Combining native and 'omics' mass spectrometry to identify endogenous ligands bound to membrane proteins
Ligands bound to protein assemblies provide critical information for function, yet are often difficult to capture and define. Here we develop a top-down method, 'nativeomics', unifying 'omics' (lipidomics, proteomics, metabolomics) analysis with native mass spectrometry to identi...
| Main Authors: | , , , , , , , , , , , , , , , , , , |
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| 格式: | Journal article |
| 語言: | English |
| 出版: |
Springer Nature
2020
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| _version_ | 1826302782377820160 |
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| author | Gault, J Liko, I Landreh, M Shutinm, D Bolla, JR Jefferies, D Agasid, M Yen, H-Y Ladds, MJGW Lane, DP Khalid, S Mullen, C Remes, PM Huguet, R McAlister, G Goodwin, M Viner, R Syka, JEP Robinson, CV |
| author_facet | Gault, J Liko, I Landreh, M Shutinm, D Bolla, JR Jefferies, D Agasid, M Yen, H-Y Ladds, MJGW Lane, DP Khalid, S Mullen, C Remes, PM Huguet, R McAlister, G Goodwin, M Viner, R Syka, JEP Robinson, CV |
| author_sort | Gault, J |
| collection | OXFORD |
| description | Ligands bound to protein assemblies provide critical information for function, yet are often difficult to capture and define. Here we develop a top-down method, 'nativeomics', unifying 'omics' (lipidomics, proteomics, metabolomics) analysis with native mass spectrometry to identify ligands bound to membrane protein assemblies. By maintaining the link between proteins and ligands, we define the lipidome/metabolome in contact with membrane porins and a mitochondrial translocator to discover potential regulators of protein function. |
| first_indexed | 2024-03-07T05:52:42Z |
| format | Journal article |
| id | oxford-uuid:e96f7511-216e-453f-85bf-15c9cc18f0e6 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:52:42Z |
| publishDate | 2020 |
| publisher | Springer Nature |
| record_format | dspace |
| spelling | oxford-uuid:e96f7511-216e-453f-85bf-15c9cc18f0e62022-03-27T10:54:24ZCombining native and 'omics' mass spectrometry to identify endogenous ligands bound to membrane proteinsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:e96f7511-216e-453f-85bf-15c9cc18f0e6EnglishSymplectic ElementsSpringer Nature 2020Gault, JLiko, ILandreh, MShutinm, DBolla, JRJefferies, DAgasid, MYen, H-YLadds, MJGWLane, DPKhalid, SMullen, CRemes, PMHuguet, RMcAlister, GGoodwin, MViner, RSyka, JEPRobinson, CVLigands bound to protein assemblies provide critical information for function, yet are often difficult to capture and define. Here we develop a top-down method, 'nativeomics', unifying 'omics' (lipidomics, proteomics, metabolomics) analysis with native mass spectrometry to identify ligands bound to membrane protein assemblies. By maintaining the link between proteins and ligands, we define the lipidome/metabolome in contact with membrane porins and a mitochondrial translocator to discover potential regulators of protein function. |
| spellingShingle | Gault, J Liko, I Landreh, M Shutinm, D Bolla, JR Jefferies, D Agasid, M Yen, H-Y Ladds, MJGW Lane, DP Khalid, S Mullen, C Remes, PM Huguet, R McAlister, G Goodwin, M Viner, R Syka, JEP Robinson, CV Combining native and 'omics' mass spectrometry to identify endogenous ligands bound to membrane proteins |
| title | Combining native and 'omics' mass spectrometry to identify endogenous ligands bound to membrane proteins |
| title_full | Combining native and 'omics' mass spectrometry to identify endogenous ligands bound to membrane proteins |
| title_fullStr | Combining native and 'omics' mass spectrometry to identify endogenous ligands bound to membrane proteins |
| title_full_unstemmed | Combining native and 'omics' mass spectrometry to identify endogenous ligands bound to membrane proteins |
| title_short | Combining native and 'omics' mass spectrometry to identify endogenous ligands bound to membrane proteins |
| title_sort | combining native and omics mass spectrometry to identify endogenous ligands bound to membrane proteins |
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