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Artykuły w czasopismach na temat „BRET”

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Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 30 lipca 2024

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1

Kocan, Martina, Heng B. See, Ruth M. Seeber, Karin A. Eidne i Kevin D. G. Pfleger. "Demonstration of Improvements to the Bioluminescence Resonance Energy Transfer (BRET) Technology for the Monitoring of G Protein–Coupled Receptors in Live Cells". Journal of Biomolecular Screening 13, nr 9 (23.09.2008): 888–98. http://dx.doi.org/10.1177/1087057108324032.

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The bioluminescence resonance energy transfer (BRET) technique has become extremely popular for studying protein-protein interactions in living cells and real time. Of particular interest is the ability to monitor interactions between G protein–coupled receptors, such as the thyrotropin-releasing hormone receptor (TRHR), and proteins critical for regulating their function, such as β-arrestin. Using TRHR/β-arrestin interactions, we have demonstrated improvements to all 3 generations of BRET (BRET1, BRET2, and eBRET) by using the novel forms of luciferase, Rluc2 and Rluc8, developed by the Gambhir laboratory. Furthermore, for the 1st time it was possible to use the BRET2 system to detect ligand-induced G protein–coupled receptor/β-arrestin interactions over prolonged periods (on the scale of hours rather than seconds) with a very stable signal. As demonstrated by our Z′-factor data, these luciferases increase the sensitivity of BRET to such an extent that they substantially increase the potential applicability of this technology for effective drug discovery high-throughput screening. ( Journal of Biomolecular Screening 2008:888-898)

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2

Bae Kim, Sung, Rika Fujii, Arutselvan Natarajan, Tarik F. Massoud i Ramasamy Paulmurugan. "Ligand-activated BRET9 imaging for measuring protein–protein interactions in living mice". Chemical Communications 56, nr 2 (2020): 281–84. http://dx.doi.org/10.1039/c9cc07634d.

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We engineered a conceptually unique ligand-activatable BRET system (termed BRET9). This system simultaneously enhanced both the total bioluminescence spectrum and the BRET signal in the far-red region as a robust optical platform for animal imaging.

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3

RAMSAY, Douglas, Elaine KELLETT, Mary McVEY, Stephen REES i Graeme MILLIGAN. "Homo- and hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences". Biochemical Journal 365, nr 2 (15.07.2002): 429–40. http://dx.doi.org/10.1042/bj20020251.

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Homo- and hetero-oligomerization of G-protein-coupled receptors (GPCRs) were examined in HEK-293 cells using two variants of bioluminescence resonance energy transfer (BRET). BRET2 (a variant of BRET) offers greatly improved separation of the emission spectra of the donor and acceptor moieties compared with traditional BRET. Previously recorded homo-oligomerization of the human δ-opioid receptor was confirmed using BRET2. Homo-oligomerization of the κ-opioid receptor was observed using both BRET techniques. Both homo- and hetero-oligomers, containing both δ- and κ-opioid receptors, were unaffected by the presence of receptor ligands. BRET detection of opioid receptor homo- and hetero-oligomers required expression of 50000–100000 copies of the receptor energy acceptor construct per cell. The effectiveness of δ—κ-opioid receptor hetero-oligomer formation was as great as for homomeric interactions. The capacity of the two opioid receptors to form oligomeric complexes with the β2-adrenoceptor was also assessed. Although such interactions were detected, at least 250000 copies per cell of the energy acceptor were required. Requirement for high levels of receptor expression was equally pronounced in attempts to measure hetero-oligomer formation between the κ-opioid receptor and the thyrotropin-releasing hormone receptor-1. These studies indicate that constitutively formed homo- and hetero-oligomers of opioid receptor subtypes can be detected in living cells containing less than 100000 copies of the receptors. However, although hetero-oligomeric interactions between certain less closely related GPCRs can be detected, they appear to be of lower affinity than homo- or hetero-oligomers containing closely related sequences. Interactions recorded between certain GPCR family members in heterologous expression systems are likely to be artefacts of extreme levels of overexpression.

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4

Parkes. "Reply to Bret Davis". Journal of Nietzsche Studies 46, nr 1 (2015): 82. http://dx.doi.org/10.5325/jnietstud.46.1.0082.

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5

Scharnhorst, Gary. "Byron and Bret Harte". Byron Journal 32, nr 1 (styczeń 2004): 45–50. http://dx.doi.org/10.3828/bj.32.1.6.

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6

Scharnhorst, Gary. "Browning and Bret Harte". ANQ: A Quarterly Journal of Short Articles, Notes and Reviews 12, nr 3 (styczeń 1999): 41–43. http://dx.doi.org/10.1080/08957699909598065.

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7

Feugang, J. M., R. C. Youngblood, A. Fahad, J. M. Greene, S. T. Willard i P. L. Ryan. "73 APPLICATION OF QUANTUM DOT CONJUGATES FOR INVESTIGATING MAMMALIAN SPERMATOZOA". Reproduction, Fertility and Development 24, nr 1 (2012): 149. http://dx.doi.org/10.1071/rdv24n1ab73.

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Self-illuminating quantum dots are nanoparticles that are less than 100 nm in diameter. Their coating with the light-emitting protein Renilla luciferase forms complexes that have promising applications in in vivo imaging. These complexes can be further combined to specific tags such as antibodies or peptides for various in vitro studies. Especially in reproduction, these conjugates may contribute to a better comprehension of molecular events associated with fertilization and beyond. To this end, we evaluated the ability of mammalian spermatozoa to harmlessly incorporate nanoparticles. Motile spermatozoa of freshly collected boar and stallion semen were purified, washed in PBS/polyvinylpyrrolidone (PVP) (1 mg mL–1) and adjusted at desired concentrations according to experiments. Spermatozoa were fixed at 107 in Experiment 1 and incubated for 30 min at 37°C with 0, 1, or 5 nM quantum dots conjugated with the bioluminescence resonance energy transfer and R9 cell internalization peptide (BRET-Qdot-R9). In Experiment 2, different amounts of spermatozoa (25 × 106, 50 × 106 and 100 × 106) were incubated as in Experiment 1 with 0 or 1 nM BRET-Qdot-R9. After incubation, aliquots of BRET-Qdot-R9-loaded spermatozoa in both experiments were set aside for motility analysis using the computer-assisted sperm analyzer (only boar data shown). Remaining spermatozoa were centrifuged to eliminate the excess of BRET-Qdot-R9 and washed twice with PBS/PVP at 22°C. Resulting pellets were re-suspended with 50 μL of PBS/PVP and aliquots were mounted on slides for confocal fluorescence microscopic evaluation. Remaining cells and supernatants were mixed with 2 μg of coelenterazine and immediately imaged for bioluminescence using the IVIS-100 Imaging System. Experiments were repeated 3 times and analysed (Student's t-test; P < 0.05 for threshold of significance). Higher light emissions were detected in tubes containing both spermatozoa and BRET-Qdot-R9 as compared to the control (0 nM BRET-Qdot-R9) and last wash-derived supernatants. Low background signals of coelenterazine were observed in tubes (± sperm) without BRET-Qdot-R9. Experiment 1 revealed a dose-dependent response of BRET-Qdot-R9, whereas experiment 2 indicated a potential decrease of light emission with the higher sperm quantity. Interestingly, the presence of BRET-Qdot-R9 did not compromise sperm motility; however, the sperm/BRET-Qdot-R9 ratio appears essential to maintain comparable proportions of motile and rapid spermatozoa to the control group (86 ± 6 and 74 ± 5% for control vs 63 ± 17 and 46 ± 15%, 81 ± 8 and 68 ± 11% and 93 ± 1 and 85 ± 1% for 25 × 106, 50 × 106 and 100 × 106 sperm/1 nM ratios, respectively; P ≥ 0.05; mean ± standard error of the means). The BRET-Qdot-R9 fluorescence signal was mostly detected in the sperm head and intermediate piece with 1 nM BRET-Qdot-R9, whereas the entire spermatozoa fluoresced with 5 nM BRET-Qdot-R9. This study indicates that the incorporation of BRET-Qdot-R9 by boar and stallion spermatozoa does not impair their motility. Further investigations are needed to evaluate the proportion of cells incorporating BRET-Qdot-R9. Supported by the USDA-ARS Biophotonics Initiative #58-6402-3-0120.

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8

Cooray, Sadani N., Teng-Teng Chung, Khansa Mazhar, Laszlo Szidonya i Adrian J. L. Clark. "Bioluminescence Resonance Energy Transfer Reveals the Adrenocorticotropin (ACTH)-Induced Conformational Change of the Activated ACTH Receptor Complex in Living Cells". Endocrinology 152, nr 2 (1.02.2011): 495–502. http://dx.doi.org/10.1210/en.2010-1053.

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Abstract The melanocortin 2 receptor (MC2R) accessory protein (MRAP) is a small single-transmembrane domain protein that plays a pivotal role in the function of the MC2R. The pituitary hormone, ACTH, acts via this receptor complex to stimulate adrenal steroidogenesis. Using both coimmunoprecipitation and bioluminescence resonance energy transfer (BRET), we show that the MC2R is constitutively homodimerized in cells. Furthermore, consistent with previous data, we also show that MRAP exists as an antiparallel homodimer. ACTH enhanced the BRET signal between MC2R homodimers as well as MC2R-MRAP heterodimers. However, ACTH did not enhance the physical interaction between these dimers as determined by coimmunoprecipitation. Real-time BRET analysis of the MRAP-MC2R interaction revealed two distinct phases of the ACTH-dependent BRET increase, an initial complex series of changes occurring over the first 2 min and a later persistent increase in BRET signal. The slower ACTH-dependent phase was inhibited by the protein kinase A inhibitor KT5720, suggesting that signal transduction was a prerequisite for this later conformational change. The MRAP-MC2R BRET approach provides a unique tool with which to analyze the activation of this receptor.

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9

Wang, Lufei, Dong Joon Lee, Han Han, Lixing Zhao, Hiroshi Tsukamoto, Yong-IL Kim, Adele M. Musicant i in. "Application of bioluminescence resonance energy transfer-based cell tracking approach in bone tissue engineering". Journal of Tissue Engineering 12 (styczeń 2021): 204173142199546. http://dx.doi.org/10.1177/2041731421995465.

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Bioluminescent imaging (BLI) has emerged as a popular in vivo tracking modality in bone regeneration studies stemming from its clear advantages: non-invasive, real-time, and inexpensive. We recently adopted bioluminescence resonance energy transfer (BRET) principle to improve BLI cell tracking and generated the brightest bioluminescent signal known to date, which thus enables more sensitive real-time cell tracking at deep tissue level. In the present study, we brought BRET-based cell tracking strategy into the field of bone tissue engineering for the first time. We labeled rat mesenchymal stem cells (rMSCs) with our in-house BRET-based GpNLuc reporter and evaluated the cell tracking efficacy both in vitro and in vivo. In scaffold-free spheroid 3D culture system, using BRET-based GpNLuc labeling resulted in significantly better correlation to cell numbers than a fluorescence based approach. In scaffold-based 3D culture system, GpNLuc-rMSCs displayed robust bioluminescence signals with minimal background noise. Furthermore, a tight correlation between BLI signal and cell number highlighted the robust reliability of using BRET-based BLI. In calvarial critical sized defect model, robust signal and the consistency in cell survival evaluation collectively supported BRET-based GpNLuc labeling as a reliable approach for non-invasively tracking MSC. In summary, BRET-based GpNLuc labeling is a robust, reliable, and inexpensive real-time cell tracking method, which offers a promising direction for the technological innovation of BLI and even non-invasive tracking systems, in the field of bone tissue engineering.

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10

Hwang, Eugene, Jisu Song i Jin Zhang. "Integration of Nanomaterials and Bioluminescence Resonance Energy Transfer Techniques for Sensing Biomolecules". Biosensors 9, nr 1 (16.03.2019): 42. http://dx.doi.org/10.3390/bios9010042.

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Bioluminescence resonance energy transfer (BRET) techniques offer a high degree of sensitivity, reliability and ease of use for their application to sensing biomolecules. BRET is a distance dependent, non-radiative energy transfer, which uses a bioluminescent protein to excite an acceptor through the resonance energy transfer. A BRET sensor can quickly detect the change of a target biomolecule quantitatively without an external electromagnetic field, e.g., UV light, which normally can damage tissue. Having been developed quite recently, this technique has evolved rapidly. Here, different bioluminescent proteins have been reviewed. In addition to a multitude of bioluminescent proteins, this manuscript focuses on the recent development of BRET sensors by utilizing quantum dots. The special size-dependent properties of quantum dots have made the BRET sensing technique attractive for the real-time monitoring of the changes of target molecules and bioimaging in vivo. This review offers a look into the basis of the technique, donor/acceptor pairs, experimental applications and prospects.

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11

Kim, Hye Mi, Hyeyeong Seo, Yooheon Park, Hee-Seok Lee, Seok-Hee Lee i Kwang Suk Ko. "Development of a Human Estrogen Receptor Dimerization Assay for the Estrogenic Endocrine-Disrupting Chemicals Using Bioluminescence Resonance Energy Transfer". International Journal of Environmental Research and Public Health 18, nr 16 (23.08.2021): 8875. http://dx.doi.org/10.3390/ijerph18168875.

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Endocrine-disrupting chemicals (EDCs) are found in food and various other substances, including pesticides and plastics. EDCs are easily absorbed into the body and have the ability to mimic or block hormone function. The radioligand binding assay based on the estrogen receptors binding affinity is widely used to detect estrogenic EDCs but is limited to radioactive substances and requires specific conditions. As an alternative, we developed a human cell-based dimerization assay for detecting EDC-mediated ER-alpha (ERα) dimerization using bioluminescence resonance energy transfer (BRET). The resultant novel BRET-based on the ERα dimerization assay was used to identify the binding affinity of 17β-estradiol (E2), 17α-estradiol, corticosterone, diethylhexyl phthalate, bisphenol A, and 4-nonylphenol with ERα by measuring the corresponding BRET signals. Consequently, the BRET signals from five chemicals except corticosterone showed a dose-dependent sigmoidal curve for ERα, and these chemicals were suggested as positive chemicals for ERα. In contrast, corticosterone, which induced a BRET signal comparable to that of the vehicle control, was suggested as a negative chemical for ERα. Therefore, these results were consistent with the results of the existing binding assay for ERα and suggested that a novel BRET system can provide information about EDCs-mediated dimerization to ERα.

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12

Parkes. "Open Letter to Bret Davis". Journal of Nietzsche Studies 46, nr 1 (2015): 42. http://dx.doi.org/10.5325/jnietstud.46.1.0042.

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13

Campbell, Donna M. "BRET HARTE: PRINCE AND PAUPER". Resources for American Literary Study 29, nr 1 (1.01.2004): 371–73. http://dx.doi.org/10.2307/26367167.

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14

Monnier, François. "Cardin Le Bret (1558-1655)". Revue Française d'Histoire des Idées Politiques N° 47, nr 1 (2018): 303. http://dx.doi.org/10.3917/rfhip1.047.0303.

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15

Campbell, Donna M. "BRET HARTE: PRINCE AND PAUPER". Resources for American Literary Study 29, nr 1 (1.01.2004): 371–73. http://dx.doi.org/10.2307/resoamerlitestud.29.2004.0371.

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16

Berkove, Lawrence I. "SELECTED LETTERS OF BRET HARTE". Resources for American Literary Study 25, nr 1 (1.01.1999): 120–21. http://dx.doi.org/10.5325/resoamerlitestud.25.1.0120.

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17

Tara Penry. "Bret Harte's Oscar Wilde Tale". American Literary Realism 51, nr 1 (2018): 21. http://dx.doi.org/10.5406/amerlitereal.51.1.0021.

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18

Goodpaster, Bret H. "Rebuttal from Bret H. Goodpaster". Journal of Physiology 598, nr 18 (8.07.2020): 3811. http://dx.doi.org/10.1113/jp279714.

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19

Hahn, Henry. "Bret Harte by Gary Scharnhorst." Western American Literature 28, nr 3 (1993): 266–67. http://dx.doi.org/10.1353/wal.1993.0167.

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Pétigny, Cécile, Audrey-Ann Dumont, Hugo Giguère, Audrey Collette, Brian J. Holleran, Mircea Iftinca, Christophe Altier, Élie Besserer-Offroy, Mannix Auger-Messier i Richard Leduc. "Monitoring TRPC7 Conformational Changes by BRET Following GPCR Activation". International Journal of Molecular Sciences 23, nr 5 (24.02.2022): 2502. http://dx.doi.org/10.3390/ijms23052502.

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Transient receptor potential canonical (TRPC) channels are membrane proteins involved in regulating Ca2+ homeostasis, and whose functions are modulated by G protein-coupled receptors (GPCR). In this study, we developed bioluminescent resonance energy transfer (BRET) biosensors to better study channel conformational changes following receptor activation. For this study, two intramolecular biosensors, GFP10-TRPC7-RLucII and RLucII-TRPC7-GFP10, were constructed and were assessed following the activation of various GPCRs. We first transiently expressed receptors and the biosensors in HEK293 cells, and BRET levels were measured following agonist stimulation of GPCRs. The activation of GPCRs that engage Gαq led to a Gαq-dependent BRET response of the functional TRPC7 biosensor. Focusing on the Angiotensin II type-1 receptor (AT1R), GFP10-TRPC7-RLucII was tested in rat neonatal cardiac fibroblasts, expressing endogenous AT1R and TRPC7. We detected similar BRET responses in these cells, thus validating the use of the biosensor in physiological conditions. Taken together, our results suggest that activation of Gαq-coupled receptors induce conformational changes in a novel and functional TRPC7 BRET biosensor.

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21

Min, Se-Hong, Alexander R. French, Keelan J. Trull, Kiet Tat, S. Ashley Varney i Mathew Tantama. "Ratiometric BRET Measurements of ATP with a Genetically-Encoded Luminescent Sensor". Sensors 19, nr 16 (10.08.2019): 3502. http://dx.doi.org/10.3390/s19163502.

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Luciferase-based reporters provide a key measurement approach in a broad range of applications, from in vitro high-throughput screening to whole animal imaging. For example, luminescence intensity is widely used to measure promoter activity, protein expression levels, and cell growth. However, luminescence intensity measurements are subject to quantitative irregularities caused by luminescence decay and variation in reporter expression level. In contrast, bioluminescence resonance energy transfer (BRET) sensors provide the advantages of luciferase-based reporters but overcome the aforementioned irregularities because of the inherently ratiometric readout. Here, we generated a new ratiometric BRET sensor of ATP (ARSeNL—ATP detection with a Ratiometric mScarlet-NanoLuc sensor), and we demonstrated that it provides a stable and robust readout across protein, cell, and whole animal tissue contexts. The ARSeNL sensor was engineered by screening a color palette of sensors utilizing variants of the high photon flux NanoLuc luciferase as donors and a panel of red fluorescent proteins as acceptors. We found that the novel combination of NanoLuc and mScarlet exhibited the largest dynamic range, with a 5-fold change in the BRET ratio upon saturation with ATP. Importantly, the NanoLuc-mScarlet BRET pair provided a large spectral separation between luminescence emission channels that is compatible with green and red filter sets extensively used in typical biological microscopes and animal imaging systems. Using this new sensor, we showed that the BRET ratio was independent of luminescence intensity decay and sensor expression level, and the BRET ratio faithfully reported differences in live-cell energy metabolism whether in culture or within mouse tissue. In particular, BRET analyte sensors have not been used broadly in tissue contexts, and thus, in principle, our sensor could provide a new tool for in vivo imaging of metabolic status.

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22

Kim, Sung-Bae, Ryo Nishihara i Ramasamy Paulmurugan. "Near-Infrared Imaging of Steroid Hormone Activities Using Bright BRET Templates". International Journal of Molecular Sciences 24, nr 1 (30.12.2022): 677. http://dx.doi.org/10.3390/ijms24010677.

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Bioluminescence (BL) is an excellent optical readout for bioassays and molecular imaging. Herein, we accomplished new near infrared bioluminescence resonance energy transfer (NIR-BRET) templates for monitoring molecular events in cells with higher sensitivity. We first identified the best resonance energy donor for the NIR-BRET templates through the characterization of many coelenterazine (CTZ)–marine luciferase combinations. As a result, we found that NLuc–DBlueC and ALuc47–nCTZ combinations showed luminescence in the blue emission wavelength with excellent BL intensity and stability, for example, the NLuc–DBlueC and ALuc47–nCTZ combinations were 17-fold and 22-fold brighter than their second highest combinations, respectively, and were stably bright in living mammalian cells for at least 10 min. To harness the excellent BL properties to the NIR-BRET systems, NLuc and ALuc47 were genetically fused to fluorescent proteins (FPs), allowing large “blue-to-red” shifts, such as LSSmChe, LSSmKate2, and LSSmNep (where LSS means Large Stokes Shift). The excellent LSSmNep–NLuc combination showed approximately 170 nm large resonance energy shift from blue to red. The established templates were further utilized in the development of new NIR-BRET systems for imaging steroid hormone activities by sandwiching the ligand-binding domain of a nuclear receptor (NR-LBD) between the luciferase and the FP of the template. The NIR-BRET systems showed a specific luminescence signal upon exposure to steroid hormones, such as androgen, estrogen, and cortisol. The present NIR-BRET templates are important additions for utilizing their advantageous imaging of various molecular events with high efficiency and brightness in physiological samples.

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23

Wu, Yuexin, i Tianyu Jiang. "Developments in FRET- and BRET-Based Biosensors". Micromachines 13, nr 10 (20.10.2022): 1789. http://dx.doi.org/10.3390/mi13101789.

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Resonance energy transfer technologies have achieved great success in the field of analysis. Particularly, fluorescence resonance energy transfer (FRET) and bioluminescence resonance energy transfer (BRET) provide strategies to design tools for sensing molecules and monitoring biological processes, which promote the development of biosensors. Here, we provide an overview of recent progress on FRET- and BRET-based biosensors and their roles in biomedicine, environmental applications, and synthetic biology. This review highlights FRET- and BRET-based biosensors and gives examples of their applications with their design strategies. The limitations of their applications and the future directions of their development are also discussed.

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24

El Khamlichi, Chayma, Flora Reverchon-Assadi, Nadège Hervouet-Coste, Lauren Blot, Eric Reiter i Séverine Morisset-Lopez. "Bioluminescence Resonance Energy Transfer as a Method to Study Protein-Protein Interactions: Application to G Protein Coupled Receptor Biology". Molecules 24, nr 3 (1.02.2019): 537. http://dx.doi.org/10.3390/molecules24030537.

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The bioluminescence resonance energy transfer (BRET) approach involves resonance energy transfer between a light-emitting enzyme and fluorescent acceptors. The major advantage of this technique over biochemical methods is that protein-protein interactions (PPI) can be monitored without disrupting the natural environment, frequently altered by detergents and membrane preparations. Thus, it is considered as one of the most versatile technique for studying molecular interactions in living cells at “physiological” expression levels. BRET analysis has been applied to study many transmembrane receptor classes including G-protein coupled receptors (GPCR). It is well established that these receptors may function as dimeric/oligomeric forms and interact with multiple effectors to transduce the signal. Therefore, they are considered as attractive targets to identify PPI modulators. In this review, we present an overview of the different BRET systems developed up to now and their relevance to identify inhibitors/modulators of protein–protein interaction. Then, we introduce the different classes of agents that have been recently developed to target PPI, and provide some examples illustrating the use of BRET-based assays to identify and characterize innovative PPI modulators in the field of GPCRs biology. Finally, we discuss the main advantages and the limits of BRET approach to characterize PPI modulators.

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Wu, Yuting, Whitney Lewis, Jing Luen Wai, Mengyi Xiong, Jiao Zheng, Zhenglin Yang, Chloe Gordon i in. "Ratiometric Detection of Zn2+ Using DNAzyme-Based Bioluminescence Resonance Energy Transfer Sensors". Chemistry 5, nr 3 (8.08.2023): 1745–59. http://dx.doi.org/10.3390/chemistry5030119.

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While fluorescent sensors have been developed for monitoring metal ions in health and diseases, they are limited by the requirement of an excitation light source that can lead to photobleaching and a high autofluorescence background. To address these issues, bioluminescence resonance energy transfer (BRET)-based protein or small molecule sensors have been developed; however, most of them are not highly selective nor generalizable to different metal ions. Taking advantage of the high selectivity and generalizability of DNAzymes, we report herein DNAzyme-based ratiometric sensors for Zn2+ based on BRET. The 8-17 DNAzyme was labeled with luciferase and Cy3. The proximity between luciferase and Cy3 permitted BRET when coelenterazine, the substrate for luciferase, was introduced. Adding samples containing Zn2+ resulted in a cleavage of the substrate strand, causing dehybridization of the DNAzyme construct, thus increasing the distance between Cy3 and luciferase and changing the BRET signals. Using these sensors, we detected Zn2+ in serum samples and achieved Zn2+ detection with a smartphone camera. Moreover, since the BRET pair is not the component that determines the selectivity of the sensors, this sensing platform has the potential to be adapted for the detection of other metal ions with other metal-dependent DNAzymes.

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26

Fortier, Frances. "L’esthétique hyperréaliste de Bret Easton Ellis". Tangence, nr 44 (1994): 94. http://dx.doi.org/10.7202/025816ar.

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SAITO, Kenta, i Takeharu NAGAI. "Development of BRET based Ca2+ Indicator". Seibutsu Butsuri 52, nr 1 (2012): 030–31. http://dx.doi.org/10.2142/biophys.52.030.

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28

Giesey, Ralph E., Lanny Haldy i James Millhorn. "Cardin Le Bret and Lese Majesty". Law and History Review 4, nr 1 (1986): 23–54. http://dx.doi.org/10.2307/743713.

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Cardin Le Bret, councillor of state during the ministry of Richelieu, is sufficiently distinguished to have merited two monographs in modern historiography. The basis of his renown is not his official deeds, however, but his political writings. Moreover, within the large corpus of those writings (630 folio pages, published three times), one treatise alone raises him from obscurity: De la Souveraineté du Roy, first published in 1632. And finally (to allot Le Bret the least that is due him), the fame of that treatise owes less to the perspicuity of its author than to the timeliness of its subject. It is one of the first comprehensive treatments of sovereignty to appear after Jean Bodin ‘invented’ that concept in his Six livres de la République (1576). Le Bret's treatise could thus provide important evidence of the status of ‘sovereignty’ in legal and political discourse two generations after Bodin.

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29

John Conley. "The Poverty of Bret Easton Ellis". Arizona Quarterly: A Journal of American Literature, Culture, and Theory 65, nr 3 (2009): 117–37. http://dx.doi.org/10.1353/arq.0.0043.

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30

Borghei, Golnaz, i Elizabeth A. H. Hall. "BRET-linked ATP assay with luciferase". Analyst 139, nr 17 (2014): 4185–92. http://dx.doi.org/10.1039/c4an00436a.

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RHODES, JOHN. "BRET TILSON: HIS LIFE AND WORK". International Journal of Algebra and Computation 20, nr 02 (marzec 2010): vii—xvii. http://dx.doi.org/10.1142/s0218196710005601.

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Molinari, Paola, Ida Casella i Tommaso Costa. "Functional complementation of high-efficiency resonance energy transfer: a new tool for the study of protein binding interactions in living cells". Biochemical Journal 409, nr 1 (11.12.2007): 251–61. http://dx.doi.org/10.1042/bj20070803.

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Green bioluminescence in Renilla species is generated by a ∼100% efficient RET (resonance energy transfer) process that is caused by the direct association of a blue-emitting luciferase [Rluc (Renilla luciferase)] and an RGFP (Renilla green fluorescent protein). Despite the high efficiency, such a system has never been evaluated as a potential reporter of protein–protein interactions. To address the question, we compared and analysed in mammalian cells the bioluminescence of Rluc and RGFP co-expressed as free native proteins, or as fused single-chain polypeptides and tethered partners of self-assembling coiled coils. Here, we show that: (i) no spontaneous interactions generating detectable BRET (bioluminescence RET) signals occur between the free native proteins; (ii) high-efficiency BRET similar to that observed in Renilla occurs in both fusion proteins and self-interacting chimaeras, but only if the N-terminal of RGFP is free; (iii) the high-efficiency BRET interaction is associated with a dramatic increase in light output when the luminescent reaction is triggered by low-quantum yield coelenterazine analogues. Here, we propose a new functional complementation assay based on the detection of the high-efficiency BRET signal that is generated when the reporters Rluc and RGFP are brought into close proximity by a pair of interacting proteins to which they are linked. To demonstrate its performance, we implemented the assay to measure the interaction between GPCRs (G-protein-coupled receptors) and β-arrestins. We show that complementation-induced BRET allows detection of the GPCR–β-arrestin interaction in a simple luminometric assay with high signal-to-noise ratio, good dynamic range and rapid response.

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33

Shramova, E. I., A. Yu Frolova, V. P. Filimonova, S. M. Deyev i G. M. Proshkina. "System for Self-excited Targeted Photodynamic Therapy Based on the Multimodal Protein DARP-NanoLuc-SOPP3". Acta Naturae 15, nr 4 (17.01.2024): 100–110. http://dx.doi.org/10.32607/actanaturae.27331.

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Despite the significant potential of photodynamic therapy (PDT) as a minimally invasive treatment modality, the use of this method in oncology has remained limited due to two serious problems: 1) limited penetration of the excitation light in tissues, which makes it impossible to affect deep-seated tumors and 2) use of chemical photosensitizers that slowly degrade in the body and cause photodermatoses and hyperthermia in patients. To solve these problems, we propose a fully biocompatible targeted system for PDT that does not require an external light source. The proposed system is based on bioluminescent resonance energy transfer (BRET) from the oxidized form of the luciferase substrate to the photosensitizing protein SOPP3. The BRET-activated system is composed of the multimodal protein DARP-NanoLuc-SOPP3, which contains a BRET pair NanoLuc-SOPP3 and a targeting module DARPin. The latter provides the interaction of the multimodal protein with tumors overexpressing tumor-associated antigen HER2 (human epidermal growth factor receptor type II). In vitro experiments in a 2D monolayer cell culture and a 3D spheroid model have confirmed HER2-specific photo-induced cytotoxicity of the system without the use of an external light source; in addition, experiments in animals with subcutaneous HER2-positive tumors have shown selective accumulation of DARP-NanoLuc-SOPP3 on the tumor site. The fully biocompatible system for targeted BRET-induced therapy proposed in this work makes it possible to overcome the following limitations: 1) the need to use an external light source and 2) the side phototoxic effect from aberrant accumulation of chemical photosensitizers. The obtained results demonstrate that the fully protein-based self-excited BRET system has a high potential for targeted PDT.

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34

Mie, Masayasu, Rena Hirashima, Yasumasa Mashimo i Eiry Kobatake. "Construction of an Enzymatically-Conjugated DNA Aptamer–Protein Hybrid Molecule for Use as a BRET-Based Biosensor". Applied Sciences 10, nr 21 (29.10.2020): 7646. http://dx.doi.org/10.3390/app10217646.

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DNA-protein conjugates are useful molecules for construction of biosensors. Herein, we report the development of an enzymatically-conjugated DNA aptamer–protein hybrid molecule for use as a bioluminescence resonance energy transfer (BRET)-based biosensor. DNA aptamers were enzymatically conjugated to a fusion protein via the catalytic domain of porcine circovirus type 2 replication initiation protein (PCV2 Rep) comprising residues 14–109 (tpRep), which was truncated from the full catalytic domain of PCV2 Rep comprising residues 1–116 by removing the flexible regions at the N- and C-terminals. For development of a BRET-based biosensor, we constructed a fusion protein in which tpRep was positioned between NanoLuc luciferase and a fluorescent protein and conjugated to single-stranded DNA aptamers that specifically bind to either thrombin or lysozyme. We demonstrated that the BRET ratios depended on the concentration of the target molecules.

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Nieman, Marvin T. "Mapping the Protease Activated Receptor 4 (PAR4) Homodimer Interface." Blood 114, nr 22 (20.11.2009): 773. http://dx.doi.org/10.1182/blood.v114.22.773.773.

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Abstract Abstract 773 Thrombin activates platelets by binding and cleaving protease activated receptors 1 and 4 (PAR1 and PAR4). PAR1 and PAR4 communicate with each other to lower the concentration of thrombin required for PAR4 activation (Nieman Biochemistry, 2008). In addition, PAR1 and PAR4 form homo and heterodimers. However, where these receptors interact has not been defined and it is not known if dimerization influences receptor activation, downstream signaling, or both. Since PAR4 activation is important on human and mouse platelets, we sought to characterize the interaction site between PAR4 homodimers. Using bioluminescence resonance energy transfer (BRET), we mapped the PAR4 homodimer interface. The PAR4 homodimers show a specific interaction as indicated by a hyperbolic BRET signal in response to increasing PAR4-GFP expression with a fixed concentration of PAR4-Rluc. The threshold maximum BRET signal was disrupted in a concentration-dependent manner by unlabeled PAR4. In contrast, the unrelated G-protein coupled receptor, rhodopsin, was unable to disrupt the BRET signal indicating that the disruption of the PAR4 homodimer is a specific interaction. We have mapped the region required for PAR4 homodimer formation using chimeras between rhodopsin and PAR4. PAR4 does not interact with rhodopsin in BRET assays. Using a library of rho-PAR4 chimeras that have the junction at the beginning of transmembrane (TM) 2, 3, 4, 5, 6 or 7, we determined where dimer formation is restored. When the junction is placed at the beginning of TM4 or TM5, the chimera does not interact with PAR4-WT. In contrast, when the junction is moved to the end of TM2, the BRET signal is restored. These results indicate that the region on PAR4 required for homodimer formation encompasses a 63 amino acid region that includes the first extracellular loop, TM3 and the second intracellular loop. These studies establish techniques that may be used to define the interactions between other GPCRs found on the platelet surface. These receptor-receptor interactions may be another level of regulation of agonist activity and platelet function in vivo and may provide novel targets for anti-platelet therapies. Disclosures: No relevant conflicts of interest to declare.

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Corbel, Caroline, Sara Sartini, Elisabetta Levati, Pierre Colas, Laurent Maillet, Cyril Couturier, Barbara Montanini i Stéphane Bach. "Screening for Protein-Protein Interaction Inhibitors Using a Bioluminescence Resonance Energy Transfer (BRET)–Based Assay in Yeast". SLAS DISCOVERY: Advancing the Science of Drug Discovery 22, nr 6 (31.01.2017): 751–59. http://dx.doi.org/10.1177/2472555216689530.

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The bioluminescence resonance energy transfer (BRET) technology is a widely used live cell-based method for monitoring protein-protein interactions as well as conformational changes within proteins or molecular complexes. Considering the emergence of protein-protein interactions as a new promising class of therapeutic targets, we have adapted the BRET method in budding yeast. In this technical note, we describe the advantages of using this simple eukaryotic model rather than mammalian cells to perform high-throughput screening of chemical compound collections: genetic tractability, tolerance to solvent, rapidity, and no need of expensive robotic systems. Here, the HDM2/p53 interaction, related to cancer, is used to highlight the interest of this technology in yeast. Sharing the protocol of this BRET-based assay with the scientific community will extend its application to other protein-protein interactions, even though it is toxic for mammalian cells, in order to discover promising therapeutic candidates.

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37

Lin, Hang. "Bret Hinsch (2016). Women in Imperial China." British Journal of Chinese Studies 8, nr 2 (15.03.2019): 160–62. http://dx.doi.org/10.51661/bjocs.v8i2.14.

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The vast scope of Chinese women’s history throughout its two millennia-long imperial period invites sustained scholarly attention to their status, position, image, and a wide range of gender-related issues. Whereas recent years have witnessed an increasing interest in examining historical Chinese women in different dynasties, Bret Hinsch’s new book offers a succinct, yet eloquent survey of womanhood in the shifting contexts of Chinese history, from remote antiquity to the end of the Qing dynasty (1644-1911).

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Flora, Joseph M., Gary Scharnhorst i Stephen J. May. "Bret Harte: Opening the American Literary West". Western Historical Quarterly 32, nr 3 (2001): 385. http://dx.doi.org/10.2307/3650762.

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SCHARNHORST, GARY F. "Prospects for the Study of Bret Harte". Resources for American Literary Study 31, nr 1 (1.01.2006): 1–10. http://dx.doi.org/10.2307/26367025.

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40

Molnár, Bálint. "Intermedialitás Bret Easton Ellis Glamoráma című regényében." Eruditio-Educatio 16., nr 2 (2021): 067–80. http://dx.doi.org/10.36007/eruedu.2021.2.67-80.

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SCHARNHORST, GARY F. "Prospects for the Study of Bret Harte". Resources for American Literary Study 31, nr 1 (1.01.2006): 1–10. http://dx.doi.org/10.2307/resoamerlitestud.31.2006.0001.

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Rosenbaum, Jonathan. "Orson Welles: A Bio-Bibliography Bret Wood". Film Quarterly 44, nr 2 (grudzień 1990): 56–57. http://dx.doi.org/10.2307/1212661.

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Lullo, Sheri A. "Women in Ancient China by Bret Hinsch". Asian Perspectives 58, nr 2 (2019): 413–17. http://dx.doi.org/10.1353/asi.2019.0025.

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Albertini, Virgil. "Bret Harte’s California ed. by Gary Scharnhorst". Western American Literature 26, nr 3 (1991): 251–52. http://dx.doi.org/10.1353/wal.1991.0138.

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Bredahl, A. Carl. "At Odds With Progress by Bret Wallach". Western American Literature 27, nr 2 (1992): 151–52. http://dx.doi.org/10.1353/wal.1992.0081.

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Rosenbaum, Jonathan. ": Orson Welles: A Bio-Bibliography . Bret Wood." Film Quarterly 44, nr 2 (grudzień 1990): 56–57. http://dx.doi.org/10.1525/fq.1990.44.2.04a00090.

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Tardi, Mark. "Review of "White" by Bret Easton Ellis". Text Matters, nr 9 (30.12.2019): 403–7. http://dx.doi.org/10.18778/2083-2931.09.25.

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Holloway, D. "Bret Harte: Opening the American Literary West". American Literature 73, nr 4 (1.12.2001): 870–71. http://dx.doi.org/10.1215/00029831-73-4-870.

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Weihs, Felix, Jian Wang, Kevin D. G. Pfleger i Helen Dacres. "Experimental determination of the bioluminescence resonance energy transfer (BRET) Förster distances of NanoBRET and red-shifted BRET pairs". Analytica Chimica Acta: X 6 (listopad 2020): 100059. http://dx.doi.org/10.1016/j.acax.2020.100059.

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Olsen, Birgit. "Et amerikansk mareridt". K&K - Kultur og Klasse 20, nr 73 (17.03.1993): 117–34. http://dx.doi.org/10.7146/kok.v20i73.20567.

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