Guide FRET and FLIM Techniques (Laboratory Techniques in Biochemistry and Molecular Biology)

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This was realised by acquiring FLIM data of a reference dye solution rhodamine 6G in some of the plate wells and fitting the measured decay data to a monoexponential model in order to precisely determine the relative excitation time i. This information was combined with the measurement of a scattering sample to construct the IRF that is convolved with the exponential decay model to provide the function to which the experimental FLIM data is fitted.

How to cite this article : Margineanu, A. The error has not been fixed in the paper. Eggeling, C. Lens-based fluorescence nanoscopy. Patterson, G. Superresolution imaging using single-molecule localization. Zanella, F. High content screening: seeing is believing. Trends Biotechnol. Jares-Erijman, E.

Imaging molecular interactions in living cells by FRET microscopy. Hoppe, A. Fluorescence resonance energy transfer-based stoichiometry in living cells. Chen, H. Measurement of FRET efficiency and ratio of donor to acceptor concentration in living cells. Biophys, J.

Bader, A. Imaging of protein cluster sizes by means of confocal time-gated fluorescence anisotropy microscopy. Express 15 , — Warren, S. Homo-FRET based biosensors and their application to multiplexed imaging of signalling events in live cells. Matthews, D. A multi-functional imaging approach to high-content protein interaction screening. Marcu L. Kumar, S. FLIM FRET technology for drug discovery: automated multiwell-plate high-content analysis, multiplexed readouts and application in situ. ChemPhysChem 12 , — How many photons are necessary for fluorescence-lifetime measurements?

Digman, M. The phasor approach to fluorescence lifetime imaging analysis. Eichorst, J. Engelborghs, Y. Chan, J. Scheel, H. Oh, H.

Publications

Cancer Res. Praskova, M. Biochem J. Khokhlatchev, A. Identification of a novel Ras-regulated proapoptotic pathway. Guo, C. Ikeda, M. Ras-association domain family protein 6 induces apoptosis via both caspase-dependent and caspase-independent pathways. Cell Res. Signal 2 , ra59 Del Re, D. Park, J. Sherwood, V. Hwang, E. USA , — Ni, L. Structure 21 , — Acta Crystallogr. D Biol.


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Miertzschke, M. Stieglitz, B. EMBO J. Rodriguez-Viciana, P. Signaling specificity by Ras family GTPases is determined by the full spectrum of effectors they regulate. Avruch, J. Methods Enzymol. Ciani, B. Molecular basis of coiled-coil oligomerization-state specificity. Moutevelis, E. A periodic table of coiled-coil protein structures. Rapid global fitting of large fluorescence lifetime imaging microscopy datasets. Raab, M. Barlow, D. Helix geometry in proteins.

Vogel, S.

The impact of heterogeneity and dark acceptor states on FRET: Implications for using fluorescent protein donors and acceptors. Koturenkiene, A. PhD thesis, University Bochum Constantinescu Aruxandei, D. Dimerization-induced folding of MST1 SARAH and the influence of the intrinsically unstructured inhibitory domain: low thermodynamic stability of monomer. Biochemistry 50 , — Makbul, C. Biochemistry 52 , — Song, Y. Development of FRET assay into quantitative and high-throughput screening technology platforms for protein—protein interactions.

Protein interaction affinity determination by quantitative FRET technology. Chakraborty, S. PLoS One 10 , e Du, Y. A time-resolved fluorescence resonance energy transfer assay for high-throughput screening of protein—protein interaction inhibitors. Assay Drug Dev. Optics 12 , Mehta, K. A computational approach to inferring cellular protein binding affinities from quantitative fluorescence resonance energy transfer imaging. Proteomics 9 , — Day, R. Methods 66 , — Hom, E. Analysis of coupled bimolecular reaction kinetics and diffusion by two-color fluorescence correlation spectroscopy: enhanced resolution of kinetics by resonance energy transfer.

Foo, Y. Factors affecting the quantification of biomolecular interactions by fluorescence cross-correlation spectroscopy. Hohng, S. Maciej Zborowski. Van Regenmortel. Max M. Theodorus W. Arnis Kuksis. Home Contact us Help Free delivery worldwide. Free delivery worldwide. Bestselling Series.

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FRET and FLIM techniques

Popular Features. New Releases. Both have become staple techniques in many biological and biophysical fields. Product details Format Paperback pages Dimensions x x Other books in this series. Add to basket. Synthetic Peptides as Antigens: Volume 28 M. Synthetic Peptides as Antigens: Volume 28 S. Dry Chemistry: Volume 25 O. Table of contents Chapter 1. Robert M. Clegg Chapter 2. Peter J. Verveer and Quentin Hanley. Chapter 3. Hans C. Gerritsen, A.

Agronskaia, A. Bader, A.


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  3. FRET and FLIM Techniques: Volume 33.
  4. FRET with FLIM | Learn & Share | Leica Microsystems;
  5. Quantitative In-vivo Biochemistry?
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  7. Chapter 4. Multidimensional fluorescence imaging. Talbot, M. John Lever, Andrew J. Stamp, Mark A. Neil and Paul M. French Chapter 5. Visible fluorescent proteins for FRET.

    Laboratory Techniques in Biochemistry and Molecular Biology, Volume 33

    Gert-Jan Kremers and Joachim Goedhart. Chapter 6.

    Quantitative In-vivo Biochemistry

    Chapter 7. Filter FRET: quantitative imaging of sensitized emission. Kees Jalink and Jacco van Rheenen. Chapter 8.