DySCo: Quantitating associations of membrane proteins using two-color single-molecule tracking

Paul D. Dunne; Ricardo A. Fernandes; James McColl; Won Yoon Ji; John R. James; Simon J. Davis; David Klenerman

doi:10.1016/j.bpj.2009.05.046

DySCo: Quantitating associations of membrane proteins using two-color single-molecule tracking

Paul D. Dunne
, Ricardo A. Fernandes
, James McColl
, Won Yoon Ji
, John R. James
, Simon J. Davis
, David Klenerman

Research output: Contribution to journal › Article › peer-review

61 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	L5-L7
Journal	Biophysical Journal
Volume	97
Issue number	4
DOIs	https://doi.org/10.1016/j.bpj.2009.05.046
Publication status	Published - 2009 Aug 19
Externally published	Yes

Bibliographical note

Funding Information:
This project was funded by the Engineering and Physical Sciences Research Council, Biotechnology and Biological Sciences Research Council, Medical Research Council and The Wellcome Trust, UK, and by Fundação para a Ciência e a Tecnologia, Portugal.

ASJC Scopus subject areas

Biophysics

Access to Document

10.1016/j.bpj.2009.05.046

Cite this

@article{54ae76b2dea94d469a3411574649c640,

title = "DySCo: Quantitating associations of membrane proteins using two-color single-molecule tracking",

abstract = "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.",

author = "Dunne, \{Paul D.\} and Fernandes, \{Ricardo A.\} and James McColl and Ji, \{Won Yoon\} and James, \{John R.\} and Davis, \{Simon J.\} and David Klenerman",

note = "Funding Information: This project was funded by the Engineering and Physical Sciences Research Council, Biotechnology and Biological Sciences Research Council, Medical Research Council and The Wellcome Trust, UK, and by Funda{\c c}{\~a}o para a Ci{\^e}ncia e a Tecnologia, Portugal. ",

year = "2009",

month = aug,

day = "19",

doi = "10.1016/j.bpj.2009.05.046",

language = "English",

volume = "97",

pages = "L5--L7",

journal = "Biophysical Journal",

issn = "0006-3495",

publisher = "Elsevier Inc.",

number = "4",

}

TY - JOUR

T1 - DySCo

T2 - Quantitating associations of membrane proteins using two-color single-molecule tracking

AU - Dunne, Paul D.

AU - Fernandes, Ricardo A.

AU - McColl, James

AU - Ji, Won Yoon

AU - James, John R.

AU - Davis, Simon J.

AU - Klenerman, David

N1 - Funding Information: This project was funded by the Engineering and Physical Sciences Research Council, Biotechnology and Biological Sciences Research Council, Medical Research Council and The Wellcome Trust, UK, and by Fundação para a Ciência e a Tecnologia, Portugal.

PY - 2009/8/19

Y1 - 2009/8/19

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/69349092619

U2 - 10.1016/j.bpj.2009.05.046

DO - 10.1016/j.bpj.2009.05.046

M3 - Article

C2 - 19686638

AN - SCOPUS:69349092619

SN - 0006-3495

VL - 97

SP - L5-L7

JO - Biophysical Journal

JF - Biophysical Journal

IS - 4

ER -

DySCo: Quantitating associations of membrane proteins using two-color single-molecule tracking

Abstract

Bibliographical note

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this