-helical binding site of a glucagon receptor antagonist

Author

Jazayeri, Ali, Doré, Andrew S., Lamb, Daniel, Krishnamurthy, Harini, Southall, Stacey M., Baig, Asma H., Bortolato, Andrea, Koglin, Markus, Robertson, Nathan J., Errey, James C., Andrews, Stephen P., Teobald, Iryna, Brown, Alastair J. H., Cooke, Robert M., Weir, Malcolm, and Marshall, Fiona H.

Published
2016
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21. Advances in long-wavelength native phasing at X-ray free-electron lasers

Author

Nass, Karol, primary, Cheng, Robert, additional, Vera, Laura, additional, Mozzanica, Aldo, additional, Redford, Sophie, additional, Ozerov, Dmitry, additional, Basu, Shibom, additional, James, Daniel, additional, Knopp, Gregor, additional, Cirelli, Claudio, additional, Martiel, Isabelle, additional, Casadei, Cecilia, additional, Weinert, Tobias, additional, Nogly, Przemyslaw, additional, Skopintsev, Petr, additional, Usov, Ivan, additional, Leonarski, Filip, additional, Geng, Tian, additional, Rappas, Mathieu, additional, Doré, Andrew S., additional, Cooke, Robert, additional, Nasrollahi Shirazi, Shahrooz, additional, Dworkowski, Florian, additional, Sharpe, May, additional, Olieric, Natacha, additional, Bacellar, Camila, additional, Bohinc, Rok, additional, Steinmetz, Michel O., additional, Schertler, Gebhard, additional, Abela, Rafael, additional, Patthey, Luc, additional, Schmitt, Bernd, additional, Hennig, Michael, additional, Standfuss, Jörg, additional, Wang, Meitian, additional, and Milne, Christopher J., additional

Published
2020
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22. X‐Ray Crystallography and Free Energy Calculations Reveal the Binding Mechanism of A2A Adenosine Receptor Antagonists

Author

Jespers, Willem, primary, Verdon, Grégory, additional, Azuaje, Jhonny, additional, Majellaro, Maria, additional, Keränen, Henrik, additional, García‐Mera, Xerardo, additional, Congreve, Miles, additional, Deflorian, Francesca, additional, de Graaf, Chris, additional, Zhukov, Andrei, additional, Doré, Andrew S., additional, Mason, Jonathan S., additional, Åqvist, Johan, additional, Cooke, Robert M., additional, Sotelo, Eddy, additional, and Gutiérrez‐de‐Terán, Hugo, additional

Published
2020
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23. X‐Ray Crystallography and Free Energy Calculations Reveal the Binding Mechanism of A 2A Adenosine Receptor Antagonists

Author

Jespers, Willem, primary, Verdon, Grégory, additional, Azuaje, Jhonny, additional, Majellaro, Maria, additional, Keränen, Henrik, additional, García‐Mera, Xerardo, additional, Congreve, Miles, additional, Deflorian, Francesca, additional, Graaf, Chris, additional, Zhukov, Andrei, additional, Doré, Andrew S., additional, Mason, Jonathan S., additional, Åqvist, Johan, additional, Cooke, Robert M., additional, Sotelo, Eddy, additional, and Gutiérrez‐de‐Terán, Hugo, additional

Published
2020
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25. X-Ray crystallography and free energy calculations reveal the binding mechanism of A2A adenosine receptor antagonists

Author

Universidade de Santiago de Compostela. Departamento de Química Orgánica, Jespers, Willem, Verdon, Grégory, Azuaje, Jhonny, Majellaro, María, Keränen, Henrik, García Mera, Xerardo, Congreve, Miles, Deflorian, Francesca, De Graaf, Chris, Zhukov, Andrey, Doré, Andrew S., Mason, Jonathan S., Åqvist, Johan, Cooke, Robert M., Sotelo, Eddy, Gutiérrez de Terán, Hugo, Universidade de Santiago de Compostela. Departamento de Química Orgánica, Jespers, Willem, Verdon, Grégory, Azuaje, Jhonny, Majellaro, María, Keränen, Henrik, García Mera, Xerardo, Congreve, Miles, Deflorian, Francesca, De Graaf, Chris, Zhukov, Andrey, Doré, Andrew S., Mason, Jonathan S., Åqvist, Johan, Cooke, Robert M., Sotelo, Eddy, and Gutiérrez de Terán, Hugo

Abstract

We present a robust protocol based on iterations of free energy perturbation (FEP) calculations, chemical synthesis, biophysical mapping and X-ray crystallography to reveal the binding mode of an antagonist series to the adenosine A2A receptor (AR). Eight A2AAR binding site mutations from biophysical mapping experiments were initially analysed with sidechain FEP simulations, performed on alternate binding modes. The results distinctively supported one binding mode, which was subsequently used to design new chromone derivatives. Their affinities for the A2AAR were experimentally determined and investigated through a cycle of ligandFEP calculations, validating the binding orientation of the different chemical substituents proposed. Subsequent X-ray crystallography of the A2AAR with a low and a high affinity chromone derivative confirmed the predicted binding orientation. The new molecules and structures here reported were driven by free energy calculations, and provide new insights on antagonist binding to the A2AAR, an emerging target in immuno-oncology.

Published
2020

26. X‐Ray Crystallography and Free Energy Calculations Reveal the Binding Mechanism of A2A Adenosine Receptor Antagonists

Author

Universidade de Santiago de Compostela. Centro de Investigación en Química Biolóxica e Materiais Moleculares, Universidade de Santiago de Compostela. Departamento de Química Orgánica, Jespers, Willem, Verdon, Grégory, Azuaje Guerrero, Jhonny Alberto, Majellaro, María, Keränen, Henrik, García Mera, Xerardo Xusto, Congreve, Miles, Deflorian, Francesca, De Graaf, Chris, Zhukov, Andrei, Doré, Andrew S., Mason, Jonathan S., Åqvist, Johan, Cooke, Robert M., Sotelo Pérez, Eddy, Gutiérrez de Terán, Hugo, Universidade de Santiago de Compostela. Centro de Investigación en Química Biolóxica e Materiais Moleculares, Universidade de Santiago de Compostela. Departamento de Química Orgánica, Jespers, Willem, Verdon, Grégory, Azuaje Guerrero, Jhonny Alberto, Majellaro, María, Keränen, Henrik, García Mera, Xerardo Xusto, Congreve, Miles, Deflorian, Francesca, De Graaf, Chris, Zhukov, Andrei, Doré, Andrew S., Mason, Jonathan S., Åqvist, Johan, Cooke, Robert M., Sotelo Pérez, Eddy, and Gutiérrez de Terán, Hugo

Abstract

We present a robust protocol based on iterations of free energy perturbation (FEP) calculations, chemical synthesis, biophysical mapping and X‐ray crystallography to reveal the binding mode of an antagonist series to the A2A adenosine receptor (AR). Eight A2AAR binding site mutations from biophysical mapping experiments were initially analyzed with sidechain FEP simulations, performed on alternate binding modes. The results distinctively supported one binding mode, which was subsequently used to design new chromone derivatives. Their affinities for the A2AAR were experimentally determined and investigated through a cycle of ligand‐FEP calculations, validating the binding orientation of the different chemical substituents proposed. Subsequent X‐ray crystallography of the A2AAR with a low and a high affinity chromone derivative confirmed the predicted binding orientation. The new molecules and structures here reported were driven by free energy calculations, and provide new insights on antagonist binding to the A2AAR, an emerging target in immuno‐oncology

Published
2020

29. Molecular basis for high affinity agonist binding in GPCRs

Author

Warne, Tony, Edwards, Patricia C., Doré, Andrew S., Leslie, Andrew G. W., and Tate, Christopher G.

Subjects
0303 health sciences, 03 medical and health sciences, 0302 clinical medicine, 030217 neurology & neurosurgery, 030304 developmental biology
Abstract

A characteristic of GPCRs in the G protein-coupled state is that the affinity of the agonist often increases significantly, but the molecular basis for this is unclear. We have determined six active-state structures of the β1-adrenoceptor (β1AR) bound to conformation-specific nanobodies in the presence of agonists of varying efficacy. A direct comparison with structures of β1AR in inactive states bound to the identical ligands showed a 24-42% reduction in the volume of the orthosteric binding site. Potential hydrogen bonds were also shorter, and there was up to a 30% increase in the number of atomic contacts between the receptor and ligand. GPCRs are highly conserved, so these factors will likely be essential in increasing the affinity of a wide range of structurally distinct agonists.One Sentence SummaryHigh affinity agonist binding to G protein-coupled GPCRs results from an increase in the number and strength of protein-ligand interactions.

Published
2018
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30. Comparison of Orexin 1 and Orexin 2 Ligand Binding Modes Using X-ray Crystallography and Computational Analysis

Author

Rappas, Mathieu, primary, Ali, Ammar A. E., additional, Bennett, Kirstie A., additional, Brown, Jason D., additional, Bucknell, Sarah J., additional, Congreve, Miles, additional, Cooke, Robert M., additional, Cseke, Gabriella, additional, de Graaf, Chris, additional, Doré, Andrew S., additional, Errey, James C., additional, Jazayeri, Ali, additional, Marshall, Fiona H., additional, Mason, Jonathan S., additional, Mould, Richard, additional, Patel, Jayesh C., additional, Tehan, Benjamin G., additional, Weir, Malcolm, additional, and Christopher, John A., additional

Published
2019
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31. Crystal structures of the human neurokinin 1 receptor in complex with clinically used antagonists

Author

Schöppe, Jendrik; https://orcid.org/0000-0002-2689-5549, Ehrenmann, Janosch; https://orcid.org/0000-0003-4447-9298, Klenk, Christoph; https://orcid.org/0000-0001-5199-7144, Rucktooa, Prakash, Schütz, Marco, Doré, Andrew S, Plückthun, Andreas; https://orcid.org/0000-0003-4191-5306, Schöppe, Jendrik; https://orcid.org/0000-0002-2689-5549, Ehrenmann, Janosch; https://orcid.org/0000-0003-4447-9298, Klenk, Christoph; https://orcid.org/0000-0001-5199-7144, Rucktooa, Prakash, Schütz, Marco, Doré, Andrew S, and Plückthun, Andreas; https://orcid.org/0000-0003-4191-5306

Abstract

Neurokinins (or tachykinins) are peptides that modulate a wide variety of human physiology through the neurokinin G protein-coupled receptor family, implicated in a diverse array of pathological processes. Here we report high-resolution crystal structures of the human NK receptor (NKR) bound to two small-molecule antagonist therapeutics - aprepitant and netupitant and the progenitor antagonist CP-99,994. The structures reveal the detailed interactions between clinically approved antagonists and NKR, which induce a distinct receptor conformation resulting in an interhelical hydrogen-bond network that cross-links the extracellular ends of helices V and VI. Furthermore, the high-resolution details of NKR bound to netupitant establish a structural rationale for the lack of basal activity in NKR. Taken together, these co-structures provide a comprehensive structural basis of NKR antagonism and will facilitate the design of new therapeutics targeting the neurokinin receptor family.

Published
2019

32. X‐Ray Crystallography and Free Energy Calculations Reveal the Binding Mechanism of A2A Adenosine Receptor Antagonists.

Author

Jespers, Willem, Verdon, Grégory, Azuaje, Jhonny, Majellaro, Maria, Keränen, Henrik, García‐Mera, Xerardo, Congreve, Miles, Deflorian, Francesca, Graaf, Chris, Zhukov, Andrei, Doré, Andrew S., Mason, Jonathan S., Åqvist, Johan, Cooke, Robert M., Sotelo, Eddy, and Gutiérrez‐de‐Terán, Hugo

Subjects
ADENOSINES, G protein coupled receptors, CHEMICAL synthesis, BINDING sites
Abstract

We present a robust protocol based on iterations of free energy perturbation (FEP) calculations, chemical synthesis, biophysical mapping and X‐ray crystallography to reveal the binding mode of an antagonist series to the A2A adenosine receptor (AR). Eight A2AAR binding site mutations from biophysical mapping experiments were initially analyzed with sidechain FEP simulations, performed on alternate binding modes. The results distinctively supported one binding mode, which was subsequently used to design new chromone derivatives. Their affinities for the A2AAR were experimentally determined and investigated through a cycle of ligand‐FEP calculations, validating the binding orientation of the different chemical substituents proposed. Subsequent X‐ray crystallography of the A2AAR with a low and a high affinity chromone derivative confirmed the predicted binding orientation. The new molecules and structures here reported were driven by free energy calculations, and provide new insights on antagonist binding to the A2AAR, an emerging target in immuno‐oncology. [ABSTRACT FROM AUTHOR]

Published
2020
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34. Structure-Based Optimization Strategies for G Protein-Coupled Receptor (GPCR) Allosteric Modulators: A Case Study from Analyses of New Metabotropic Glutamate Receptor 5 (mGlu5) X-ray Structures

Author

Christopher, John A., primary, Orgován, Zoltán, additional, Congreve, Miles, additional, Doré, Andrew S., additional, Errey, James C., additional, Marshall, Fiona H., additional, Mason, Jonathan S., additional, Okrasa, Krzysztof, additional, Rucktooa, Prakash, additional, Serrano-Vega, Maria J., additional, Ferenczy, György G., additional, and Keserű, György M., additional

Published
2018
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36. Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons

Author

Weinert, Tobias, primary, Olieric, Natacha, additional, Cheng, Robert, additional, Brünle, Steffen, additional, James, Daniel, additional, Ozerov, Dmitry, additional, Gashi, Dardan, additional, Vera, Laura, additional, Marsh, May, additional, Jaeger, Kathrin, additional, Dworkowski, Florian, additional, Panepucci, Ezequiel, additional, Basu, Shibom, additional, Skopintsev, Petr, additional, Doré, Andrew S., additional, Geng, Tian, additional, Cooke, Robert M., additional, Liang, Mengning, additional, Prota, Andrea E., additional, Panneels, Valerie, additional, Nogly, Przemyslaw, additional, Ermler, Ulrich, additional, Schertler, Gebhard, additional, Hennig, Michael, additional, Steinmetz, Michel O., additional, Wang, Meitian, additional, and Standfuss, Jörg, additional

Published
2017
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38. Erratum: Corrigendum: Crystal structure of the GLP-1 receptor bound to a peptide agonist

Author

Jazayeri, Ali, primary, Rappas, Mathieu, additional, Brown, Alastair J. H., additional, Kean, James, additional, Errey, James C., additional, Robertson, Nathan J., additional, Fiez-Vandal, Cédric, additional, Andrews, Stephen P., additional, Congreve, Miles, additional, Bortolato, Andrea, additional, Mason, Jonathan S., additional, Baig, Asma H., additional, Teobald, Iryna, additional, Doré, Andrew S., additional, Weir, Malcolm, additional, Cooke, Robert M., additional, and Marshall, Fiona H., additional

Published
2017
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39. Crystal structure of the GLP-1 receptor bound to a peptide agonist

Author

Jazayeri, Ali, primary, Rappas, Mathieu, additional, Brown, Alastair J. H., additional, Kean, James, additional, Errey, James C., additional, Robertson, Nathan J., additional, Fiez-Vandal, Cédric, additional, Andrews, Stephen P., additional, Congreve, Miles, additional, Bortolato, Andrea, additional, Mason, Jonathan S., additional, Baig, Asma H., additional, Teobald, Iryna, additional, Doré, Andrew S., additional, Weir, Malcolm, additional, Cooke, Robert M., additional, and Marshall, Fiona H., additional

Published
2017
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40. Structural insight into allosteric modulation of protease-activated receptor 2

Author

Cheng, Robert K. Y., primary, Fiez-Vandal, Cédric, additional, Schlenker, Oliver, additional, Edman, Karl, additional, Aggeler, Birte, additional, Brown, Dean G., additional, Brown, Giles A., additional, Cooke, Robert M., additional, Dumelin, Christoph E., additional, Doré, Andrew S., additional, Geschwindner, Stefan, additional, Grebner, Christoph, additional, Hermansson, Nils-Olov, additional, Jazayeri, Ali, additional, Johansson, Patrik, additional, Leong, Louis, additional, Prihandoko, Rudi, additional, Rappas, Mathieu, additional, Soutter, Holly, additional, Snijder, Arjan, additional, Sundström, Linda, additional, Tehan, Benjamin, additional, Thornton, Peter, additional, Troast, Dawn, additional, Wiggin, Giselle, additional, Zhukov, Andrei, additional, Marshall, Fiona H., additional, and Dekker, Niek, additional

Published
2017
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41. Controlling the Dissociation of Ligands from the Adenosine A2A Receptor through Modulation of Salt Bridge Strength

Author

Segala, Elena, primary, Guo, Dong, additional, Cheng, Robert K. Y., additional, Bortolato, Andrea, additional, Deflorian, Francesca, additional, Doré, Andrew S., additional, Errey, James C., additional, Heitman, Laura H., additional, IJzerman, Adriaan P., additional, Marshall, Fiona H., additional, and Cooke, Robert M., additional

Published
2016
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42. Comparison of Orexin 1 and Orexin 2 Ligand Binding Modes Using X-ray Crystallography and Computational Analysis

Author

Rappas, Mathieu, Ali, Ammar A. E., Bennett, Kirstie A., Brown, Jason D., Bucknell, Sarah J., Congreve, Miles, Cooke, Robert M., Cseke, Gabriella, de Graaf, Chris, Doré, Andrew S., Errey, James C., Jazayeri, Ali, Marshall, Fiona H., Mason, Jonathan S., Mould, Richard, Patel, Jayesh C., Tehan, Benjamin G., Weir, Malcolm, and Christopher, John A.

Abstract

The orexin system, which consists of the two G protein-coupled receptors OX1and OX2, activated by the neuropeptides OX-A and OX-B, is firmly established as a key regulator of behavioral arousal, sleep, and wakefulness and has been an area of intense research effort over the past two decades. X-ray structures of the receptors in complex with 10 new antagonist ligands from diverse chemotypes are presented, which complement the existing structural information for the system and highlight the critical importance of lipophilic hotspots and water molecules for these peptidergic GPCR targets. Learnings from the structural information regarding the utility of pharmacophore models and how selectivity between OX1and OX2can be achieved are discussed.

Published
2020
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43. Fragment and Structure-Based Drug Discovery for a Class C GPCR: Discovery of the mGlu5 Negative Allosteric Modulator HTL14242 (3-Chloro-5-[6-(5-fluoropyridin-2-yl)pyrimidin-4-yl]benzonitrile)

Author

Christopher, John A., primary, Aves, Sarah J., additional, Bennett, Kirstie A., additional, Doré, Andrew S., additional, Errey, James C., additional, Jazayeri, Ali, additional, Marshall, Fiona H., additional, Okrasa, Krzysztof, additional, Serrano-Vega, Maria J., additional, Tehan, Benjamin G., additional, Wiggin, Giselle R., additional, and Congreve, Miles, additional

Published
2015
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44. Structure-Based Optimization Strategies for G Protein-Coupled Receptor (GPCR) Allosteric Modulators: A Case Study from Analyses of New Metabotropic Glutamate Receptor 5 (mGlu5) X-ray Structures

Author

Christopher, John A., Orgován, Zoltán, Congreve, Miles, Doré, Andrew S., Errey, James C., Marshall, Fiona H., Mason, Jonathan S., Okrasa, Krzysztof, Rucktooa, Prakash, Serrano-Vega, Maria J., Ferenczy, György G., and Keserű, György M.

Abstract

Two interesting new X-ray structures of negative allosteric modulator (NAM) ligands for the mGlu5receptor, M-MPEP (3) and fenobam (4), are reported. The new structures show how the binding of the ligands induces different receptor water channel conformations to previously published structures. The structure of fenobam, where a urea replaces the acetylenic linker in M-MPEP and mavoglurant, reveals a binding mode where the ligand is rotated by 180° compared to a previously proposed docking model. The need for multiple ligand structures for accurate GPCR structure-based drug design is demonstrated by the different growing vectors identified for the head groups of M-MPEP and mavoglurant and by the unexpected water-mediated receptor interactions of a new chemotype represented by fenobam. The implications of the new structures for ligand design are discussed, with extensive analysis of the energetics of the water networks of both pseudoapo and bound structures providing a new design strategy for allosteric modulators.

Published
2019
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45. Electron microscopy of Xrcc4 and the DNA ligase IV-Xrcc4 DNA repair complex

Author

Recuero-Checa, María Ángeles, Doré, Andrew S., Arias-Palomo, Ernesto, Rivera-Calzada, Angel, Scheres, Sjors H.W., Maman, Joseph D., Pearl, Laurence H., Llorca, Óscar, Recuero-Checa, María Ángeles, Doré, Andrew S., Arias-Palomo, Ernesto, Rivera-Calzada, Angel, Scheres, Sjors H.W., Maman, Joseph D., Pearl, Laurence H., and Llorca, Óscar

Abstract

The DNA ligase IV–Xrcc4 complex is responsible for the ligation of broken DNA ends in the non-homologous end-joining (NHEJ) pathway of DNA double strand break repair in mammals. Mutations in DNA ligase IV (Lig4) lead to immunodeficiency and radiosensitivity in humans. Only partial structural information for Lig4 and Xrcc4 is available, while the structure of the full-length proteins and their arrangement within the Lig4–Xrcc4 complex is unknown. The C-terminal domain of Xrcc4, whose structure has not been solved, contains phosphorylation sites for DNA-PKcs and is phylogenetically conserved, indicative of a regulatory role in NHEJ. Here, we have purified full length Xrcc4 and the Lig4–Xrcc4 complex, and analysed their structure by single-particle electron microscopy. The three-dimensional structure of Xrcc4 at a resolution of ∼37 Å reveals that the C-terminus of Xrcc4 forms a dimeric globular domain connected to the N-terminus by a coiled-coil. The N- and C-terminal domains of Xrcc4 locate at opposite ends of an elongated molecule. The electron microscopy images of the Lig4–Xrcc4 complex were examined by two-dimensional image processing and a double-labelling strategy, identifying the site of the C-terminus of Xrcc4 and the catalytic core of Lig4 within the complex. The catalytic domains of Lig4 were found to be in the vicinity of the N-terminus of Xrcc4. We provide a first sight of the structural organization of the Lig4–Xrcc4 complex, which suggests that the BRCT domains could provide the link of the ligase to Xrcc4 while permitting some movements of the catalytic domains of Lig4. This arrangement may facilitate the ligation of diverse configurations of damaged DNA

Published
2009

46. Biophysical Fragment Screening of the β1-Adrenergic Receptor: Identification of High Affinity Arylpiperazine Leads Using Structure-Based Drug Design

Author

Christopher, John A., primary, Brown, Jason, additional, Doré, Andrew S., additional, Errey, James C., additional, Koglin, Markus, additional, Marshall, Fiona H., additional, Myszka, David G., additional, Rich, Rebecca L., additional, Tate, Christopher G., additional, Tehan, Benjamin, additional, Warne, Tony, additional, and Congreve, Miles, additional

Published
2013
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48. Outrunning free radicals in room-temperature macromolecular crystallography

Author

Owen, Robin L., primary, Axford, Danny, additional, Nettleship, Joanne E., additional, Owens, Raymond J., additional, Robinson, James I., additional, Morgan, Ann W., additional, Doré, Andrew S., additional, Lebon, Guillaume, additional, Tate, Christopher G., additional, Fry, Elizabeth E., additional, Ren, Jingshan, additional, Stuart, David I., additional, and Evans, Gwyndaf, additional

Published
2012
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49. Discovery of 1,2,4-Triazine Derivatives as Adenosine A2A Antagonists using Structure Based Drug Design

Author

Congreve, Miles, primary, Andrews, Stephen P., additional, Doré, Andrew S., additional, Hollenstein, Kaspar, additional, Hurrell, Edward, additional, Langmead, Christopher J., additional, Mason, Jonathan S., additional, Ng, Irene W., additional, Tehan, Benjamin, additional, Zhukov, Andrei, additional, Weir, Malcolm, additional, and Marshall, Fiona H., additional

Published
2012
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50. Structure of the Adenosine A2A Receptor in Complex with ZM241385 and the Xanthines XAC and Caffeine

Author

Doré, Andrew S., primary, Robertson, Nathan, additional, Errey, James C., additional, Ng, Irene, additional, Hollenstein, Kaspar, additional, Tehan, Ben, additional, Hurrell, Edward, additional, Bennett, Kirstie, additional, Congreve, Miles, additional, Magnani, Francesca, additional, Tate, Christopher G., additional, Weir, Malcolm, additional, and Marshall, Fiona H., additional

Published
2011
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