Explore the words cloud of the ENABLE project. It provides you a very rough idea of what is the project "ENABLE" about.
The following table provides information about the project.
THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD
|Coordinator Country||United Kingdom [UK]|
|Total cost||2˙481˙744 €|
|EC max contribution||2˙481˙744 € (100%)|
1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
|Duration (year-month-day)||from 2016-06-01 to 2021-05-31|
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|1||THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD||UK (OXFORD)||coordinator||2˙481˙744.00|
Excising a membrane protein from its natural environment, preserving the lipid bilayer, and characterising the lipids that surround it is the ‘holy grail’ of membrane protein biophysics. However, with some 40,000 different lipid structures the challenges we face in understanding selective binding arise not just from the complexity and dynamics of the lipidome, but also from the transient nature of protein lipid interactions. To overcome these challenges we will take mass spectrometry (MS) into a new era, allowing, for the first time, the study of proteins in an environment as close as possible to the natural one. To do this we will (i) characterise protein lipid interactions by employing a high resolution Orbitrap mass spectrometer developed in-house, specifically for membrane proteins, (ii) capture the native lipid environment in vehicles suitable for use in conjunction with MS, and (iii) establish a new platform to be known as integral membrane protein desorption electrospray ionization (impDESI). Designed and built in-house impDESI is capable of releasing membrane proteins from surfaces directly into the mass spectrometer (MS). We will develop impDESI for membrane mimetics, and subsequently portions of natural membranes, enabling us to extract proteins with oligomeric state preserved and native lipid binding intact. The development of impDESI, in conjunction with high resolution Orbitrap MS, and coupled with the optimisation of membrane mimetics, has the potential to radically transform our understanding of native lipid binding, not only directly, but also temporally and spatially. Together these advances will answer key questions about how lipids modulate protein interfaces, occupy different binding sites, modulate membrane protein structure and modify function in vivo. Given the importance of membrane proteins as potential drugs targets understanding their modulation by lipids would be a major step towards more effective drug development.
|year||authors and title||journal||last update|
Hsin-Yung Yen, Jonathan T. S. Hopper, Idlir Liko, Timothy M. Allison, Ya Zhu, Dejian Wang, Monika Stegmann, Shabaz Mohammed, Beili Wu, Carol V. Robinson
Ligand binding to a G proteinâ€“coupled receptor captured in a mass spectrometer
published pages: e1701016, ISSN: 2375-2548, DOI: 10.1126/sciadv.1701016
|Science Advances 3/6||2019-02-28|
Hsin-Yung Yen, Kin Kuan Hoi, Idlir Liko, George Hedger, Michael R. Horrell, Wanling Song, Di Wu, Philipp Heine, Tony Warne, Yang Lee, Byron Carpenter, Andreas PlÃ¼ckthun, Christopher G. Tate, Mark S. P. Sansom, Carol V. Robinson
PtdIns(4,5)P2 stabilizes active states of GPCRs and enhances selectivity of G-protein coupling
published pages: 423-427, ISSN: 0028-0836, DOI: 10.1038/s41586-018-0325-6
Dror S. Chorev, Lindsay A. Baker, Di Wu, Victoria Beilsten-Edmands, Sarah L. Rouse, Tzviya Zeev-Ben-Mordehai, Chimari Jiko, Firdaus Samsudin, Christoph Gerle, Syma Khalid, Alastair G. Stewart, Stephen J. Matthews, Kay GrÃ¼newald, Carol V. Robinson
Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry
published pages: 829-834, ISSN: 0036-8075, DOI: 10.1126/science.aau0976
Michael Landreh, Erik G. Marklund, Povilas Uzdavinys, Matteo T. Degiacomi, Mathieu Coincon, Joseph Gault, Kallol Gupta, Idlir Liko, Justin L. P. Benesch, David Drew, Carol V. Robinson
Integrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters
published pages: 13993, ISSN: 2041-1723, DOI: 10.1038/ncomms13993
|Nature Communications 8||2019-02-28|
Stephen Ambrose, Nicholas G. Housden, Kallol Gupta, Jieyuan Fan, Paul White, Hsin-Yung Yen, Julien Marcoux, Colin Kleanthous, Jonathan T. S. Hopper, Carol V. Robinson
Native Desorption Electrospray Ionization Liberates Soluble and Membrane Protein Complexes from Surfaces
published pages: 14463-14468, ISSN: 1433-7851, DOI: 10.1002/anie.201704849
|Angewandte Chemie International Edition 56/46||2019-02-28|
Kallol Gupta, Jingwen Li, Idlir Liko, Joseph Gault, Cherine Bechara, Di Wu, Jonathan T S Hopper, Kevin Giles, Justin L P Benesch, Carol V Robinson
Identifying key membrane protein lipid interactions using mass spectrometry
published pages: 1106-1120, ISSN: 1754-2189, DOI: 10.1038/nprot.2018.014
|Nature Protocols 13/5||2019-02-28|
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The information about "ENABLE" are provided by the European Opendata Portal: CORDIS opendata.