| Year |
Citation |
Score |
| 2023 |
Potratz JP, Russell R. Tracking Native Ribozyme Folding with Fluorescence. Biochemistry. PMID 37910627 DOI: 10.1021/acs.biochem.3c00363 |
0.356 |
|
| 2022 |
Jarmoskaite I, Helmers AE, Russell R. Measurement of ATP utilization in RNA unwinding and RNA chaperone activities by DEAD-box helicase proteins. Methods in Enzymology. 673: 53-76. PMID 35965018 DOI: 10.1016/bs.mie.2022.04.004 |
0.587 |
|
| 2022 |
Chang-Gu B, Venkatesan S, Russell R. Kinetics measurements of G-quadruplex binding and unfolding by helicases. Methods (San Diego, Calif.). PMID 35483547 DOI: 10.1016/j.ymeth.2022.04.012 |
0.327 |
|
| 2021 |
Das R, Russell R. How to Kinetically Dissect an RNA Machine. Biochemistry. PMID 34492193 DOI: 10.1021/acs.biochem.1c00392 |
0.495 |
|
| 2021 |
Lentzsch AM, Stamos JL, Yao J, Russell R, Lambowitz AM. Structural basis for template switching by a group II intron-encoded non-LTR-retroelement reverse transcriptase. The Journal of Biological Chemistry. 100971. PMID 34280434 DOI: 10.1016/j.jbc.2021.100971 |
0.548 |
|
| 2021 |
Luke Ward W, Russell R. Key Points to Consider When Studying RNA Remodeling by Proteins. Methods in Molecular Biology (Clifton, N.J.). 2209: 1-16. PMID 33201459 DOI: 10.1007/978-1-0716-0935-4_1 |
0.619 |
|
| 2020 |
Jarmoskaite I, Tijerina P, Russell R. ATP utilization by a DEAD-box protein during refolding of a misfolded group I intron ribozyme. The Journal of Biological Chemistry. PMID 33262215 DOI: 10.1074/jbc.RA120.015029 |
0.564 |
|
| 2019 |
Lentzsch AM, Yao J, Russell R, Lambowitz AM. Template switching mechanism of a group II intron-encoded reverse transcriptase and its implications for biological function and RNA-Seq. The Journal of Biological Chemistry. PMID 31712313 DOI: 10.1074/Jbc.Ra119.011337 |
0.483 |
|
| 2018 |
Gracia B, Al-Hashimi HM, Bisaria N, Das R, Herschlag D, Russell R. Hidden Structural Modules in a Cooperative RNA Folding Transition. Cell Reports. 22: 3240-3250. PMID 29562180 DOI: 10.1016/J.Celrep.2018.02.101 |
0.669 |
|
| 2017 |
Yangyuoru PM, Bradburn DA, Liu Z, Xiao TS, Russell R. The G-quadruplex (G4) resolvase DHX36 efficiently and specifically disrupts DNA G4s via a translocation-based helicase mechanism. The Journal of Biological Chemistry. PMID 29269411 DOI: 10.1074/Jbc.M117.815076 |
0.302 |
|
| 2017 |
Gilman B, Tijerina P, Russell R. Distinct RNA-unwinding mechanisms of DEAD-box and DEAH-box RNA helicase proteins in remodeling structured RNAs and RNPs. Biochemical Society Transactions. PMID 29150525 DOI: 10.1042/Bst20170095 |
0.674 |
|
| 2017 |
Busa VF, Rector MJ, Russell R. The DEAD-box Protein CYT-19 Uses Arginine Residues in Its C-tail to Tether RNA Substrates. Biochemistry. PMID 28650145 DOI: 10.1021/Acs.Biochem.7B00362 |
0.639 |
|
| 2016 |
Gracia B, Xue Y, Bisaria N, Herschlag D, Al-Hashimi HM, Russell R. RNA Structural Modules Control the Rate and Pathway of RNA Folding and Assembly. Journal of Molecular Biology. PMID 27452365 DOI: 10.1016/J.Jmb.2016.07.013 |
0.589 |
|
| 2016 |
Xue Y, Gracia B, Herschlag D, Russell R, Al-Hashimi HM. Visualizing the formation of an RNA folding intermediate through a fast highly modular secondary structure switch. Nature Communications. 7: ncomms11768. PMID 27292179 DOI: 10.1038/Ncomms11768 |
0.596 |
|
| 2015 |
Cannon B, Kachroo AH, Jarmoskaite I, Jayaram M, Russell R. Hexapeptides That Inhibit Processing of Branched DNA Structures Induce a Dynamic Ensemble of Holliday Junction Conformations. The Journal of Biological Chemistry. 290: 22734-46. PMID 26209636 DOI: 10.1074/Jbc.M115.663930 |
0.364 |
|
| 2015 |
Russell R. Unwinding the mechanisms of a DEAD-box RNA helicase in cancer. Journal of Molecular Biology. 427: 1797-800. PMID 25836982 DOI: 10.1016/J.Jmb.2015.03.009 |
0.601 |
|
| 2015 |
Russell R. Reflections on 20 years of RNA folding, dynamics, and structure. Rna (New York, N.Y.). 21: 723-4. PMID 25780209 DOI: 10.1261/Rna.050781.115 |
0.691 |
|
| 2015 |
Ward WL, Russell R. Key points to consider when studying RNA remodeling by proteins. Methods in Molecular Biology (Clifton, N.J.). 1259: 1-16. PMID 25579576 DOI: 10.1007/978-1-4939-2214-7_1 |
0.678 |
|
| 2014 |
Pan C, Potratz JP, Cannon B, Simpson ZB, Ziehr JL, Tijerina P, Russell R. DEAD-box helicase proteins disrupt RNA tertiary structure through helix capture. Plos Biology. 12: e1001981. PMID 25350280 DOI: 10.1371/Journal.Pbio.1001981 |
0.701 |
|
| 2014 |
Jarmoskaite I, Bhaskaran H, Seifert S, Russell R. DEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA. Proceedings of the National Academy of Sciences of the United States of America. 111: E2928-36. PMID 25002474 DOI: 10.1073/Pnas.1404307111 |
0.851 |
|
| 2014 |
Mitchell D, Russell R. Folding pathways of the Tetrahymena ribozyme. Journal of Molecular Biology. 426: 2300-12. PMID 24747051 DOI: 10.1016/J.Jmb.2014.04.011 |
0.504 |
|
| 2014 |
Jarmoskaite I, Russell R. RNA helicase proteins as chaperones and remodelers. Annual Review of Biochemistry. 83: 697-725. PMID 24635478 DOI: 10.1146/Annurev-Biochem-060713-035546 |
0.582 |
|
| 2014 |
Gracia B, Russell R. RNA catalytic activity as a probe of chaperone-mediated RNA folding. Methods in Molecular Biology (Clifton, N.J.). 1086: 225-37. PMID 24136607 DOI: 10.1007/978-1-62703-667-2_13 |
0.669 |
|
| 2013 |
Contreras LM, Huang T, Piazza CL, Smith D, Qu G, Gelderman G, Potratz JP, Russell R, Belfort M. Group II intron-ribosome association protects intron RNA from degradation. Rna (New York, N.Y.). 19: 1497-509. PMID 24046482 DOI: 10.1261/Rna.039073.113 |
0.61 |
|
| 2013 |
Truong DM, Sidote DJ, Russell R, Lambowitz AM. Enhanced group II intron retrohoming in magnesium-deficient Escherichia coli via selection of mutations in the ribozyme core. Proceedings of the National Academy of Sciences of the United States of America. 110: E3800-9. PMID 24043808 DOI: 10.1073/Pnas.1315742110 |
0.533 |
|
| 2013 |
Mitchell D, Jarmoskaite I, Seval N, Seifert S, Russell R. The long-range P3 helix of the Tetrahymena ribozyme is disrupted during folding between the native and misfolded conformations. Journal of Molecular Biology. 425: 2670-86. PMID 23702292 DOI: 10.1016/J.Jmb.2013.05.008 |
0.449 |
|
| 2013 |
Russell R, Jarmoskaite I, Lambowitz AM. Toward a molecular understanding of RNA remodeling by DEAD-box proteins. Rna Biology. 10: 44-55. PMID 22995827 DOI: 10.4161/Rna.22210 |
0.653 |
|
| 2012 |
Potratz JP, Russell R. RNA catalysis as a probe for chaperone activity of DEAD-box helicases. Methods in Enzymology. 511: 111-30. PMID 22713317 DOI: 10.1016/B978-0-12-396546-2.00005-X |
0.648 |
|
| 2011 |
Sinan S, Yuan X, Russell R. The Azoarcus group I intron ribozyme misfolds and is accelerated for refolding by ATP-dependent RNA chaperone proteins. The Journal of Biological Chemistry. 286: 37304-12. PMID 21878649 DOI: 10.1074/Jbc.M111.287706 |
0.69 |
|
| 2011 |
Mallam AL, Jarmoskaite I, Tijerina P, Del Campo M, Seifert S, Guo L, Russell R, Lambowitz AM. Solution structures of DEAD-box RNA chaperones reveal conformational changes and nucleic acid tethering by a basic tail Proceedings of the National Academy of Sciences of the United States of America. 108: 12254-12259. PMID 21746911 DOI: 10.1073/Pnas.1109566108 |
0.655 |
|
| 2011 |
Potratz JP, Del Campo M, Wolf RZ, Lambowitz AM, Russell R. ATP-dependent roles of the DEAD-box protein Mss116p in group II intron splicing in vitro and in vivo Journal of Molecular Biology. 411: 661-679. PMID 21679717 DOI: 10.1016/J.Jmb.2011.05.047 |
0.673 |
|
| 2011 |
Jarmoskaite I, Russell R. DEAD-box proteins as RNA helicases and chaperones. Wiley Interdisciplinary Reviews. Rna. 2: 135-52. PMID 21297876 DOI: 10.1002/Wrna.50 |
0.654 |
|
| 2011 |
Wan Y, Russell R. Enhanced specificity against misfolding in a thermostable mutant of the Tetrahymena ribozyme. Biochemistry. 50: 864-74. PMID 21174447 DOI: 10.1021/Bi101467Q |
0.623 |
|
| 2010 |
Pan C, Russell R. Roles of DEAD-box proteins in RNA and RNP Folding. Rna Biology. 7: 667-76. PMID 21045543 DOI: 10.4161/Rna.7.6.13571 |
0.693 |
|
| 2010 |
Wan Y, Suh H, Russell R, Herschlag D. Multiple unfolding events during native folding of the Tetrahymena group I ribozyme. Journal of Molecular Biology. 400: 1067-77. PMID 20541557 DOI: 10.1016/J.Jmb.2010.06.010 |
0.517 |
|
| 2010 |
Chadee AB, Bhaskaran H, Russell R. Protein roles in group I intron RNA folding: the tyrosyl-tRNA synthetase CYT-18 stabilizes the native state relative to a long-lived misfolded structure without compromising folding kinetics. Journal of Molecular Biology. 395: 656-70. PMID 19913030 DOI: 10.1016/J.Jmb.2009.11.009 |
0.775 |
|
| 2010 |
Flores SC, Wan Y, Russell R, Altman RB. Predicting RNA structure by multiple template homology modeling. Pacific Symposium On Biocomputing. Pacific Symposium On Biocomputing. 216-27. PMID 19908374 |
0.565 |
|
| 2009 |
Wan Y, Mitchell D, Russell R. Catalytic activity as a probe of native RNA folding. Methods in Enzymology. 468: 195-218. PMID 20946771 DOI: 10.1016/S0076-6879(09)68010-1 |
0.668 |
|
| 2009 |
Mertz JA, Chadee AB, Byun H, Russell R, Dudley JP. Mapping of the functional boundaries and secondary structure of the mouse mammary tumor virus Rem-responsive element. The Journal of Biological Chemistry. 284: 25642-52. PMID 19632991 DOI: 10.1074/Jbc.M109.012476 |
0.766 |
|
| 2008 |
Chen Y, Potratz JP, Tijerina P, Del Campo M, Lambowitz AM, Russell R. DEAD-box proteins can completely separate an RNA duplex using a single ATP Proceedings of the National Academy of Sciences of the United States of America. 105: 20203-20208. PMID 19088196 DOI: 10.1073/Pnas.0811075106 |
0.637 |
|
| 2008 |
Bevilacqua PC, Russell R. Editorial overview: exploring the vast dynamic range of RNA dynamics. Current Opinion in Chemical Biology. 12: 601-3. PMID 19013256 DOI: 10.1016/J.Cbpa.2008.10.006 |
0.551 |
|
| 2008 |
Russell R. RNA misfolding and the action of chaperones. Frontiers in Bioscience : a Journal and Virtual Library. 13: 1-20. PMID 17981525 DOI: 10.2741/2557 |
0.687 |
|
| 2007 |
Bhaskaran H, Russell R. Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperone. Nature. 449: 1014-8. PMID 17960235 DOI: 10.1038/Nature06235 |
0.843 |
|
| 2007 |
Tijerina P, Mohr S, Russell R. DMS footprinting of structured RNAs and RNA-protein complexes. Nature Protocols. 2: 2608-23. PMID 17948004 DOI: 10.1038/Nprot.2007.380 |
0.658 |
|
| 2007 |
Del Campo M, Tijerina P, Bhaskaran H, Mohr S, Yang Q, Jankowsky E, Russell R, Lambowitz AM. Do DEAD-Box Proteins Promote Group II Intron Splicing without Unwinding RNA? Molecular Cell. 28: 159-166. PMID 17936712 DOI: 10.1016/J.Molcel.2007.07.028 |
0.831 |
|
| 2007 |
Russell R, Tijerina P, Chadee AB, Bhaskaran H. Deletion of the P5abc peripheral element accelerates early and late folding steps of the Tetrahymena group I ribozyme. Biochemistry. 46: 4951-61. PMID 17419589 DOI: 10.1021/Bi0620149 |
0.722 |
|
| 2007 |
Grohman JK, Del Campo M, Bhaskaran H, Tijerina P, Lambowitz AM, Russell R. Probing the mechanisms of DEAD-box proteins as general RNA chaperones: The C-terminal domain of CYT-19 mediates general recognition of RNA Biochemistry. 46: 3013-3022. PMID 17311413 DOI: 10.1021/Bi0619472 |
0.842 |
|
| 2006 |
Tijerina P, Bhaskaran H, Russell R. Nonspecific binding to structured RNA and preferential unwinding of an exposed helix by the CYT-19 protein, a DEAD-box RNA chaperone. Proceedings of the National Academy of Sciences of the United States of America. 103: 16698-703. PMID 17075070 DOI: 10.1073/Pnas.0603127103 |
0.844 |
|
| 2006 |
Russell R, Das R, Suh H, Travers KJ, Laederach A, Engelhardt MA, Herschlag D. The paradoxical behavior of a highly structured misfolded intermediate in RNA folding. Journal of Molecular Biology. 363: 531-44. PMID 16963081 DOI: 10.1016/J.Jmb.2006.08.024 |
0.597 |
|
| 2006 |
Lee JC, Gutell RR, Russell R. The UAA/GAN internal loop motif: a new RNA structural element that forms a cross-strand AAA stack and long-range tertiary interactions. Journal of Molecular Biology. 360: 978-88. PMID 16828489 DOI: 10.1016/J.Jmb.2006.05.066 |
0.637 |
|
| 2005 |
Johnson TH, Tijerina P, Chadee AB, Herschlag D, Russell R. Structural specificity conferred by a group I RNA peripheral element. Proceedings of the National Academy of Sciences of the United States of America. 102: 10176-81. PMID 16009943 DOI: 10.1073/Pnas.0501498102 |
0.822 |
|
| 2002 |
Russell R, Millett IS, Tate MW, Kwok LW, Nakatani B, Gruner SM, Mochrie SG, Pande V, Doniach S, Herschlag D, Pollack L. Rapid compaction during RNA folding. Proceedings of the National Academy of Sciences of the United States of America. 99: 4266-71. PMID 11929997 DOI: 10.1073/Pnas.072589599 |
0.63 |
|
| 2002 |
Russell R, Zhuang X, Babcock HP, Millett IS, Doniach S, Chu S, Herschlag D. Exploring the folding landscape of a structured RNA. Proceedings of the National Academy of Sciences of the United States of America. 99: 155-60. PMID 11756689 DOI: 10.1073/Pnas.221593598 |
0.64 |
|
| 2001 |
Russell R, Herschlag D. Probing the folding landscape of the Tetrahymena ribozyme: commitment to form the native conformation is late in the folding pathway. Journal of Molecular Biology. 308: 839-51. PMID 11352576 DOI: 10.1006/Jmbi.2001.4751 |
0.596 |
|
| 2000 |
Zhuang X, Bartley LE, Babcock HP, Russell R, Ha T, Herschlag D, Chu S. A single-molecule study of RNA catalysis and folding. Science (New York, N.Y.). 288: 2048-51. PMID 10856219 DOI: 10.1126/Science.288.5473.2048 |
0.521 |
|
| 2000 |
Russell R, Millett IS, Doniach S, Herschlag D. Small angle X-ray scattering reveals a compact intermediate in RNA folding. Nature Structural Biology. 7: 367-70. PMID 10802731 DOI: 10.1038/75132 |
0.547 |
|
| 2000 |
Zhuang X, Bartley L, Babcock H, Russell R, Ha T, Herschlag D, Chu S. Observing folding and catalysis of a single RNA enzyme molecule Pacific Rim Conference On Lasers and Electro-Optics, Cleo - Technical Digest. 588-589. |
0.446 |
|
| 1999 |
Russell R, Herschlag D. New pathways in folding of the Tetrahymena group I RNA enzyme Journal of Molecular Biology. 291: 1155-1167. PMID 10518951 DOI: 10.1006/Jmbi.1999.3026 |
0.56 |
|
| 1999 |
Russell R, Herschlag D. Specificity from steric restrictions in the guanosine binding pocket of a group I ribozyme Rna. 5: 158-166. PMID 10024168 DOI: 10.1017/S1355838299981839 |
0.427 |
|
| 1998 |
Russell R, Jordan R, McMacken R. Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone Biochemistry. 37: 596-607. PMID 9425082 DOI: 10.1021/Bi972025P |
0.664 |
|
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