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Items: 1 to 20 of 325

1.

Structural changes of yellow Cameleon domains observed by quantitative FRET analysis and polarized fluorescence correlation spectroscopy.

Borst JW, Laptenok SP, Westphal AH, Kühnemuth R, Hornen H, Visser NV, Kalinin S, Aker J, van Hoek A, Seidel CA, Visser AJ.

Biophys J. 2008 Dec;95(11):5399-411. doi: 10.1529/biophysj.107.114587.

2.

Disentangling picosecond events that complicate the quantitative use of the calcium sensor YC3.60.

Laptenok SP, van Stokkum IH, Borst JW, van Oort B, Visser AJ, van Amerongen H.

J Phys Chem B. 2012 Mar 8;116(9):3013-20. doi: 10.1021/jp211830e.

PMID:
22320307
3.
4.

Perrin and Förster unified: Dual-laser triple-polarization FRET (3polFRET) for interactions at the Förster-distance and beyond.

Ungvári T, Gogolák P, Bagdány M, Damjanovich L, Bene L.

Biochim Biophys Acta. 2016 Apr;1863(4):703-16. doi: 10.1016/j.bbamcr.2016.02.002.

PMID:
26854711
5.

Analysis of photobleaching in single-molecule multicolor excitation and Förster resonance energy transfer measurements.

Eggeling C, Widengren J, Brand L, Schaffer J, Felekyan S, Seidel CA.

J Phys Chem A. 2006 Mar 9;110(9):2979-95.

PMID:
16509620
6.

Time-resolved FRET fluorescence spectroscopy of visible fluorescent protein pairs.

Visser AJ, Laptenok SP, Visser NV, van Hoek A, Birch DJ, Brochon JC, Borst JW.

Eur Biophys J. 2010 Jan;39(2):241-53. doi: 10.1007/s00249-009-0528-8. Erratum in: Eur Biophys J. 2010 Mar;39(4):721.

PMID:
19693494
7.

Fluorescence resonance energy transfer (FRET) measurement by gradual acceptor photobleaching.

Van Munster EB, Kremers GJ, Adjobo-Hermans MJ, Gadella TW Jr.

J Microsc. 2005 Jun;218(Pt 3):253-62.

8.

Rise-time of FRET-acceptor fluorescence tracks protein folding.

Lindhoud S, Westphal AH, van Mierlo CP, Visser AJ, Borst JW.

Int J Mol Sci. 2014 Dec 19;15(12):23836-50. doi: 10.3390/ijms151223836.

9.
10.

Flow cytometric measurement of fluorescence (Förster) resonance energy transfer from cyan fluorescent protein to yellow fluorescent protein using single-laser excitation at 458 nm.

He L, Bradrick TD, Karpova TS, Wu X, Fox MH, Fischer R, McNally JG, Knutson JR, Grammer AC, Lipsky PE.

Cytometry A. 2003 May;53(1):39-54.

11.

A quantitative protocol for intensity-based live cell FRET imaging.

Kaminski CF, Rees EJ, Schierle GS.

Methods Mol Biol. 2014;1076:445-54. doi: 10.1007/978-1-62703-649-8_19.

PMID:
24108638
12.

Global analysis of Förster resonance energy transfer in live cells measured by fluorescence lifetime imaging microscopy exploiting the rise time of acceptor fluorescence.

Laptenok SP, Borst JW, Mullen KM, van Stokkum IH, Visser AJ, van Amerongen H.

Phys Chem Chem Phys. 2010 Jul 21;12(27):7593-602. doi: 10.1039/b919700a.

PMID:
20490396
14.

Using structure-function constraints in FRET studies of large macromolecular complexes.

Bujalowski WM, Jezewska MJ.

Methods Mol Biol. 2012;875:135-64. doi: 10.1007/978-1-61779-806-1_7.

PMID:
22573439
15.

Fluorescence resonance energy transfer-based stoichiometry in living cells.

Hoppe A, Christensen K, Swanson JA.

Biophys J. 2002 Dec;83(6):3652-64.

16.

Fluorescence resonance energy transfer of GFP and YFP by spectral imaging and quantitative acceptor photobleaching.

Dinant C, van Royen ME, Vermeulen W, Houtsmuller AB.

J Microsc. 2008 Jul;231(Pt 1):97-104. doi: 10.1111/j.1365-2818.2008.02020.x.

17.

Depolarized FRET (depolFRET) on the cell surface: FRET control by photoselection.

Bene L, Gogolák P, Ungvári T, Bagdány M, Nagy I, Damjanovich L.

Biochim Biophys Acta. 2016 Feb;1863(2):322-34. doi: 10.1016/j.bbamcr.2015.12.003.

PMID:
26657258
18.

High throughput FRET analysis of protein-protein interactions by slide-based imaging laser scanning cytometry.

Szalóki N, Doan-Xuan QM, Szöllősi J, Tóth K, Vámosi G, Bacsó Z.

Cytometry A. 2013 Sep;83(9):818-29. doi: 10.1002/cyto.a.22315.

19.

Photobleaching-based quantitative analysis of fluorescence resonance energy transfer inside single living cell.

Wang L, Chen T, Qu J, Wei X.

J Fluoresc. 2010 Jan;20(1):27-35. doi: 10.1007/s10895-009-0518-3.

PMID:
19588234
20.

Fluorescence resonance energy transfer reports properties of syntaxin1a interaction with Munc18-1 in vivo.

Liu J, Ernst SA, Gladycheva SE, Lee YY, Lentz SI, Ho CS, Li Q, Stuenkel EL.

J Biol Chem. 2004 Dec 31;279(53):55924-36.

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