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...

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Detalles Bibliográficos
Autores principales: Dunne, Paul D., Fernandes, Ricardo A., McColl, James, Yoon, Ji Won, James, John R., Davis, Simon J., Klenerman, David
Formato: Texto
Lenguaje:English
Publicado: The Biophysical Society 2009
Materias:
Biophysical Letter
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2726305/
https://www.ncbi.nlm.nih.gov/pubmed/19686638
http://dx.doi.org/10.1016/j.bpj.2009.05.046
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author Dunne, Paul D.
Fernandes, Ricardo A.
McColl, James
Yoon, Ji Won
James, John R.
Davis, Simon J.
Klenerman, David
author_facet Dunne, Paul D.
Fernandes, Ricardo A.
McColl, James
Yoon, Ji Won
James, John R.
Davis, Simon J.
Klenerman, David
author_sort Dunne, Paul D.
collection PubMed
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.
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spelling pubmed-27263052009-08-19 DySCo: Quantitating Associations of Membrane Proteins Using Two-Color Single-Molecule Tracking Dunne, Paul D. Fernandes, Ricardo A. McColl, James Yoon, Ji Won James, John R. Davis, Simon J. Klenerman, David Biophys J Biophysical Letter 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. The Biophysical Society 2009-08-19 /pmc/articles/PMC2726305/ /pubmed/19686638 http://dx.doi.org/10.1016/j.bpj.2009.05.046 Text en © 2009 by the Biophysical Society. https://creativecommons.org/licenses/by-nc-nd/3.0/This is an open access article under the CC BY NC ND license (https://creativecommons.org/licenses/by-nc-nd/3.0/).
spellingShingle Biophysical Letter
Dunne, Paul D.
Fernandes, Ricardo A.
McColl, James
Yoon, Ji Won
James, John R.
Davis, Simon J.
Klenerman, David
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
topic Biophysical Letter
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2726305/
https://www.ncbi.nlm.nih.gov/pubmed/19686638
http://dx.doi.org/10.1016/j.bpj.2009.05.046
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