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Hengesbach, Martin, Kim, Nak-Kyoon, Feigon, Juli, Stone, Michael D. (2012) Single-Molecule FRET Reveals the Folding Dynamics of the Human Telomerase RNA Pseudoknot Domain. Angewandte Chemie, 124 (24). 5978-5981 doi:10.1002/ange.201200526

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Reference TypeJournal (article/letter/editorial)
TitleSingle-Molecule FRET Reveals the Folding Dynamics of the Human Telomerase RNA Pseudoknot Domain
JournalAngewandte Chemie
AuthorsHengesbach, MartinAuthor
Kim, Nak-KyoonAuthor
Feigon, JuliAuthor
Stone, Michael D.Author
Year2012 (June 11)Volume124
Issue24
PublisherWiley
DOIdoi:10.1002/ange.201200526Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID7319093Long-form Identifiermindat:1:5:7319093:0
GUID0
Full ReferenceHengesbach, Martin, Kim, Nak-Kyoon, Feigon, Juli, Stone, Michael D. (2012) Single-Molecule FRET Reveals the Folding Dynamics of the Human Telomerase RNA Pseudoknot Domain. Angewandte Chemie, 124 (24). 5978-5981 doi:10.1002/ange.201200526
Plain TextHengesbach, Martin, Kim, Nak-Kyoon, Feigon, Juli, Stone, Michael D. (2012) Single-Molecule FRET Reveals the Folding Dynamics of the Human Telomerase RNA Pseudoknot Domain. Angewandte Chemie, 124 (24). 5978-5981 doi:10.1002/ange.201200526
In(2012, June) Angewandte Chemie Vol. 124 (24) Wiley

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Hengesbach, Martin, Kim, Nak-Kyoon, Feigon, Juli, Stone, Michael D. (2012) Single-Molecule FRET Reveals the Folding Dynamics of the Human Telomerase RNA Pseudoknot Domain. Angewandte Chemie International Edition, 51 (24). 5876-5879 doi:10.1002/anie.201200526
Kim, Nak-Kyoon, Zhang, Qi, Zhou, Jing, Theimer, Carla A., Peterson, Robert D., Feigon, Juli (2008) Solution Structure and Dynamics of the Wild-type Pseudoknot of Human Telomerase RNA. Journal of Molecular Biology, 384 (5). 1249-1261 doi:10.1016/j.jmb.2008.10.005
Wang, Yaqiang, Yesselman, Joseph D., Zhang, Qi, Kang, Mijeong, Feigon, Juli (2016) Structural conservation in the template/pseudoknot domain of vertebrate telomerase RNA from teleost fish to human. Proceedings of the National Academy of Sciences, 113 (35) doi:10.1073/pnas.1607411113
Holmstrom, Erik D., Nesbitt, David J. (2014) Single-Molecule Fluorescence Resonance Energy Transfer Studies of the Human Telomerase RNA Pseudoknot: Temperature-/Urea-Dependent Folding Kinetics and Thermodynamics. The Journal of Physical Chemistry B, 118 (14). 3853-3863 doi:10.1021/jp501893c
Holmstrom, Erik D., Nesbitt, David J. (2014) Correction to “Single-Molecule Fluorescence Resonance Energy Transfer Studies of the Human Telomerase RNA Pseudoknot: Temperature-/Urea-Dependent Folding Kinetics and Thermodynamics”. The Journal of Physical Chemistry B, 118 (22). 6048 doi:10.1021/jp504558u
Kobitski, Andrei Yu., Hengesbach, Martin, Helm, Mark, Nienhaus, G. Ulrich (2008) Sculpting an RNA Conformational Energy Landscape by a Methyl Group Modification—A Single-Molecule FRET Study. Angewandte Chemie International Edition, 47 (23). 4326-4330 doi:10.1002/anie.200705675
Kobitski, Andrei Yu., Hengesbach, Martin, Helm, Mark, Nienhaus, G. Ulrich (2008) Ausformung einer RNA-Konformationsenergielandschaft durch eine Methylgruppenmodifikation – eine Einzelmolekül-FRET-Studie. Angewandte Chemie, 120 (23). 4398-4402 doi:10.1002/ange.200705675
Kang, Mijeong, Heuberger, Ben, Chaput, John C., Switzer, Christopher, Feigon, Juli (2012) Solution Structure of a Parallel-Stranded Oligoisoguanine DNA Pentaplex Formed by d(T(iG)4T) in the Presence of Cs+ Ions. Angewandte Chemie, 124 (32). 8076-8079 doi:10.1002/ange.201203459
Biyun, Shi, Cho, Samuel S., Thirumalai, D. (2011) Folding of Human Telomerase RNA Pseudoknot Using Ion-Jump and Temperature-Quench Simulations. Journal Of The American Chemical Society, 133 (50) 20634-20643 doi:10.1021/ja2092823
Hengesbach, Martin, Schwalbe, Harald (2014) Strukturelle Grundlage der Regulation der 2′-O-Methylierung ribosomaler RNA. Angewandte Chemie, 126 (7). 1770-1772 doi:10.1002/ange.201309604
Zhang, Q., Kim, N.-K., Peterson, R. D., Wang, Z., Feigon, J. (2010) Structurally conserved five nucleotide bulge determines the overall topology of the core domain of human telomerase RNA. Proceedings of the National Academy of Sciences, 107 (44) 18761-18768 doi:10.1073/pnas.1013269107
 
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