Year |
Citation |
Score |
2023 |
Forino NM, Woo JZ, Zaug AJ, Jimenez AG, Cech TR, Rouskin S, Stone MD. Dissecting telomerase RNA structural heterogeneity in living human cells with DMS-MaPseq. Biorxiv : the Preprint Server For Biology. PMID 37873413 DOI: 10.1101/2023.10.04.560962 |
0.424 |
|
2023 |
Hentschel J, Badstübner M, Choi J, Bagshaw CR, Lapointe CP, Wang J, Jansson LI, Puglisi JD, Stone MD. Real-time detection of human telomerase DNA synthesis by multiplexed single-molecule FRET. Biophysical Journal. PMID 37515327 DOI: 10.1016/j.bpj.2023.07.019 |
0.687 |
|
2022 |
Chang TR, Long X, Shastry S, Parks JW, Stone MD. Single-Molecule Mechanical Analysis of Strand Invasion in Human Telomere DNA. Biochemistry. 61: 1554-1560. PMID 35852986 DOI: 10.1021/acs.biochem.1c00448 |
0.758 |
|
2021 |
Bagshaw CR, Hentschel J, Stone MD. The Processivity of Telomerase: Insights from Kinetic Simulations and Analyses. Molecules (Basel, Switzerland). 26. PMID 34946615 DOI: 10.3390/molecules26247532 |
0.655 |
|
2021 |
Chang T, Draper JM, Van den Bout A, Kephart E, Maul-Newby H, Vasquez Y, Woodbury J, Randi S, Pedersen M, Nave M, La S, Gallagher N, McCabe MM, Dhillon N, Bjork I, ... ... Stone MD, et al. A method for campus-wide SARS-CoV-2 surveillance at a large public university. Plos One. 16: e0261230. PMID 34919584 DOI: 10.1371/journal.pone.0261230 |
0.519 |
|
2021 |
Thornlow B, Hinrichs AS, Jain M, Dhillon N, La S, Kapp JD, Anigbogu I, Cassatt-Johnstone M, McBroome J, Haeussler M, Turakhia Y, Chang T, Olsen HE, Sanford J, Stone M, et al. A new SARS-CoV-2 lineage that shares mutations with known Variants of Concern is rejected by automated sequence repository quality control. Biorxiv : the Preprint Server For Biology. PMID 33851162 DOI: 10.1101/2021.04.05.438352 |
0.535 |
|
2020 |
Palka C, Forino N, Hentschel J, Das R, Stone MD. Folding heterogeneity in the essential human telomerase RNA three-way junction. Rna (New York, N.Y.). PMID 32817241 DOI: 10.1261/Rna.077255.120 |
0.544 |
|
2019 |
Jansson LI, Stone MD. Single-Molecule Analysis of Reverse Transcriptase Enzymes. Cold Spring Harbor Perspectives in Biology. 11. PMID 31481455 DOI: 10.1101/Cshperspect.A032458 |
0.487 |
|
2019 |
Jansson LI, Hentschel J, Parks JW, Chang TR, Lu C, Baral R, Bagshaw CR, Stone MD. Telomere DNA G-quadruplex folding within actively extending human telomerase. Proceedings of the National Academy of Sciences of the United States of America. PMID 31019071 DOI: 10.1073/Pnas.1814777116 |
0.796 |
|
2018 |
Stone MD. Detailed view of human telomerase enzyme invites rethink of its structure. Nature. 557: 174-175. PMID 29730671 DOI: 10.1038/D41586-018-04756-3 |
0.444 |
|
2018 |
Shastry S, Steinberg-Neifach O, Lue N, Stone MD. Direct observation of nucleic acid binding dynamics by the telomerase essential N-terminal domain. Nucleic Acids Research. PMID 29474579 DOI: 10.1093/Nar/Gky117 |
0.575 |
|
2018 |
Long X, Chang T, Shastry S, Parks JW, Stone MD. Direct Measurement of Torque Induced Telomere Strand Invasion using Magnetic Tweezers Biophysical Journal. 114: 86a. DOI: 10.1016/J.Bpj.2017.11.515 |
0.494 |
|
2018 |
Palka C, Das R, Tzfati Y, Stone M. Investigating the Function of Conformational Heterogeneity in Telomerase RNA using Multi-dimensional Chemical Mapping and Single-Molecule Spectroscopy Biophysical Journal. 114: 215a. DOI: 10.1016/J.Bpj.2017.11.1201 |
0.384 |
|
2017 |
Musgrove C, Jansson LI, Stone MD. New perspectives on telomerase RNA structure and function. Wiley Interdisciplinary Reviews. Rna. PMID 29124890 DOI: 10.1002/Wrna.1456 |
0.512 |
|
2017 |
Parks JW, Stone MD. Single-Molecule Studies of Telomeres and Telomerase. Annual Review of Biophysics. PMID 28375735 DOI: 10.1146/Annurev-Biophys-062215-011256 |
0.469 |
|
2017 |
Parks JW, Kappel K, Das R, Stone MD. Single-molecule FRET-Rosetta reveals RNA structural rearrangements during human telomerase catalysis. Rna (New York, N.Y.). 23: 175-188. PMID 28096444 DOI: 10.1261/Rna.058743.116 |
0.479 |
|
2016 |
Long X, Parks JW, Stone MD. Integrated magnetic tweezers and single-molecule FRET for investigating the mechanical properties of nucleic acid. Methods (San Diego, Calif.). PMID 27320203 DOI: 10.1016/J.Ymeth.2016.06.009 |
0.507 |
|
2015 |
Jansson LI, Akiyama BM, Ooms A, Lu C, Rubin SM, Stone MD. Structural basis of template-boundary definition in Tetrahymena telomerase. Nature Structural & Molecular Biology. PMID 26436828 DOI: 10.1038/Nsmb.3101 |
0.8 |
|
2015 |
Akiyama BM, Parks JW, Stone MD. The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids. Nucleic Acids Research. 43: 5537-49. PMID 25940626 DOI: 10.1093/Nar/Gkv406 |
0.823 |
|
2015 |
Long X, Stone MD. Mechanical Properties and Strand Invasion of Duplex Telomere DNA Probed using Magnetic Tweezers Biophysical Journal. 108: 352a. DOI: 10.1016/J.Bpj.2014.11.1926 |
0.669 |
|
2014 |
Parks JW, Stone MD. Coordinated DNA dynamics during the human telomerase catalytic cycle. Nature Communications. 5: 4146. PMID 24923681 DOI: 10.1038/Ncomms5146 |
0.582 |
|
2014 |
Akiyama BM, Stone MD. Direct Visualization of DNA Dynamics During the Telomerase Catalytic Cycle Reveals the Function of a Conserved Telomerase Domain Biophysical Journal. 106: 429a-430a. DOI: 10.1016/J.Bpj.2013.11.2420 |
0.824 |
|
2013 |
Long X, Stone MD. Kinetic partitioning modulates human telomere DNA G-quadruplex structural polymorphism Plos One. 8. PMID 24367594 DOI: 10.1371/Journal.Pone.0083420 |
0.65 |
|
2013 |
Akiyama BM, Gomez A, Stone MD. A conserved motif in tetrahymena thermophila telomerase reverse transcriptase is proximal to the RNA template and is essential for boundary definition Journal of Biological Chemistry. 288: 22141-22149. PMID 23760279 DOI: 10.1074/Jbc.M113.452425 |
0.807 |
|
2013 |
Akiyama BM, Stone MD. Structural biology: A solution to the telomerase puzzle Nature. 496: 177-178. PMID 23552897 DOI: 10.1038/Nature12090 |
0.785 |
|
2013 |
Long X, Parks JW, Bagshaw CR, Stone MD. Mechanical unfolding of human telomere G-quadruplex DNA probed by integrated fluorescence and magnetic tweezers spectroscopy. Nucleic Acids Research. 41: 2746-55. PMID 23303789 DOI: 10.1093/Nar/Gks1341 |
0.736 |
|
2012 |
Hengesbach M, Kim NK, Feigon J, Stone MD. Single-molecule FRET reveals the folding dynamics of the human telomerase rna pseudoknot domain Angewandte Chemie - International Edition. 51: 5876-5879. PMID 22544760 DOI: 10.1002/Anie.201200526 |
0.571 |
|
2012 |
Akiyama BM, Loper J, Najarro K, Stone MD. The C-terminal domain of Tetrahymena thermophila telomerase holoenzyme protein p65 induces multiple structural changes in telomerase RNA Rna. 18: 653-660. PMID 22315458 DOI: 10.1261/Rna.031377.111 |
0.775 |
|
2012 |
Hengesbach M, Stone MD. Single Molecule Analysis of Human Telomerase RNA Pseudoknot Folding and Dynamics Biophysical Journal. 102: 644a. DOI: 10.1016/J.Bpj.2011.11.3507 |
0.528 |
|
2012 |
Wu JY, Mihalusova M, Stone MD, Zhuang X. Single-Molecule Analysis of the Functional Structure of Telomerase RNP Biophysical Journal. 102: 421a. DOI: 10.1016/J.Bpj.2011.11.2302 |
0.719 |
|
2011 |
Berman AJ, Akiyama BM, Stone MD, Cech TR. The RNA accordion model for template positioning by telomerase RNA during telomeric DNA synthesis. Nature Structural & Molecular Biology. 18: 1371-5. PMID 22101935 DOI: 10.1038/Nsmb.2174 |
0.817 |
|
2011 |
Hengesbach M, Akiyama BM, Stone MD. Single-molecule analysis of telomerase structure and function Current Opinion in Chemical Biology. 15: 846-852. PMID 22057212 DOI: 10.1016/J.Cbpa.2011.10.008 |
0.79 |
|
2009 |
Akiyama BM, Stone MD. Assembly of complex RNAs by splinted ligation. Methods in Enzymology. 469: 27-46. PMID 20946783 DOI: 10.1016/S0076-6879(09)69002-9 |
0.771 |
|
2009 |
Blosser TR, Yang JG, Stone MD, Narlikar GJ, Zhuang X. Dynamics of nucleosome remodelling by individual ACF complexes Nature. 462: 1022-1027. PMID 20033040 DOI: 10.1038/Nature08627 |
0.786 |
|
2009 |
Wu JY, Stone MD, Zhuang X. A single-molecule assay for telomerase structure-function analysis Nucleic Acids Research. 38: e16.1-e16.11. PMID 19920121 DOI: 10.1093/Nar/Gkp1033 |
0.688 |
|
2009 |
Blosser TR, Stone MD, Yang J, Narlikar G, Zhuang X. Nucleosome Sliding by ACF is Processive and Bidirectional Biophysical Journal. 96: 566a. DOI: 10.1016/J.Bpj.2008.12.3713 |
0.8 |
|
2009 |
Mihalusova M, Stone MD, Wu JY, Zhuang X. Conformation of Telomerase RNP Established through Footprinting and Single-Molecule FRET Biophysical Journal. 96: 416a. DOI: 10.1016/J.Bpj.2008.12.2127 |
0.717 |
|
2009 |
Wu JY, Stone MD, Mihalusova M, Zhuang X. Caught in the Act: Single Molecule Structure-Function Studies of Telomerase Biophysical Journal. 96: 416a. DOI: 10.1016/J.Bpj.2008.12.2126 |
0.731 |
|
2007 |
Nöllmann M, Stone MD, Bryant Z, Gore J, Crisona NJ, Hong SC, Mitelheiser S, Maxwell A, Bustamante C, Cozzarelli NR. Multiple modes of Escherichia coli DNA gyrase activity revealed by force and torque. Nature Structural & Molecular Biology. 14: 264-71. PMID 17334374 DOI: 10.1038/Nsmb1213 |
0.761 |
|
2007 |
Stone MD, Mihalusova M, O'Connor CM, Prathapam R, Collins K, Zhuang X. Stepwise protein-mediated RNA folding directs assembly of telomerase ribonucleoprotein Nature. 446: 458-461. PMID 17322903 DOI: 10.1038/Nature05600 |
0.631 |
|
2006 |
Gore J, Bryant Z, Stone MD, Nöllmann M, Cozzarelli NR, Bustamante C. Mechanochemical analysis of DNA gyrase using rotor bead tracking. Nature. 439: 100-4. PMID 16397501 DOI: 10.1038/Nature04319 |
0.674 |
|
2004 |
Hardy CD, Crisona NJ, Stone MD, Cozzarelli NR. Disentangling DNA during replication: a tale of two strands. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 359: 39-47. PMID 15065655 DOI: 10.1098/Rstb.2003.1363 |
0.801 |
|
2003 |
Bryant Z, Stone MD, Gore J, Smith SB, Cozzarelli NR, Bustamante C. Structural transitions and elasticity from torque measurements on DNA. Nature. 424: 338-41. PMID 12867987 DOI: 10.1038/Nature01810 |
0.66 |
|
2003 |
Stone MD, Bryant Z, Crisona NJ, Smith SB, Vologodskii A, Bustamante C, Cozzarelli NR. Chirality sensing by Escherichia coli topoisomerase IV and the mechanism of type II topoisomerases. Proceedings of the National Academy of Sciences of the United States of America. 100: 8654-9. PMID 12857958 DOI: 10.1073/Pnas.1133178100 |
0.656 |
|
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