ライフサイエンスコーパス: Forster resonance energy transfer

1 xibility in RP(o) with single-molecule FRET (Forster resonance energy transfer).

2 t originating from one or many traces (e.g., Forster resonance energy transfer).

3 I of EF-G using ensemble and single-molecule Forster resonance energy transfer.

4 nd probing protein structure and dynamics by Forster resonance energy transfer.

5 in vivo CheA activity with an assay based on Forster resonance energy transfer.

6 sing an environment-sensitive fluorophore or Forster resonance energy transfer.

7 sing fluorescence lifetime imaging to detect Forster resonance energy transfer.

8 er formation and pyrene-perylene interstrand Forster resonance energy transfer.

9 cial behavior on surfaces by single-molecule Forster resonance energy transfer.

10 s detection of intermolecular Tb(III)-to-dye Forster resonance energy transfer.

11 in protein Hsp90 measured by single-molecule Forster resonance energy transfer.

12 imators used particularly in single-molecule Forster resonance energy transfer.

13 cting partner of IRSp53 through pulldown and Forster resonance energy transfer analysis, and we explo

14 P) and NaCl concentrations using single-pair Forster resonance energy transfer and alternating laser

15 live CHO cells was demonstrated by means of Forster resonance energy transfer and dual-color fluores

16 In this study, we utilized both Forster resonance energy transfer and electron microscop

17 Comparison with single-molecule Forster Resonance Energy Transfer and ensemble measureme

18 We demonstrate here that the combination of Forster Resonance Energy Transfer and Fluorescence Corre

19 vels: molecular aggregations and mobility by Forster resonance energy transfer and fluorescence corre

20 of protein domains monitored in real time by Forster resonance energy transfer and fluorescence-inten

21 In this work, a novel combination of Forster resonance energy transfer and Monte Carlo simula

22 on of three different functionalities (RNAi, Forster resonance energy transfer and RNA aptamer) confi

23 imultaneously detected using single-molecule Forster resonance energy transfer and single-molecule fl

24 By combining single-molecule Forster resonance energy transfer and the Bayesian param

25 We have used single-molecule Forster resonance energy transfer and unwinding assays t

26 Bimolecular fluorescence complementation, Forster resonance energy transfer, and coimmunoprecipita

27 s interpretation of atomic force microscopy, Forster resonance energy transfer, and small-angle x-ray

28 In this study, a Forster resonance energy transfer approach was utilized

29 omplementary set of short- and long-distance Forster resonance energy transfer approaches to distingu

30 and Fluorescent Lifetime Imaging to measure Forster Resonance Energy Transfer approaches.

31 energy transfer based on exciton theory and Forster resonance energy transfer are explored.

32 F) peptide substrates originating from FRET (Forster Resonance Energy Transfer) are powerful tool for

33 oscale distance-dependent phenomena, such as Forster resonance energy transfer, are important interac

34 l eukaryotic complexes using single-molecule Forster resonance energy transfer as well as site-specif

35 A.SUR1 complexes, corroborated by an in vivo Forster resonance energy transfer assay showing disrupti

36 and Raman spectroscopy, circular dichroism, Forster resonance energy transfer, atomic force microsco

37 n measured their looping rates using a FRET (Forster resonance energy transfer)-based assay and extra

38 ing a DNA polymerase coupled assay and FRET (Forster resonance energy transfer)-based helicase assays

39 microdomains using a novel membrane-targeted Forster resonance energy transfer-based biosensor transg

40 expression of the highly sensitive cytosolic Forster resonance energy transfer-based cGMP biosensor r

41 xchange factor for Rab13 and develop a novel Forster resonance energy transfer-based Rab biosensor to

42 now report the development of a quantitative Forster resonance energy transfer-based system using mul

43 Ca(2+)/calmodulin biosensor (Forster resonance energy transfer-based) mice were made

44 in plasma membrane-derived vesicles using a Forster-resonance-energy-transfer-based method.

45 id bodies of Chlorella sp. and that there is Forster resonance energy transfer between BaP and photos

46 The technique is also used to force a Forster resonance energy transfer between fluorophores o

47 as a versatile platform for developing FRET (Forster resonance energy transfer) biomimetic assays.

48 Time-lapse imaging using a Forster resonance energy transfer biosensor, immunostain

49 veloped a genetically encoded bioluminescent Forster resonance energy transfer (BRET) assay using the

50 Forster resonance energy transfer by fluorescence lifeti

51 Concentric Forster resonance energy transfer (cFRET) configurations

52 This method is based on Forster resonance energy transfer combined with fluoresc

53 Here, we employed time-resolved Forster resonance energy transfer combined with SNAP- an

54 Single-molecule Forster resonance energy transfer data support the obser

55 ented combination of NMR and single-molecule Forster resonance energy transfer demonstrates for the f

56 FP and BK-CFP, displayed robust co-localized Forster resonance energy transfer, demonstrating intermo

57 mixing with microsecond time resolution and Forster resonance energy transfer detection provides ins

58 d displacement was monitored by the quenched Forster resonance energy transfer effect.

59 on nuclear magnetic resonance resonances and Forster resonance energy transfer efficiencies suggest t

60 kappa(2), one of the key parameters defining Forster resonance energy transfer efficiency, is determi

61 d with an exchange protein activated by cAMP-Forster resonance energy transfer (EPAC-FRET) sensor and

62 A time-resolved Forster resonance energy transfer experiment confirmed t

63 were established by comparing time-resolved Forster resonance energy transfer experiments and MD sim

64 Forster Resonance Energy Transfer experiments further re

65 Forster resonance energy transfer experiments show that

66 e (DPA) is a commonly used acceptor agent in Forster resonance energy transfer experiments that allow

67 Using intramolecular Forster resonance energy transfer experiments to detect

68 We confirmed this experimentally by Forster resonance energy transfer experiments using dual

69 tion of free energy simulations, single-pair Forster resonance energy transfer experiments, and exist

70 Here, using single-molecule Forster resonance energy transfer experiments, we show t

71 e spectroscopy, atomic force microscopy, and Forster resonance energy transfer experiments, we show t

72 odel selection was guided by single-molecule Forster resonance energy transfer experiments, which rev

73 Forster resonance energy transfer (family FRET) efficien

74 orescence lifetime image microscopy based on Forster resonance energy transfer (FLIM-FRET) we identif

75 uorescence lifetime imaging microscopy-based Forster resonance energy transfer (FLIM-FRET) we reveale

76 CPK20 (but not CPK17/CPK34) was confirmed by Forster-resonance energy transfer fluorescence lifetime

77 interacts in plant cells with KAT2 channels (Forster resonance energy transfer-fluorescence lifetime

78 Furthermore, our Forster resonance energy transfer-fluorescence lifetime

79 In this study, we used two-photon excitation-Forster resonance energy transfer-fluorescence lifetime

80 We developed a novel Forster resonance energy transfer-fluorescence lifetime

81 Here, we used Forster resonance energy transfer/fluorescence lifetime

82 f the receptor PqsRLBD for PQS and have used Forster resonance energy transfer fluorimetry and kineti

83 internally labeled iCy3/iCy5 donor-acceptor Forster resonance energy transfer fluorophore pairs that

84 ne binding protein (LUMP), which serves as a Forster resonance energy transfer (FRET) acceptor protei

85 novel strategy that combines single-molecule Forster resonance energy transfer (FRET) and chemical de

86 pm4 heteromers, as shown in experiments with Forster resonance energy transfer (FRET) and co-immunopr

87 Forster resonance energy transfer (FRET) and coimmunopre

88 R and Akt1 coimmunoprecipitated, and in-cell Forster resonance energy transfer (FRET) and glutathione

89 Forster resonance energy transfer (FRET) and molecular b

90 Studies using Forster resonance energy transfer (FRET) and other metho

91 eraction sites in the alpha1C- subunit using Forster resonance energy transfer (FRET) and recording o

92 troscopic method based on the combination of Forster resonance energy transfer (FRET) and total inter

93 ation properties which have been ascribed to Forster resonance energy transfer (FRET) and, to a lesse

94 Here, we use a quantitative Forster resonance energy transfer (FRET) approach to sho

95 resis) through particle size measurement and forster resonance energy transfer (FRET) approach.

96 Using Forster resonance energy transfer (FRET) approaches we f

97 Fluorescence and Forster resonance energy transfer (FRET) are potent and

98 The use of Forster resonance energy transfer (FRET) as a probe of t

99 A growing number of these structures utilize Forster resonance energy transfer (FRET) as part of the

100 Using a novel tC(o)-tCnitro Forster Resonance Energy Transfer (FRET) assay, we were

101 those isoforms using a novel flow cytometry-Forster resonance energy transfer (FRET) assay.

102 as DC-SIGN/R) using a sensitive, ratiometric Forster resonance energy transfer (FRET) assay.

103 In the last few decades, Forster resonance energy transfer (FRET) based spectrosc

104 we propose a simple and continuous real-time Forster resonance energy transfer (FRET) based-assay for

105 Most current GEZIs are based on Forster resonance energy transfer (FRET) between a selec

106 We monitored the buckling transition via Forster Resonance Energy Transfer (FRET) between appende

107 e employed a novel method to reliably detect Forster resonance energy transfer (FRET) between pairs o

108 en been monitored via macroscopic changes in Forster resonance energy transfer (FRET) between probes

109 Using single-molecule Forster resonance energy transfer (FRET) between RPS25 a

110 This is achieved by exploiting a Forster resonance energy transfer (FRET) between the two

111 e present an optically multiplexed six-color Forster resonance energy transfer (FRET) biosensor for s

112 multicellular spheroids expressing a glucose Forster resonance energy transfer (FRET) biosensor is de

113 The performance of Forster Resonance Energy Transfer (FRET) biosensors depe

114 Recently developed Forster resonance energy transfer (FRET) biosensors for

115 y quantitatively imaging near-infrared (NIR) Forster resonance energy transfer (FRET) both in vitro a

116 y probing the level of molecular assembly by Forster resonance energy transfer (FRET) can be used to

117 Genetically encoded biosensors based on Forster resonance energy transfer (FRET) can visualize r

118 nstructs labeled with Cy3/Cy5 donor-acceptor Forster resonance energy transfer (FRET) chromophore pai

119 enge, we report a multifunctional concentric Forster resonance energy transfer (FRET) configuration t

120 nt a fluctuation-based approach to biosensor Forster resonance energy transfer (FRET) detection that

121 aging applications because they can serve as Forster resonance energy transfer (FRET) donors to two o

122 orescein and tetramethylrhodamine (TAMRA), a Forster resonance energy transfer (FRET) dye pair, were

123 Forster resonance energy transfer (FRET) experiments are

124 Single-molecule Forster resonance energy transfer (FRET) experiments are

125 aspects of the NMD process in parallel with Forster resonance energy transfer (FRET) experiments rev

126 Recent Forster resonance energy transfer (FRET) experiments sho

127 In Forster resonance energy transfer (FRET) experiments, ex

128 t with the interpretation of single-molecule Forster resonance energy transfer (FRET) experiments, if

129 s (Fe(3+) or Al(3+) or Cr(3+)) via ultrafast Forster resonance energy transfer (FRET) from naphthalim

130 sing either atomic force microscopy (AFM) or Forster resonance energy transfer (FRET) have shown that

131 Using Forster resonance energy transfer (FRET) imaging of fluo

132 annels under basal conditions as shown using Forster resonance energy transfer (FRET) imaging.

133 Ultrafast Forster resonance energy transfer (FRET) in a polymer-po

134 d species were detected as robust changes in Forster resonance energy transfer (FRET) in a range of c

135 a combination of whole-cell patch-clamp and Forster resonance energy transfer (FRET) in single cells

136 Understanding of Forster resonance energy transfer (FRET) in thin films c

137 ending the standard molecular ruler based on Forster resonance energy transfer (FRET) into a two-dime

138 Forster resonance energy transfer (FRET) is a nonradiati

139 The single-molecule Forster resonance energy transfer (FRET) is a powerful t

140 Forster resonance energy transfer (FRET) is a versatile

141 easurement of donor lifetime modification by Forster resonance energy transfer (FRET) is a widely use

142 Forster resonance energy transfer (FRET) is an exquisite

143 Forster Resonance Energy Transfer (FRET) is the phenomen

144 We analyzed, with in vivo Forster resonance energy transfer (FRET) kinase assays,

145 To solve this conundrum, we used Forster resonance energy transfer (FRET) measured by flu

146 itions were chosen as potentially useful for Forster resonance energy transfer (FRET) measurements on

147 eflection fluorescence-based single-molecule Forster resonance energy transfer (FRET) measurements we

148 Time-resolved Forster resonance energy transfer (FRET) measurements yi

149 rably with dose-response curves from in vivo Forster resonance energy transfer (FRET) measurements, d

150 In this contribution, we use a Forster resonance energy transfer (FRET) method to inves

151 idic-based nanoparticle synthesis method and Forster resonance energy transfer (FRET) microscopy imag

152 Forster resonance energy transfer (FRET) microscopy is a

153 l resolution afforded by genetically encoded Forster resonance energy transfer (FRET) nanosensors.

154 he specific roles that QDs provide as either Forster resonance energy transfer (FRET) or charge/elect

155 tforms where emission is controlled/tuned by Forster Resonance Energy Transfer (FRET) or pH-dependent

156 iching GB binding protein (ProX) between the Forster resonance energy transfer (FRET) pair, the cyan

157 s, QSY9 and QSY35, respectively, to generate Forster resonance energy transfer (FRET) pairs sensitive

158 combined various competitive and sequential Forster resonance energy transfer (FRET) pathways betwee

159 Under nondenaturing conditions, two Forster resonance energy transfer (FRET) populations wer

160 ed to other probe and assay formats, such as Forster resonance energy transfer (FRET) probes and immu

161 NSET) mechanism rather than the conventional Forster resonance energy transfer (FRET) process.

162 ) demonstrating solid-state fluorescence and Forster resonance energy transfer (FRET) processes by fi

163 protein interactions directly in cells using Forster resonance energy transfer (FRET) read out by aut

164 tion and accumulation can techniques such as Forster resonance energy transfer (FRET) realize their p

165 hile drug quantification was enabled using a Forster Resonance Energy Transfer (FRET) relationship be

166 Ensemble Forster resonance energy transfer (FRET) results can be

167 work combines the use of genetically encoded Forster resonance energy transfer (FRET) sensors and a n

168 The absence of a Forster resonance energy transfer (FRET) signal demonstr

169 FtTM measures Forster resonance energy transfer (FRET) signals, genera

170 Forster resonance energy transfer (FRET) studies perform

171 Many genetically encoded biosensors use Forster resonance energy transfer (FRET) to dynamically

172 We use single-molecule Forster resonance energy transfer (FRET) to measure the

173 tryptophan (W) residues, which then relax by Forster Resonance Energy Transfer (FRET) to the chromoph

174 high-throughput single-molecule three-color Forster resonance energy transfer (FRET) tracking method

175 Forster resonance energy transfer (FRET) using fluoresce

176 ctor quantum dots (QDs), in combination with Forster resonance energy transfer (FRET), are also suita

177 gic receptor-Rab protein interactions, using Forster resonance energy transfer (FRET), confocal micro

178 In this work, a combination of Forster resonance energy transfer (FRET), nonreducing SD

179 el approach based on the competition between Forster resonance energy transfer (FRET), protein-induce

180 ere, we use a combination of single-molecule Forster resonance energy transfer (FRET), SAXS, dynamic

181 Using subunit exchange Forster resonance energy transfer (FRET), we determine d

182 ng, small-angle X-ray scattering (SAXS), and Forster resonance energy transfer (FRET), we show that 6

183 a novel assay using amplified, time-resolved Forster resonance energy transfer (FRET), which is highl

184 X-ray scattering (SAXS), and single-molecule Forster resonance energy transfer (FRET), with the goal

185 Therefore, we established new Forster resonance energy transfer (FRET)-based assays to

186 Here, we develop the first Forster resonance energy transfer (FRET)-based biosensor

187 scribe a protocol that simplifies the use of Forster resonance energy transfer (FRET)-based biosensor

188 tion, a ratiometric mitochondrially targeted Forster resonance energy transfer (FRET)-based calcium i

189 ouse ventricular cardiomyocytes expressing a Forster resonance energy transfer (FRET)-based cAMP bios

190 Here, we present a set of Forster resonance energy transfer (FRET)-based crowding-

191 Here, we developed multi-color Forster resonance energy transfer (FRET)-based enzymatic

192 scent conjugates of biomolecules and a novel Forster resonance energy transfer (FRET)-based probe sui

193 d two fluorescence-based Ca(2+) sensors: the Forster resonance energy transfer (FRET)-based reporter

194 fluorescence a parallelized high-throughput Forster resonance energy transfer (FRET)-based reporter

195 m) that they cannot be readily detected with Forster resonance energy transfer (FRET)-labeled lipid p

196 Tunable Forster resonance energy transfer (FRET)-quenched substr

197 ent, as determined by means of intracellular Forster resonance energy transfer (FRET).

198 ng of the donor lifetime as a clear hint for Forster resonance energy transfer (FRET).

199 ion of multiplexed solution conditions using Forster resonance energy transfer (FRET).

200 o red shifts in emission of up to +140 nm by Forster resonance energy transfer (FRET).

201 ermination of the extent of encapsulation by Forster resonance energy transfer (FRET).

202 tion of a biosensor for NE activity based on Forster resonance energy transfer (FRET).

203 with other fluorescence techniques, such as Forster resonance energy transfer (FRET).

204 s of NPs in cells and biomimetic media using Forster resonance energy transfer (FRET).

205 in solution, on beads, and in live cells by Forster resonance energy transfer (FRET).

206 Fluorescence (or Forster) resonance energy transfer (FRET) is commonly us

207 Here, we show that fluorescence (Forster) resonance energy transfer (FRET) measurements c

208 mmunosorbent assay (FLISA), fluorescence (or Forster) resonance energy transfer (FRET), immunochromat

209 A Forster-resonance energy transfer (FRET) probe for N-WAS

210 en sulfide anion) based on the alteration of Forster resonance energy transfer from an emissive semic

211 Forster resonance energy transfer from the quantum dot (

212 contrast mechanisms of linear dichroism and Forster resonance energy transfer further distinguish OR

213 Whereas forster resonance energy transfer has a detection range

214 aging and biosensors, including photochromic Forster resonance energy transfer, high-resolution micro

215 Model predictions, validated with Ca(2+) and Forster resonance energy transfer imaging of adult rat v

216 Forster resonance energy transfer imaging suggests the i

217 Here we use Forster resonance energy transfer, immunoprecipitation,

218 to-heme distance was probed by time-resolved Forster resonance energy transfer in the microsecond tim

219 -1A and SERT was visualized in live cells by Forster resonance energy transfer: it was restricted to

220 e jump with fluorescence microscopy of FRET (Forster resonance energy transfer)-labeled proteins.

221 Forster resonance energy transfer mapping of key residue

222 and fluorescence lifetime imaging microscopy/Forster resonance energy transfer measurements demonstra

223 anic fluorophores to perform single-molecule Forster resonance energy transfer measurements in the cy

224 osensor red cGES-DE5 and performed the first Forster resonance energy transfer measurements of cGMP i

225 tegies with state-of-the-art single-molecule Forster resonance energy transfer measurements on biolog

226 At conditions where the protein is unfolded, Forster resonance energy transfer measurements reveal th

227 Live-cell Forster resonance energy transfer measurements revealed

228 By combining single-molecule Forster resonance energy transfer measurements with norm

229 luation of nanodomain sizes by time-resolved Forster resonance energy transfer measurements.

230 Using Forster resonance energy transfer microscopy in live cel

231 le osmotic stress, and a recently introduced Forster resonance energy transfer microscopy method, ful

232 Here, using total internal reflection/Forster resonance energy transfer microscopy, we observe

233 asured fluorescence intensity matched a homo-Forster Resonance Energy Transfer model.

234 high-throughput flow cytometric quantum dot Forster resonance energy transfer nanosensor system.

235 , our data from differential centrifugation, Forster resonance energy transfer, native electrophoresi

236 ifically label proteins with single-molecule Forster resonance energy transfer probes for high-throug

237 l sensitivities in other studies, such as in Forster resonance energy transfer probes to measure conf

238 e, we combine size-exclusion chromatography, Forster resonance energy transfer, pulldown, and in vitr

239 Single-molecule Forster resonance energy transfer reports on the RNA con

240 ic resonance spectroscopy or single-molecule Forster resonance energy transfer, respectively.

241 al reflection microscopy in combination with Forster resonance energy transfer reveals that there is

242 iously described citrine-Arch electrochromic Forster resonance energy transfer sensor (dubbed CAESR)

243 Using intramolecular SAP97 Forster resonance energy transfer sensors, we demonstrat

244 By using recombinant-targeted Forster resonance energy transfer sensors, we show that

245 The Forster resonance energy transfer signal between CPT and

246 Here, we devised a single molecule Forster Resonance Energy Transfer (SM-FRET) assay to mon

247 g initiation, elongation and single-molecule Forster resonance energy transfer (sm-FRET) assays.

248 computational modeling with single molecule Forster resonance energy transfer (smFRET) and catalytic

249 Using single-molecule Forster resonance energy transfer (smFRET) and multipara

250 Here, we present single-molecule Forster resonance energy transfer (smFRET) confocal spec

251 on and population sizes from single-molecule Forster resonance energy transfer (smFRET) data obtained

252 Single-molecule Forster resonance energy transfer (smFRET) experiments r

253 Single-molecule Forster resonance energy transfer (smFRET) experiments u

254 the combination of ALEX and single-molecule Forster Resonance Energy Transfer (smFRET) has been very

255 In recent years, single-molecule Forster resonance energy transfer (smFRET) has emerged a

256 Here, we used the single-molecule Forster resonance energy transfer (smFRET) method to obs

257 ctuator were investigated by single molecule Forster Resonance Energy Transfer (smFRET) microscopy to

258 Here, we present a single-molecule Forster resonance energy transfer (smFRET) study of the

259 Here we report a single-molecule Forster resonance energy transfer (smFRET) system that d

260 ency by using intramolecular single-molecule Forster Resonance Energy Transfer (smFRET) to characteri

261 Here, we have used single molecule Forster Resonance Energy Transfer (smFRET) to examine th

262 Here, we have used single-molecule Forster resonance energy transfer (smFRET) to probe the

263 Here we used single-molecule Forster resonance energy transfer (smFRET) to test this

264 ule level by combined force spectroscopy and Forster resonance energy transfer (smFRET), using an opt

265 mini, can be estimated using single-molecule Forster resonance energy transfer (smFRET).

266 lycine-bound LBD cleft using single-molecule Forster resonance energy transfer (smFRET).

267 omeric GQ interactions using single-molecule Forster resonance energy transfer (smFRET).

268 linking, electron paramagnetic resonance, or Forster resonance energy transfer spectroscopy studies.

269 se in the population of a compact high-FRET (Forster resonance energy transfer) state (efficiency>90%

270 Forster resonance energy transfer studies after PLCbeta

271 by fluorescence lifetime imaging microscopy/Forster resonance energy transfer studies in transgenic

272 We have used single-molecule Forster resonance energy transfer techniques to investig

273 Using mass spectrometry and Forster resonance energy transfer techniques, we confirm

274 nd cell-generated traction forces and used a Forster resonance energy transfer tension biosensor to a

275 Here, we use Forster resonance energy transfer theory to simulate the

276 Here we use single molecule Forster resonance energy transfer to access the conforma

277 Here we use Forster resonance energy transfer to characterize the en

278 RNA, we used nuclear magnetic resonance and Forster resonance energy transfer to demonstrate the eff

279 (III) complexes are widely used as donors in Forster resonance energy transfer to enable time-gated d

280 Here, we used stopped-flow Forster resonance energy transfer to investigate the con

281 We used a glucose nanosensor based on Forster resonance energy transfer to monitor cytosolic g

282 We have used single-molecule Forster resonance energy transfer to probe the temperatu

283 Here we use single-molecule Forster resonance energy transfer to quantify the effect

284 We used single-molecule Forster Resonance Energy Transfer to visualize directly

285 combination of ensemble and single-molecule Forster resonance energy transfer together with protein-

286 on cell-surface proteins with time-resolved Forster resonance energy transfer (TR-FRET) assays in pl

287 idization beacons that utilize time-resolved Forster resonance energy transfer (TR-FRET) between a lu

288 A Forster resonance energy transfer triple-helical peptide

289 subunits and full-length alpha7 by measuring Forster resonance energy transfer using donor recovery a

290 a new continuous fluorescent assay based on Forster resonance energy transfer, using lipid II analog

291 Forster resonance energy transfer was used to monitor th

292 Using Forster resonance energy transfer, we describe an intram

293 Utilizing Forster Resonance Energy Transfer, we describe nucleotid

294 Based on the observed Forster resonance energy transfer, we determined that up

295 From single-molecule Forster resonance energy transfer, we obtained insight i

296 Using single-molecule Forster resonance energy transfer, we show that Psi56 da

297 Using Forster resonance energy transfer, we show that Rasip1 i

298 Using single-molecule Forster resonance energy transfer, we showed that POT1 s

299 ting fluorescence quenching, enhancement, or Forster resonance energy transfer with transport methods

300 ends of different proteins support efficient Forster resonance energy transfer, with sensitivity to i