The DOI matches its Crossref record.
Photobleaching and Sensitized Emission-Based Methods for the Detection of Förster Resonance Energy Transfer
Abstract
Förster resonance energy transfer (FRET) is a non-radiative interaction between two molecules that happens at distances in the range of a few nanometers. Using FRET interactions between suitably selected fluorophores allows to study molecular interactions or conformational changes of single molecules on fluorescence microscopes even though the optical resolution of the microscope is limited to distances that are almost two orders of magnitude higher.In this chapter several variants of FRET detection methods are described that are based either on the targeted photobleaching of one of the participating molecule species or on the direct detection of the fluorescence signal that is created as a result of the FRET interactions.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
For FRET analysis, donor-only (Cy3) and acceptor-only (Cy5) samples were imaged in each imaging session to calculate the donor-emission crosstalk with the acceptor emission (beta parameter) and the direct excitation of the acceptor by the donor excitation laser line (gamma parameter).
“For FRET analysis, donor-only (Cy3) and acceptor-only (Cy5) samples were imaged in each imaging session to calculate the donor-emission crosstalk with the acceptor emission (beta parameter) and the direct excitation of the acceptor by the donor excitation laser line (gamma parameter) [75, 80].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [80]
Citations
Cites
No references could be resolved yet.
Research works printed but not linked: 39
- Förster T (1948) Zwischenmolekulare energiewanderung und fluoreszenz. Ann Phys 437(1–2):55–75 · DOI · Paper page
- Bastiaens P, Majoul IV, Verveer PJ, Söling H-D, Jovin TM (1996) Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin. EMBO J 15(16):4246–4253 · DOI
- Karpova T, Baumann C, He L, Wu X, Grammer A, Lipsky P, Hager G, McNally J (2003) Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser. J Microsc 209(1):56–70 · DOI
- Wouters FS, Bastiaens PI, Wirtz KW, Jovin TM (1998) FRET microscopy demonstrates molecular association of non-specific lipid transfer protein (nsL-TP) with fatty acid oxidation enzymes in peroxisomes. EMBO J 17(24):7179–7189 · DOI
- Jovin TM, Arndt-Jovin DJ (1989) FRET microscopy: digital imaging of fluorescence resonance energy transfer. Application in cell biology. In: Kohen E, Ploem JS, Hirschberg JG (eds) Cell structure and function by microspectrofluorometry. Academic Press, Orlando, pp 99–117 · DOI
- Miyawaki A, Llopis J, Heim R, McCaffery JM, Adams JA, Ikura M, Tsien RY (1997) Fluorescent indicators for Ca 2+ based on green fluorescent proteins and calmodulin. Nature 388(6645):882 · DOI
- Schindelin J, Arganda-Carreras I, Frise E, Kaynig V, Longair M, Pietzsch T, Preibisch S, Rueden C, Saalfeld S, Schmid B, Tinevez JY, White DJ, Hartenstein V, Eliceiri K, Tomancak P, Cardona A (2012) Fiji: an open-source platform for biological-image analysis. Nat Methods 9(7):676–682. https://doi.org/10.1038/nmeth.2019 · DOI · Paper page
- Amiri H, Schultz G, Schaefer M (2003) FRET-based analysis of TRPC subunit stoichiometry. Cell Calcium 33(5–6):463–470 · DOI
- Youvan DC, Silva CM, Bylina EJ, Coleman WJ, Dilworth MR, Yang MM (2003) Calibration of fluorescence resonance energy transfer in microscopy using genetically engineered GFP derivatives on nickel chelating beads. Biotechnology 3:1–18 · DOI
- Wouters FS, Verveer PJ, Bastiaens PI (2001) Imaging biochemistry inside cells. Trends Cell Biol 11(5):203–211 · DOI · Paper page
- Zal T, Gascoigne NR (2004) Photobleaching-corrected FRET efficiency imaging of live cells. Biophys J 86(6):3923–3939 · DOI
- Kremers G-J, Hazelwood KL, Murphy CS, Davidson MW, Piston DW (2009) Photoconversion in orange and red fluorescent proteins. Nat Methods 6(5):355 · DOI
- Valentin G, Verheggen C, Piolot T, Neel H, Coppey-Moisan M, Bertrand E (2005) Photoconversion of YFP into a CFP-like species during acceptor photobleaching FRET experiments. Nat Methods 2(11):801 · DOI
- Seitz A, Terjung S, Zimmermann T, Pepperkok R (2012) Quantifying the influence of yellow fluorescent protein photoconversion on acceptor photobleaching-based fluorescence resonance energy transfer measurements. J Biomed Opt 17(1):011010 · DOI
- Sinnecker D, Voigt P, Hellwig N, Schaefer M (2005) Reversible photobleaching of enhanced green fluorescent proteins. Biochemistry 44(18):7085–7094 · DOI
- Van Munster E, Kremers G, Adjobo-Hermans M, Gadella TW (2005) Fluorescence resonance energy transfer (FRET) measurement by gradual acceptor photobleaching. J Microsc 218(3):253–262 · DOI
- Gordon GW, Berry G, Liang XH, Levine B, Herman B (1998) Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys J 74(5):2702–2713 · DOI
- Nagy P, Vámosi G, Bodnár A, Lockett SJ, Szöllősi J (1998) Intensity-based energy transfer measurements in digital imaging microscopy. Eur Biophys J 27(4):377–389 · DOI
- van Rheenen J, Langeslag M, Jalink K (2004) Correcting confocal acquisition to optimize imaging of fluorescence resonance energy transfer by sensitized emission. Biophys J 86(4):2517–2529 · DOI
- Elangovan M, Wallrabe H, Chen Y, Day RN, Barroso M, Periasamy A (2003) Characterization of one-and two-photon excitation fluorescence resonance energy transfer microscopy. Methods 29(1):58–73 · DOI
- Vanderklish PW, Krushel LA, Holst BH, Gally JA, Crossin KL, Edelman GM (2000) Marking synaptic activity in dendritic spines with a calpain substrate exhibiting fluorescence resonance energy transfer. Proc Natl Acad Sci 97(5):2253–2258 · DOI · Paper page
- Żal T, Żal MA, Gascoigne NR (2002) Inhibition of T cell receptor-coreceptor interactions by antagonist ligands visualized by live FRET imaging of the T-hybridoma immunological synapse. Immunity 16(4):521–534 · DOI
- Erickson MG, Alseikhan BA, Peterson BZ, Yue DT (2001) Preassociation of calmodulin with voltage-gated Ca2+ channels revealed by FRET in single living cells. Neuron 31(6):973–985 · DOI
- Xia Z, Liu Y (2001) Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys J 81(4):2395–2402 · DOI
- Chen H, Puhl HL 3rd, Koushik SV, Vogel SS, Ikeda SR (2006) Measurement of FRET efficiency and ratio of donor to acceptor concentration in living cells. Biophys J 91(5):L39–L41 · DOI
- Hoppe A, Christensen K, Swanson JA (2002) Fluorescence resonance energy transfer-based stoichiometry in living cells. Biophys J 83(6):3652–3664 · DOI
- Heim R (1999) Green fluorescent protein forms for energy transfer. Methods Enzymol 302:408–423 · DOI
- Dickinson M, Bearman G, Tille S, Lansford R, Fraser S (2001) Multi-spectral imaging and linear unmixing add a whole new dimension to laser scanning fluorescence microscopy. BioTechniques 31(6):1272–1279 · DOI
- Zimmermann T, Rietdorf J, Pepperkok R (2003) Spectral imaging and its applications in live cell microscopy. FEBS Lett 546(1):87–92 · DOI
- Schleifenbaum A, Stier G, Gasch A, Sattler M, Schultz C (2004) Genetically encoded FRET probe for PKC activity based on pleckstrin. J Am Chem Soc 126(38):11786–11787 · DOI
- Zimmermann T, Rietdorf J, Girod A, Georget V, Pepperkok R (2002) Spectral imaging and linear un-mixing enables improved FRET efficiency with a novel GFP2–YFP FRET pair. FEBS Lett 531(2):245–249 · DOI
- Chen Y, Mauldin JP, Day RN, Periasamy A (2007) Characterization of spectral FRET imaging microscopy for monitoring nuclear protein interactions. J Microsc 228(2):139–152 · DOI
- Wlodarczyk J, Woehler A, Kobe F, Ponimaskin E, Zeug A, Neher E (2008) Analysis of FRET signals in the presence of free donors and acceptors. Biophys J 94(3):986–1000 · DOI
- Woehler A, Wlodarczyk J, Neher E (2010) Signal/noise analysis of FRET-based sensors. Biophys J 99(7):2344–2354 · DOI
- Megias D, Marrero R, Martinez Del Peso B, Garcia MA, Bravo-Cordero JJ, Garcia-Grande A, Santos A, Montoya MC (2009) Novel lambda FRET spectral confocal microscopy imaging method. Microsc Res Tech 72(1):1–11. https://doi.org/10.1002/jemt.20633 · DOI
- Domingo B, Sabariegos R, Picazo F, Llopis J (2007) Imaging FRET standards by steady-state fluorescence and lifetime methods. Microsc Res Tech 70(12):1010–1021 · DOI
- Pietraszewska-Bogiel A, Gadella T (2011) FRET microscopy: from principle to routine technology in cell biology. J Microsc 241(2):111–118 · DOI
- Nagai T, Ibata K, Park ES, Kubota M, Mikoshiba K, Miyawaki A (2002) A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat Biotechnol 20(1):87 · DOI
- Griesbeck O, Baird GS, Campbell RE, Zacharias DA, Tsien RY (2001) Reducing the environmental sensitivity of yellow fluorescent protein mechanism and applications. J Biol Chem 276(31):29188–29194 · DOI · Paper page
Cited by
Sorted by citations
Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease
Colom-Cadena, M., Toombs, J., Simzer, E., Holt, K., McGeachan, R., Tulloch, J., Jackson, R. J., Catterson, J. H., Spires-Jones, M. P., Rose, J., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-023-02679-6 · Cited by 44
Metadata
- Authors
- Zimmermann, T.
- Venue
- Methods in Molecular Biology
- Publisher
- Springer New York
- Published
- 2019
- Pages
- 235-274
- ISSN
- 1064-3745
- 1940-6029
- Cited by
- 5
- References
- 0
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review