Rebecca Montange, Ph.D. - Publications
Affiliations: | University of Colorado/JILA |
Year | Citation | Score | |||
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2018 | Walder R, Van Patten WJ, Ritchie DB, Montange RK, Miller TW, Woodside MT, Perkins TT. High-Precision Single-Molecule Characterization of the Folding of an HIV RNA Hairpin by Atomic Force Microscopy. Nano Letters. PMID 30234311 DOI: 10.1021/Acs.Nanolett.8B02597 | 0.609 | |||
2013 | Montange RK, Bull MS, Shanblatt ER, Perkins TT. Optimizing bead size reduces errors in force measurements in optical traps. Optics Express. 21: 39-48. PMID 23388894 DOI: 10.1364/OE.21.000039 | 0.407 | |||
2012 | Montange RK, Bull MS, Shanblatt ER, Perkins TT. Optimizing Bead Size Improves Force Precision in Optical Traps Biophysical Journal. 102: 577a. DOI: 10.1016/j.bpj.2011.11.3142 | 0.404 | |||
2010 | Stoddard CD, Montange RK, Hennelly SP, Rambo RP, Sanbonmatsu KY, Batey RT. Free state conformational sampling of the SAM-I riboswitch aptamer domain. Structure (London, England : 1993). 18: 787-97. PMID 20637415 DOI: 10.1016/J.Str.2010.04.006 | 0.718 | |||
2010 | Montange RK, Mondragón E, van Tyne D, Garst AD, Ceres P, Batey RT. Discrimination between closely related cellular metabolites by the SAM-I riboswitch. Journal of Molecular Biology. 396: 761-72. PMID 20006621 DOI: 10.1016/J.Jmb.2009.12.007 | 0.721 | |||
2008 | Montange RK, Batey RT. Riboswitches: emerging themes in RNA structure and function. Annual Review of Biophysics. 37: 117-33. PMID 18573075 DOI: 10.1146/Annurev.Biophys.37.032807.130000 | 0.711 | |||
2006 | Gilbert SD, Montange RK, Stoddard CD, Batey RT. Structural studies of the purine and SAM binding riboswitches. Cold Spring Harbor Symposia On Quantitative Biology. 71: 259-68. PMID 17381305 DOI: 10.1101/Sqb.2006.71.015 | 0.65 | |||
2006 | Montange RK, Batey RT. Structure of the S-adenosylmethionine riboswitch regulatory mRNA element. Nature. 441: 1172-5. PMID 16810258 DOI: 10.1038/Nature04819 | 0.729 | |||
2004 | Batey RT, Gilbert SD, Montange RK. Structure of a natural guanine-responsive riboswitch complexed with the metabolite hypoxanthine. Nature. 432: 411-5. PMID 15549109 DOI: 10.1038/Nature03037 | 0.701 | |||
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