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Colby Stoddard, Ph.D. - Publications

Affiliations: 
2009 Chemistry University of Colorado, Boulder, Boulder, CO, United States 
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7 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2013 Stoddard CD, Widmann J, Trausch JJ, Marcano-Velázquez JG, Knight R, Batey RT. Nucleotides adjacent to the ligand-binding pocket are linked to activity tuning in the purine riboswitch. Journal of Molecular Biology. 425: 1596-611. PMID 23485418 DOI: 10.1016/J.Jmb.2013.02.023  0.743
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  0.758
2008 Stoddard CD, Gilbert SD, Batey RT. Ligand-dependent folding of the three-way junction in the purine riboswitch. Rna (New York, N.Y.). 14: 675-84. PMID 18268025 DOI: 10.1261/Rna.736908  0.794
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  0.686
2006 Stoddard CD, Batey RT. Mix-and-match riboswitches. Acs Chemical Biology. 1: 751-4. PMID 17240972 DOI: 10.1021/Cb600458W  0.617
2006 Gilbert SD, Stoddard CD, Wise SJ, Batey RT. Thermodynamic and kinetic characterization of ligand binding to the purine riboswitch aptamer domain. Journal of Molecular Biology. 359: 754-68. PMID 16650860 DOI: 10.1016/J.Jmb.2006.04.003  0.798
2006 Gilbert SD, Stoddard CD, Wise SJ, Batey RT. Erratum to “Thermodynamic and Kinetic Characterization of Ligand Binding to the Purine Riboswitch Aptamer Domain” [J. Mol. Biol. 359 (2006) 754–768] Journal of Molecular Biology. 363: 624. DOI: 10.1016/J.Jmb.2006.04.075  0.771
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