DySCo: Quantitating associations of membrane proteins using two-color single-molecule tracking
We present a general method called dynamic single-molecule colocalization for quantitating the associations of single cell surface molecules labeled with distinct autofluorescent proteins. The chief advantages of the new quantitative approach are that, in addition to stable interactions, it is capab...
Main Authors: | , , , , , , |
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Formato: | Journal article |
Idioma: | English |
Publicado em: |
2009
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_version_ | 1826268286710448128 |
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author | Dunne, P Fernandes, R McColl, J Ji, W James, JR Davis, S Klenerman, D |
author_facet | Dunne, P Fernandes, R McColl, J Ji, W James, JR Davis, S Klenerman, D |
author_sort | Dunne, P |
collection | OXFORD |
description | We present a general method called dynamic single-molecule colocalization for quantitating the associations of single cell surface molecules labeled with distinct autofluorescent proteins. The chief advantages of the new quantitative approach are that, in addition to stable interactions, it is capable of measuring nonconstitutive associations, such as those induced by the cytoskeleton, and it is applicable to situations where the number of molecules is small. © 2009 by the Biophysical Society. |
first_indexed | 2024-03-06T21:07:21Z |
format | Journal article |
id | oxford-uuid:3cedb359-8472-4d6c-b23c-1ba593aae848 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T21:07:21Z |
publishDate | 2009 |
record_format | dspace |
spelling | oxford-uuid:3cedb359-8472-4d6c-b23c-1ba593aae8482022-03-26T14:16:27ZDySCo: Quantitating associations of membrane proteins using two-color single-molecule trackingJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3cedb359-8472-4d6c-b23c-1ba593aae848EnglishSymplectic Elements at Oxford2009Dunne, PFernandes, RMcColl, JJi, WJames, JRDavis, SKlenerman, DWe present a general method called dynamic single-molecule colocalization for quantitating the associations of single cell surface molecules labeled with distinct autofluorescent proteins. The chief advantages of the new quantitative approach are that, in addition to stable interactions, it is capable of measuring nonconstitutive associations, such as those induced by the cytoskeleton, and it is applicable to situations where the number of molecules is small. © 2009 by the Biophysical Society. |
spellingShingle | Dunne, P Fernandes, R McColl, J Ji, W James, JR Davis, S Klenerman, D DySCo: Quantitating associations of membrane proteins using two-color single-molecule tracking |
title | DySCo: Quantitating associations of membrane proteins using two-color single-molecule tracking |
title_full | DySCo: Quantitating associations of membrane proteins using two-color single-molecule tracking |
title_fullStr | DySCo: Quantitating associations of membrane proteins using two-color single-molecule tracking |
title_full_unstemmed | DySCo: Quantitating associations of membrane proteins using two-color single-molecule tracking |
title_short | DySCo: Quantitating associations of membrane proteins using two-color single-molecule tracking |
title_sort | dysco quantitating associations of membrane proteins using two color single molecule tracking |
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