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  Imaging molecular interactions in cells by dynamic and static fluorescence anisotropy (rFLIM and emFRET)

Lidke, D. S., Nagy, P., Barisas, B. G., Heintzmann, R., Post, J. N., Lidke, K. A., et al. (2003). Imaging molecular interactions in cells by dynamic and static fluorescence anisotropy (rFLIM and emFRET). Biochemical Society Transactions, 31(5), 1020-1027. Retrieved from http://www.biochemsoctrans.org/bst/031/1020/0311020.pdf.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-F1C5-4 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-EA5F-F
Genre: Journal Article

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 Creators:
Lidke, D. S.1, Author           
Nagy, P.1, Author           
Barisas, B. G., Author
Heintzmann, R.1, Author           
Post, J. N.1, Author           
Lidke, K. A.1, Author           
Clayton, A. H. A.1, Author           
Arndt-Jovin, D. J.1, Author           
Jovin, T. M.1, Author           
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1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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Free keywords: fluorescence, polarization, microscopy, erbB, receptor, FRET
 Abstract: We report the implementation and exploitation of fluorescence polarization measurements, in the form of anisotropy-lifetime (rFLIM) and resonance energy migration (emFRET) modalities, for wide-field, confocal laser scanning, and flow cytometric microscopy of cells. These methods permit the assessment of rotational motion, association, and proximity of cellular proteins in vivo. They are particularly applicable to probes generated by fusions of Visible Fluorescence Proteins (VFPs), as exemplified by studies of the erbB receptor tyrosine kinases involved in growth-factor mediated signal transduction.

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Language(s): eng - English
 Dates: 2003
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: eDoc: 42768
URI: http://www.biochemsoctrans.org/bst/031/1020/0311020.pdf
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Title: Biochemical Society Transactions
Source Genre: Journal
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Pages: - Volume / Issue: 31 (5) Sequence Number: - Start / End Page: 1020 - 1027 Identifier: -