Статті в журналах з теми "Single Molecule Fluorescence Resonance Energy Transfer (smFRET)"
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Yang, Ziyu, Haiqi Xu, Jiayu Wang, Wei Chen, and Meiping Zhao. "Single-Molecule Fluorescence Techniques for Membrane Protein Dynamics Analysis." Applied Spectroscopy 75, no. 5 (April 20, 2021): 491–505. http://dx.doi.org/10.1177/00037028211009973.
Повний текст джерелаSengupta, Bhaswati, and Mai Huynh. "Contribution of smFRET to Chromatin Research." Biophysica 3, no. 1 (February 8, 2023): 93–108. http://dx.doi.org/10.3390/biophysica3010007.
Повний текст джерелаLeBlanc, Sharonda, Prakash Kulkarni, and Keith Weninger. "Single Molecule FRET: A Powerful Tool to Study Intrinsically Disordered Proteins." Biomolecules 8, no. 4 (November 8, 2018): 140. http://dx.doi.org/10.3390/biom8040140.
Повний текст джерелаLi, Maodong, Tanlin Sun, Fan Jin, Daqi Yu, and Zhirong Liu. "Dimension conversion and scaling of disordered protein chains." Molecular BioSystems 12, no. 9 (2016): 2932–40. http://dx.doi.org/10.1039/c6mb00415f.
Повний текст джерелаYukhnovets, Olessya, Henning Höfig, Nuno Bustorff, Alexandros Katranidis, and Jörg Fitter. "Impact of Molecule Concentration, Diffusion Rates and Surface Passivation on Single-Molecule Fluorescence Studies in Solution." Biomolecules 12, no. 3 (March 18, 2022): 468. http://dx.doi.org/10.3390/biom12030468.
Повний текст джерелаHu, Jinyong, Meiyan Wu, Li Jiang, Zhensheng Zhong, Zhangkai Zhou, Thitima Rujiralai, and Jie Ma. "Combining gold nanoparticle antennas with single-molecule fluorescence resonance energy transfer (smFRET) to study DNA hairpin dynamics." Nanoscale 10, no. 14 (2018): 6611–19. http://dx.doi.org/10.1039/c7nr08397a.
Повний текст джерелаGirodat, Dylan, Avik K. Pati, Daniel S. Terry, Scott C. Blanchard, and Karissa Y. Sanbonmatsu. "Quantitative comparison between sub-millisecond time resolution single-molecule FRET measurements and 10-second molecular simulations of a biosensor protein." PLOS Computational Biology 16, no. 11 (November 5, 2020): e1008293. http://dx.doi.org/10.1371/journal.pcbi.1008293.
Повний текст джерелаYang, Jie, Sarah Perrett, and Si Wu. "Single Molecule Characterization of Amyloid Oligomers." Molecules 26, no. 4 (February 11, 2021): 948. http://dx.doi.org/10.3390/molecules26040948.
Повний текст джерелаVerma, Awadhesh Kumar, Ashab Noumani, Amit K. Yadav, and Pratima R. Solanki. "FRET Based Biosensor: Principle Applications Recent Advances and Challenges." Diagnostics 13, no. 8 (April 8, 2023): 1375. http://dx.doi.org/10.3390/diagnostics13081375.
Повний текст джерелаDurham, Ryan J., Nabina Paudyal, Elisa Carrillo, Nidhi Kaur Bhatia, David M. Maclean, Vladimir Berka, Drew M. Dolino, Alemayehu A. Gorfe, and Vasanthi Jayaraman. "Conformational spread and dynamics in allostery of NMDA receptors." Proceedings of the National Academy of Sciences 117, no. 7 (February 3, 2020): 3839–47. http://dx.doi.org/10.1073/pnas.1910950117.
Повний текст джерелаBarth, Anders, Oleg Opanasyuk, Thomas-Otavio Peulen, Suren Felekyan, Stanislav Kalinin, Hugo Sanabria, and Claus A. M. Seidel. "Unraveling multi-state molecular dynamics in single-molecule FRET experiments. I. Theory of FRET-lines." Journal of Chemical Physics 156, no. 14 (April 14, 2022): 141501. http://dx.doi.org/10.1063/5.0089134.
Повний текст джерелаKlostermeier, Dagmar. "Single-molecule FRET reveals nucleotide-driven conformational changes in molecular machines and their link to RNA unwinding and DNA supercoiling." Biochemical Society Transactions 39, no. 2 (March 22, 2011): 611–16. http://dx.doi.org/10.1042/bst0390611.
Повний текст джерелаSong, Chun-Xiao, Jiajie Diao, Axel T. Brunger, and Stephen R. Quake. "Simultaneous single-molecule epigenetic imaging of DNA methylation and hydroxymethylation." Proceedings of the National Academy of Sciences 113, no. 16 (March 28, 2016): 4338–43. http://dx.doi.org/10.1073/pnas.1600223113.
Повний текст джерелаGreenfeld, Max, Sergey V. Solomatin, and Daniel Herschlag. "Removal of Covalent Heterogeneity Reveals Simple Folding Behavior for P4-P6 RNA." Journal of Biological Chemistry 286, no. 22 (April 8, 2011): 19872–79. http://dx.doi.org/10.1074/jbc.m111.235465.
Повний текст джерелаKaur, Anisa, Roaa Mahmoud, Anoja Megalathan, Sydney Pettit, and Soma Dhakal. "Multiplexed smFRET Nucleic Acid Sensing Using DNA Nanotweezers." Biosensors 13, no. 1 (January 10, 2023): 119. http://dx.doi.org/10.3390/bios13010119.
Повний текст джерелаZhang, Yiming, Zongzhou Ji, Xin Wang, Yi Cao, and Hai Pan. "Single–Molecule Study of DNAzyme Reveals Its Intrinsic Conformational Dynamics." International Journal of Molecular Sciences 24, no. 2 (January 7, 2023): 1212. http://dx.doi.org/10.3390/ijms24021212.
Повний текст джерелаSapkota, Kaur, Megalathan, Donkoh-Moore, and Dhakal. "Single-Step FRET-Based Detection of Femtomoles DNA." Sensors 19, no. 16 (August 9, 2019): 3495. http://dx.doi.org/10.3390/s19163495.
Повний текст джерелаDu, Jinxi, Ricky Dartawan, William Rice, Forrest Gao, Joseph H. Zhou, and Jia Sheng. "Fluorescent Platforms for RNA Chemical Biology Research." Genes 13, no. 8 (July 27, 2022): 1348. http://dx.doi.org/10.3390/genes13081348.
Повний текст джерелаLeVine, Michael V., Daniel S. Terry, George Khelashvili, Zarek S. Siegel, Matthias Quick, Jonathan A. Javitch, Scott C. Blanchard, and Harel Weinstein. "The allosteric mechanism of substrate-specific transport in SLC6 is mediated by a volumetric sensor." Proceedings of the National Academy of Sciences 116, no. 32 (July 19, 2019): 15947–56. http://dx.doi.org/10.1073/pnas.1903020116.
Повний текст джерелаEdwards, Devin T., Marc-Andre LeBlanc, and Thomas T. Perkins. "Modulation of a protein-folding landscape revealed by AFM-based force spectroscopy notwithstanding instrumental limitations." Proceedings of the National Academy of Sciences 118, no. 12 (March 15, 2021): e2015728118. http://dx.doi.org/10.1073/pnas.2015728118.
Повний текст джерелаWu, Si, Liu Hong, Yuqing Wang, Jieqiong Yu, Jie Yang, Jie Yang, Hong Zhang, and Sarah Perrett. "Kinetics of the conformational cycle of Hsp70 reveals the importance of the dynamic and heterogeneous nature of Hsp70 for its function." Proceedings of the National Academy of Sciences 117, no. 14 (March 20, 2020): 7814–23. http://dx.doi.org/10.1073/pnas.1914376117.
Повний текст джерелаSapkota, Kumar, and Soma Dhakal. "FRET-Based Aptasensor for the Selective and Sensitive Detection of Lysozyme." Sensors 20, no. 3 (February 9, 2020): 914. http://dx.doi.org/10.3390/s20030914.
Повний текст джерелаGonzalez, Cuauhtemoc U., Elisa Carrillo, Vladimir Berka, and Vasanthi Jayaraman. "Structural Arrangement Produced by Concanavalin A Binding to Homomeric GluK2 Receptors." Membranes 11, no. 8 (August 11, 2021): 613. http://dx.doi.org/10.3390/membranes11080613.
Повний текст джерелаBasak, Sujit, Nabanita Saikia, David Kwun, Ucheor B. Choi, Feng Ding, and Mark E. Bowen. "Different Forms of Disorder in NMDA-Sensitive Glutamate Receptor Cytoplasmic Domains Are Associated with Differences in Condensate Formation." Biomolecules 13, no. 1 (December 20, 2022): 4. http://dx.doi.org/10.3390/biom13010004.
Повний текст джерелаFuertes, Gustavo, Niccolò Banterle, Kiersten M. Ruff, Aritra Chowdhury, Davide Mercadante, Christine Koehler, Michael Kachala, et al. "Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements." Proceedings of the National Academy of Sciences 114, no. 31 (July 17, 2017): E6342—E6351. http://dx.doi.org/10.1073/pnas.1704692114.
Повний текст джерелаPei, Kai, Jie Zhang, Tingting Zou, and Zhu Liu. "AimR Adopts Preexisting Dimer Conformations for Specific Target Recognition in Lysis-Lysogeny Decisions of Bacillus Phage phi3T." Biomolecules 11, no. 9 (September 7, 2021): 1321. http://dx.doi.org/10.3390/biom11091321.
Повний текст джерелаPlaner, William, Zhiwei Chen, Mathivanan Chinnaraj, Xiaobing Zuo, Vittorio Pengo, Paolo Macor, Francesco Tedesco, and Nicola Pozzi. "X-Ray Crystallographic and Single-Molecule Fluorescence Studies of Beta-2 Glycoprotein I Reveal an Alternative Mechanism of Autoantibody Recognition." Blood 134, Supplement_1 (November 13, 2019): 91. http://dx.doi.org/10.1182/blood-2019-122064.
Повний текст джерелаQiao, Yi, Yuhan Luo, Naiyun Long, Yi Xing, and Jing Tu. "Single-Molecular Förster Resonance Energy Transfer Measurement on Structures and Interactions of Biomolecules." Micromachines 12, no. 5 (April 27, 2021): 492. http://dx.doi.org/10.3390/mi12050492.
Повний текст джерелаHuynh, Mai, and Bhaswati Sengupta. "Analysis of Enzyme Conformation Dynamics Using Single-Molecule Förster Resonance Energy Transfer (smFRET)." Biophysica 2, no. 2 (June 6, 2022): 123–34. http://dx.doi.org/10.3390/biophysica2020014.
Повний текст джерелаHuynh, Mai, and Bhaswati Sengupta. "Analysis of Enzyme Conformation Dynamics Using Single-Molecule Förster Resonance Energy Transfer (smFRET)." Biophysica 2, no. 2 (June 6, 2022): 123–34. http://dx.doi.org/10.3390/biophysica2020014.
Повний текст джерелаHa, Taekjip. "Single-Molecule Fluorescence Resonance Energy Transfer." Methods 25, no. 1 (September 2001): 78–86. http://dx.doi.org/10.1006/meth.2001.1217.
Повний текст джерелаMetskas, Lauren Ann, and Elizabeth Rhoades. "Single-Molecule FRET of Intrinsically Disordered Proteins." Annual Review of Physical Chemistry 71, no. 1 (April 20, 2020): 391–414. http://dx.doi.org/10.1146/annurev-physchem-012420-104917.
Повний текст джерелаMeiser, Nathalie, Christin Fuks, and Martin Hengesbach. "Cooperative Analysis of Structural Dynamics in RNA-Protein Complexes by Single-Molecule Förster Resonance Energy Transfer Spectroscopy." Molecules 25, no. 9 (April 28, 2020): 2057. http://dx.doi.org/10.3390/molecules25092057.
Повний текст джерелаBeckers, M., F. Drechsler, T. Eilert, J. Nagy, and J. Michaelis. "Quantitative structural information from single-molecule FRET." Faraday Discussions 184 (2015): 117–29. http://dx.doi.org/10.1039/c5fd00110b.
Повний текст джерелаClamme, Jean-Pierre, and Ashok A. Deniz. "Three-Color Single-Molecule Fluorescence Resonance Energy Transfer." ChemPhysChem 6, no. 1 (January 14, 2005): 74–77. http://dx.doi.org/10.1002/cphc.200400261.
Повний текст джерелаHohng, Sungchul, and Taekjip Ha. "Single-Molecule Quantum-Dot Fluorescence Resonance Energy Transfer." ChemPhysChem 6, no. 5 (May 13, 2005): 956–60. http://dx.doi.org/10.1002/cphc.200400557.
Повний текст джерелаAriunbold, G. O., G. S. Agarwal, Z. Wang, M. O. Scully, and H. Walther. "Nanosecond Dynamics of Single-Molecule Fluorescence Resonance Energy Transfer." Journal of Physical Chemistry A 108, no. 13 (April 2004): 2402–4. http://dx.doi.org/10.1021/jp037609h.
Повний текст джерелаSasmal, Dibyendu K., Laura E. Pulido, Shan Kasal, and Jun Huang. "Single-molecule fluorescence resonance energy transfer in molecular biology." Nanoscale 8, no. 48 (2016): 19928–44. http://dx.doi.org/10.1039/c6nr06794h.
Повний текст джерелаOrte, Angel, Richard W. Clarke, and David Klenerman. "Fluorescence Coincidence Spectroscopy for Single-Molecule Fluorescence Resonance Energy-Transfer Measurements." Analytical Chemistry 80, no. 22 (November 15, 2008): 8389–97. http://dx.doi.org/10.1021/ac8009092.
Повний текст джерелаLi, Chen-chen, Ying Li, Yan Zhang, and Chun-yang Zhang. "Single-molecule fluorescence resonance energy transfer and its biomedical applications." TrAC Trends in Analytical Chemistry 122 (January 2020): 115753. http://dx.doi.org/10.1016/j.trac.2019.115753.
Повний текст джерелаZhao, Rui, and David Rueda. "RNA folding dynamics by single-molecule fluorescence resonance energy transfer." Methods 49, no. 2 (October 2009): 112–17. http://dx.doi.org/10.1016/j.ymeth.2009.04.017.
Повний текст джерелаLu, Maolin. "Single-Molecule FRET Imaging of Virus Spike–Host Interactions." Viruses 13, no. 2 (February 21, 2021): 332. http://dx.doi.org/10.3390/v13020332.
Повний текст джерелаBao, Shuying, Guangcun Shan, and Xinghai Zhao. "RNA Dynamics Probed by Single-Molecule Fluorescence Resonance Energy Transfer Studies." Journal of Computational and Theoretical Nanoscience 8, no. 4 (April 1, 2011): 664–69. http://dx.doi.org/10.1166/jctn.2011.1737.
Повний текст джерелаKim, Sung-Hyun, Don-Seong Choi, and Do-Seok Kim. "Single-molecule Detection of Fluorescence Resonance Energy Transfer Using Confocal Microscopy." Journal of the Optical Society of Korea 12, no. 2 (June 25, 2008): 107–11. http://dx.doi.org/10.3807/josk.2008.12.2.107.
Повний текст джерелаSchröder, Gunnar F., and Helmut Grubmüller. "Maximum likelihood trajectories from single molecule fluorescence resonance energy transfer experiments." Journal of Chemical Physics 119, no. 18 (November 8, 2003): 9920–24. http://dx.doi.org/10.1063/1.1616511.
Повний текст джерелаWang, Dong, and Eitan Geva. "Protein Structure and Dynamics from Single-Molecule Fluorescence Resonance Energy Transfer." Journal of Physical Chemistry B 109, no. 4 (February 2005): 1626–34. http://dx.doi.org/10.1021/jp0478864.
Повний текст джерелаSekatskii, S. K., G. Dietler, and V. S. Letokhov. "Single molecule fluorescence resonance energy transfer scanning near-field optical microscopy." Chemical Physics Letters 452, no. 1-3 (February 2008): 220–24. http://dx.doi.org/10.1016/j.cplett.2007.12.064.
Повний текст джерелаLi, H., L. Ying, X. Ren, S. Balasubramanian, and D. Klenerman. "Fluorescence studies of single biomolecules." Biochemical Society Transactions 32, no. 5 (October 26, 2004): 753–56. http://dx.doi.org/10.1042/bst0320753.
Повний текст джерелаRahmanseresht, Sheema, Peker Milas, Kieran P. Ramos, Ben D. Gamari, and Lori S. Goldner. "Single-molecule-sensitive fluorescence resonance energy transfer in freely-diffusing attoliter droplets." Applied Physics Letters 106, no. 19 (May 11, 2015): 194107. http://dx.doi.org/10.1063/1.4921202.
Повний текст джерелаKeller, Aaron M., Matthew S. DeVore, Dominik G. Stich, Dung M. Vu, Timothy Causgrove, and James H. Werner. "Multicolor Three-Dimensional Tracking for Single-Molecule Fluorescence Resonance Energy Transfer Measurements." Analytical Chemistry 90, no. 10 (April 19, 2018): 6109–15. http://dx.doi.org/10.1021/acs.analchem.8b00244.
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