Forster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins
Akrap N, Seidel T, Barisas BG (2010)
ANALYTICAL BIOCHEMISTRY 402(1): 105-106.
Zeitschriftenaufsatz
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Autor*in
Akrap, Nina;
Seidel, ThorstenUniBi;
Barisas, B. George
Einrichtung
Abstract / Bemerkung
We present, for the red fluorescent protein mCherry acting as both fluorescence resonant energy transfer (FRET) donor and acceptor, Forster critical distance (r(0)) values with five important visible fluorescent protein (VFP) variants as well as with itself. The pair EYFP-mCherry exhibits an r(0) of 5.66 nm, equaling or exceeding any combination of VFPs reported previously. Moreover, mCherry should be an excellent chromophore for homo-FRET with an r(0) of 5.10 nm for energy transfer between two mCherry moieties. Finally, mCherry exhibits higher r(0) values than does DsRed. These characteristics, combined with mCherry's rapid folding and excellent spectral properties, suggest that mCherry constitutes a valuable long-wavelength hetero-FRET acceptor and probe for homo-FRET experiments. (C) 2010 Elsevier Inc. All rights reserved.
Erscheinungsjahr
2010
Zeitschriftentitel
ANALYTICAL BIOCHEMISTRY
Band
402
Ausgabe
1
Seite(n)
105-106
ISSN
0003-2697
Page URI
https://pub.uni-bielefeld.de/record/1795761
Zitieren
Akrap N, Seidel T, Barisas BG. Forster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins. ANALYTICAL BIOCHEMISTRY. 2010;402(1):105-106.
Akrap, N., Seidel, T., & Barisas, B. G. (2010). Forster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins. ANALYTICAL BIOCHEMISTRY, 402(1), 105-106. https://doi.org/10.1016/j.ab.2010.03.026
Akrap, Nina, Seidel, Thorsten, and Barisas, B. George. 2010. “Forster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins”. ANALYTICAL BIOCHEMISTRY 402 (1): 105-106.
Akrap, N., Seidel, T., and Barisas, B. G. (2010). Forster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins. ANALYTICAL BIOCHEMISTRY 402, 105-106.
Akrap, N., Seidel, T., & Barisas, B.G., 2010. Forster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins. ANALYTICAL BIOCHEMISTRY, 402(1), p 105-106.
N. Akrap, T. Seidel, and B.G. Barisas, “Forster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins”, ANALYTICAL BIOCHEMISTRY, vol. 402, 2010, pp. 105-106.
Akrap, N., Seidel, T., Barisas, B.G.: Forster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins. ANALYTICAL BIOCHEMISTRY. 402, 105-106 (2010).
Akrap, Nina, Seidel, Thorsten, and Barisas, B. George. “Forster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins”. ANALYTICAL BIOCHEMISTRY 402.1 (2010): 105-106.
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25 Zitationen in Europe PMC
Daten bereitgestellt von Europe PubMed Central.
A VPS33A-binding motif on syntaxin 17 controls autophagy completion in mammalian cells.
Saleeb RS, Kavanagh DM, Dun AR, Dalgarno PA, Duncan RR., J Biol Chem 294(11), 2019
PMID: 30655294
Saleeb RS, Kavanagh DM, Dun AR, Dalgarno PA, Duncan RR., J Biol Chem 294(11), 2019
PMID: 30655294
Inward Rectifier Potassium Channels (Kir2.x) and Caveolin-3 Domain-Specific Interaction: Implications for Purkinje Cell-Dependent Ventricular Arrhythmias.
Vaidyanathan R, Van Ert H, Haq KT, Morotti S, Esch S, McCune EC, Grandi E, Eckhardt LL., Circ Arrhythm Electrophysiol 11(1), 2018
PMID: 29326130
Vaidyanathan R, Van Ert H, Haq KT, Morotti S, Esch S, McCune EC, Grandi E, Eckhardt LL., Circ Arrhythm Electrophysiol 11(1), 2018
PMID: 29326130
Genetic variants of dopamine D2 receptor impact heterodimerization with dopamine D1 receptor.
Błasiak E, Łukasiewicz S, Szafran-Pilch K, Dziedzicka-Wasylewska M., Pharmacol Rep 69(2), 2017
PMID: 28119185
Błasiak E, Łukasiewicz S, Szafran-Pilch K, Dziedzicka-Wasylewska M., Pharmacol Rep 69(2), 2017
PMID: 28119185
Investigating State Restriction in Fluorescent Protein FRET Using Time-Resolved Fluorescence and Anisotropy.
Blacker TS, Chen W, Avezov E, Marsh RJ, Duchen MR, Kaminski CF, Bain AJ., J Phys Chem C Nanomater Interfaces 121(3), 2017
PMID: 28217242
Blacker TS, Chen W, Avezov E, Marsh RJ, Duchen MR, Kaminski CF, Bain AJ., J Phys Chem C Nanomater Interfaces 121(3), 2017
PMID: 28217242
ShadowY: a dark yellow fluorescent protein for FLIM-based FRET measurement.
Murakoshi H, Shibata ACE., Sci Rep 7(1), 2017
PMID: 28754922
Murakoshi H, Shibata ACE., Sci Rep 7(1), 2017
PMID: 28754922
An improved labeling strategy enables automated detection of single-virus fusion and assessment of HIV-1 protease activity in single virions.
Sood C, Francis AC, Desai TM, Melikyan GB., J Biol Chem 292(49), 2017
PMID: 29046351
Sood C, Francis AC, Desai TM, Melikyan GB., J Biol Chem 292(49), 2017
PMID: 29046351
GPI-anchored proteins are confined in subdiffraction clusters at the apical surface of polarized epithelial cells.
Paladino S, Lebreton S, Lelek M, Riccio P, De Nicola S, Zimmer C, Zurzolo C., Biochem J 474(24), 2017
PMID: 29046391
Paladino S, Lebreton S, Lelek M, Riccio P, De Nicola S, Zimmer C, Zurzolo C., Biochem J 474(24), 2017
PMID: 29046391
Manipulation of Subunit Stoichiometry in Heteromeric Membrane Proteins.
Morales-Perez CL, Noviello CM, Hibbs RE., Structure 24(5), 2016
PMID: 27041595
Morales-Perez CL, Noviello CM, Hibbs RE., Structure 24(5), 2016
PMID: 27041595
Techniques for the Analysis of Protein-Protein Interactions in Vivo.
Xing S, Wallmeroth N, Berendzen KW, Grefen C., Plant Physiol 171(2), 2016
PMID: 27208310
Xing S, Wallmeroth N, Berendzen KW, Grefen C., Plant Physiol 171(2), 2016
PMID: 27208310
The CD4 and CD3δε Cytosolic Juxtamembrane Regions Are Proximal within a Compact TCR-CD3-pMHC-CD4 Macrocomplex.
Glassman CR, Parrish HL, Deshpande NR, Kuhns MS., J Immunol 196(11), 2016
PMID: 27183595
Glassman CR, Parrish HL, Deshpande NR, Kuhns MS., J Immunol 196(11), 2016
PMID: 27183595
Structural assemblies of the di- and oligomeric G-protein coupled receptor TGR5 in live cells: an MFIS-FRET and integrative modelling study.
Greife A, Felekyan S, Ma Q, Gertzen CG, Spomer L, Dimura M, Peulen TO, Wöhler C, Häussinger D, Gohlke H, Keitel V, Seidel CA., Sci Rep 6(), 2016
PMID: 27833095
Greife A, Felekyan S, Ma Q, Gertzen CG, Spomer L, Dimura M, Peulen TO, Wöhler C, Häussinger D, Gohlke H, Keitel V, Seidel CA., Sci Rep 6(), 2016
PMID: 27833095
Single-molecule analyses of fully functional fluorescent protein-tagged follitropin receptor reveal homodimerization and specific heterodimerization with lutropin receptor.
Mazurkiewicz JE, Herrick-Davis K, Barroso M, Ulloa-Aguirre A, Lindau-Shepard B, Thomas RM, Dias JA., Biol Reprod 92(4), 2015
PMID: 25761594
Mazurkiewicz JE, Herrick-Davis K, Barroso M, Ulloa-Aguirre A, Lindau-Shepard B, Thomas RM, Dias JA., Biol Reprod 92(4), 2015
PMID: 25761594
The action of HIF-3α variants on HIF-2α-HIF-1β heterodimer formation is directly probed in live cells.
Kim SH, Hwang D, Park H, Yang EG, Chung HS, Kim SY., Exp Cell Res 336(2), 2015
PMID: 26160453
Kim SH, Hwang D, Park H, Yang EG, Chung HS, Kim SY., Exp Cell Res 336(2), 2015
PMID: 26160453
Fluorescent Protein Based FRET Pairs with Improved Dynamic Range for Fluorescence Lifetime Measurements.
George Abraham B, Sarkisyan KS, Mishin AS, Santala V, Tkachenko NV, Karp M., PLoS One 10(8), 2015
PMID: 26237400
George Abraham B, Sarkisyan KS, Mishin AS, Santala V, Tkachenko NV, Karp M., PLoS One 10(8), 2015
PMID: 26237400
Fluorescent proteins as genetically encoded FRET biosensors in life sciences.
Hochreiter B, Garcia AP, Schmid JA., Sensors (Basel) 15(10), 2015
PMID: 26501285
Hochreiter B, Garcia AP, Schmid JA., Sensors (Basel) 15(10), 2015
PMID: 26501285
Fluorescence lifetime imaging microscopy in the medical sciences.
Ebrecht R, Don Paul C, Wouters FS., Protoplasma 251(2), 2014
PMID: 24390249
Ebrecht R, Don Paul C, Wouters FS., Protoplasma 251(2), 2014
PMID: 24390249
Quantitative real-time kinetics of optogenetic proteins CRY2 and CIB1/N using single-molecule tools.
Cui Y, Choudhury SR, Irudayaraj J., Anal Biochem 458(), 2014
PMID: 24780222
Cui Y, Choudhury SR, Irudayaraj J., Anal Biochem 458(), 2014
PMID: 24780222
Engineering genetically encoded FRET sensors.
Lindenburg L, Merkx M., Sensors (Basel) 14(7), 2014
PMID: 24991940
Lindenburg L, Merkx M., Sensors (Basel) 14(7), 2014
PMID: 24991940
Imaging live cells at the nanometer-scale with single-molecule microscopy: obstacles and achievements in experiment optimization for microbiology.
Haas BL, Matson JS, DiRita VJ, Biteen JS., Molecules 19(8), 2014
PMID: 25123183
Haas BL, Matson JS, DiRita VJ, Biteen JS., Molecules 19(8), 2014
PMID: 25123183
Kaede for detection of protein oligomerization.
Wolf H, Barisas BG, Dietz KJ, Seidel T., Mol Plant 6(5), 2013
PMID: 23430050
Wolf H, Barisas BG, Dietz KJ, Seidel T., Mol Plant 6(5), 2013
PMID: 23430050
Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells.
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PMID: 24194740
Müller SM, Galliardt H, Schneider J, Barisas BG, Seidel T., Front Plant Sci 4(), 2013
PMID: 24194740
Interaction of proteins associated with the magnetosome assembly in magnetotactic bacteria as revealed by two-hybrid two-photon excitation fluorescence lifetime imaging microscopy Förster resonance energy transfer.
Carillo MA, Bennet M, Faivre D., J Phys Chem B 117(47), 2013
PMID: 24175984
Carillo MA, Bennet M, Faivre D., J Phys Chem B 117(47), 2013
PMID: 24175984
Förster resonance energy transfer (FRET) correlates of altered subunit stoichiometry in cys-loop receptors, exemplified by nicotinic α4β2.
Srinivasan R, Richards CI, Dilworth C, Moss FJ, Dougherty DA, Lester HA., Int J Mol Sci 13(8), 2012
PMID: 22949846
Srinivasan R, Richards CI, Dilworth C, Moss FJ, Dougherty DA, Lester HA., Int J Mol Sci 13(8), 2012
PMID: 22949846
Enhancement of probe signal for screening of HIV-1 protease inhibitors in living cells.
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PMID: 23223077
Yao H, Jin S., Sensors (Basel) 12(12), 2012
PMID: 23223077
7 References
Daten bereitgestellt von Europe PubMed Central.
Zwischenmolekulare energiewanderung und fluoreszenz
Förster T., 1948
Förster T., 1948
Forster distances between green fluorescent protein pairs.
Patterson GH, Piston DW, Barisas BG., Anal. Biochem. 284(2), 2000
PMID: 10964438
Patterson GH, Piston DW, Barisas BG., Anal. Biochem. 284(2), 2000
PMID: 10964438
Practical Use of Corrected Fluorescence Excitation and Emission Spectra of Fluorescent Proteins in Förster Resonance Energy Transfer (FRET) Studies
Hink MA, Visser NV, Borst JW, Hoek A.v., Visser AJWG., 2003
Hink MA, Visser NV, Borst JW, Hoek A.v., Visser AJWG., 2003
Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolution.
Bader AN, Hofman EG, Voortman J, en Henegouwen PM, Gerritsen HC., Biophys. J. 97(9), 2009
PMID: 19883605
Bader AN, Hofman EG, Voortman J, en Henegouwen PM, Gerritsen HC., Biophys. J. 97(9), 2009
PMID: 19883605
Fluorescent proteins for single-molecule fluorescence applications.
Seefeldt B, Kasper R, Seidel T, Tinnefeld P, Dietz KJ, Heilemann M, Sauer M., J Biophotonics 1(1), 2008
PMID: 19343637
Seefeldt B, Kasper R, Seidel T, Tinnefeld P, Dietz KJ, Heilemann M, Sauer M., J Biophotonics 1(1), 2008
PMID: 19343637
Quantitative FRET analysis with the EGFP-mCherry fluorescent protein pair.
Albertazzi L, Arosio D, Marchetti L, Ricci F, Beltram F., Photochem. Photobiol. 85(1), 2008
PMID: 18764891
Albertazzi L, Arosio D, Marchetti L, Ricci F, Beltram F., Photochem. Photobiol. 85(1), 2008
PMID: 18764891
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