Dr. Curran (seated right) discusses metagenomic analysis with students and professional collaborators. ©Wake Forest University/Ken Bennett
Professor Emeritus of Biology
Teacher-Scholar Legacies: Jim Curran
B.A., University of Delaware
M.A., Ph.D., Rice University
Postdoctoral Research, University of Colorado at Boulder
curran@wfu.edu
Past Administrative Positions
Chair of the Biology Department
Co-director of the Program in Environment and Sustainability
Areas of Interest
Molecular Mechanisms of Protein Synthesis and Microbial Ecology
Research
Students and I have performed a great deal of work on the molecular mechanism of protein synthesis. Our work has become increasingly computational, and we have begun to apply metagenomic and machine-learning tools to ecological questions.
Courses Taught
I primarily teach Microbiology, but I have taught Genetics, Biochemistry, Molecular Biology, Microbial Ecology, and Microbial Pathogenesis.
Publications
Curran, J.F., Zaggia, L., and Marina Quero, G. 2022. Metagenomic characterization of microbial pollutants, antibiotic- and metal-resistance genes in sediments from the canals of Venice. Water 14(7), 1161. [doi]
Freund, C., Clark, K., Curran, J., Asner, G., and Silman, M. 2021. Landslide age, elevation and residual vegetation determine tropical montane forest canopy recovery and biomass accumulation after landslide disturbances in the Peruvian Andes. Journal of Ecology. [doi]
Rosso, G.E., Muday, J.A. and Curran, J.F. 2018. Tools for metagenomic analysis at wastewater treatment plants: Application to a foaming episode. Water Environment Research, 90, 258-268. [doi] Note: This paper was the feature article for the March 2018 issue. It was also featured in the Research Notes section of the May 2018 issue of Water Environment & Technology
Lim, V.I., Curran, J.F. and Garber, M. 2012. Hydration shells of molecules in molecular association: a mechanism for biomolecular recognition. Journal of Theoretical Biology 301, 42-48. [doi]
Sanders, C.L., Lohr, K.J., Gambill, H.L, Curran, R.B. and Curran, J.F. 2008. Anticodon loop mutations perturb reading frame maintenance by the E site tRNA. RNA 14, 1874-1881. [doi]
Sanders, C.L. and Curran, J.F. 2007. Genetic analysis of the E site during RF2 programmed frameshifting. RNA 13, 1483-1491. [doi]
Lim, V.I., Curran, J.F. and Garber, M. 2005. Ribosomal elongation cycle: Energetic, Kinetic and Stereochemical aspects, Journal of Molecular Biology 351: 470-480. [doi]
Lim, V.I. and Curran, J.F. 2001. Analysis of Codon:Anticodon Interactions within the Ribosome Provides New Insights into Codon Reading and the Genetic Code Structure. RNA 7: 942-957. [doi]
Wu, L., and Curran, J.F. 1999. An allosteric synthetic DNA. Nucleic Acids Research 27: 1512-1516. [doi]
Tsai, F., and Curran, J.F. 1998. tRNA2Gln mutants that translate the CGA arginine codon as glutamine in Escherichia coli. RNA 4: 1514-1522. [doi]
Curran, J.F. 1998. Modified Nucleosides in Translation, chapter 27 in Modification and Editing of RNA: The Alteration of RNA Structure and Function, H. Grosjean, and R. Benne, eds. American Society for Microbiology Press, pp. 493-516.
Qian, Q., Curran, J.F., and Bjork, G.R. 1998. The N6-methyl group of the modified nucleoside N6-methyl-N6-threonylcarbamoyladenosine (m6t6A) in transfer RNA of Escherichia coli improves translational efficiency, Journal of Bacteriology 180: 1808-1813. [doi]
Li, J.-n., Esberg, B, Curran, J.F., and Bjork, G.R. 1997. Three modified nucleosides present in the anticodon stem and loop influence the in vivo aa-tRNA selection in a tRNA-dependent manner. Journal of Molecular Biology 271: 209-221. [doi]
Schwartz, R. and Curran, J.F. 1997. Analyses of frameshifting at UUU-pyrimidine sites, Nucleic Acids Research 25, 2005-2011. [doi]
Curran, J.F., Poole, E.S., Tate, W.P. and Gross, B.L. 1995. Selection of aminoacyl-tRNAs at sense codons: The size of the tRNA variable loop determines whether the immediate 3’ nucleotide to the codon has a context effect, Nucleic Acids Research 23, 4104-4108. [doi]
Curran, J.F. 1995. Decoding with the A:I base pair is inefficient. Nucleic Acids Research 23, 683-688. [doi]
Curran, J.F. and Gross, B.L. 1994. Evidence that GHN phase bias does not constitute a framing code. Journal of Molecular Biology 235, 389-395. [doi]
Curran, J.F. 1993. Analysis of effects of tRNA:message stability on frameshift frequency at the Escherichia coli RF2 programmed frameshift site. Nucleic Acids Research 21, 1837-1843. [doi]
Hagervall, T. G., B. Esberg, J-n. Li, T.M.F. Tuohy, J.F. Atkins, J.F. Curran, and G.R. Björk. 1993. Functional aspects of three nucleosides, pseudouridine, ms2io6A, and m1G, present in the anticodon loop of tRNA, in The Translational Apparatus, K. Nierhaus, Ed. Springer Verlag, pp. 67-78.
Yarus, M, and F. Curran. 1992. The Translational Context Effect, chapter 11 in Transfer RNA in Protein Synthesis, eds. D. Hatfield, B. Lee and R. Pirtle. CRC Press, pp. 319-365.
Pedersen, W.T. and Curran, J.F. 1991. Effects of the nucleotide 3′ to an amber codon on ribosomal selection rates of suppressor tRNA and release factor-1. Journal of Molecular Biology 219, 231-241. [doi]
Curran, J.F. and Yarus, M. 1989. Rates of tRNA selection by 29 specific codons in vivo. Journal of Molecular Biology. 209, 65-77. [doi]
Curran, J.F. and Yarus, M. 1988. Use of tRNA suppressors to probe regulation of E.coli RF-2. Journal of Molecular Biology 203, 75-83. [doi]
Curran, J.F. and Yarus, M. 1987. Reading frame selection and tRNA anticodon loop stacking. Science 238, 1545-1550. [doi]
Curran, J.F. and Yarus, M. 1986. Base substitutions in the tRNA anticodon arm do not degrade the accuracy of reading frame maintenance. Proceedings of the National Academy of Sciences, U.S.A. 83, 1638-1642. [doi]
Curran, J.F. and Stewart, C.R. 1985. Transcription of B. subtilis plasmid pBD64, and expression of bacteriophage SP01 genes cloned therein. Virology 142, 98-111. [doi]
Curran, J.F. and Stewart, C.R. 1985. Cloning and mapping of the SP01 genome. Virology 142, 78-97. [doi]
Curran, J.F. and Stewart, C.R. 1982. Recombination and expression of a cloned fragment of the DNA of Bacillus subtilis bacteriophage SP01. Virology 120, 307-317. [doi]