Gone, S., Alfonso-Prieto, M., Paudyal, S. and Nicholson, A.W. 2016. Mechanism of ribonuclease III catalytic regulation by serine phosphorylation. Sci. Rep. 6: 25448.

Glassford, I., Teijaro, C.N., Daher, S.S., Weil. A., Small, M.C., Redhu, S.K., Colussi, D.H.J., Jacobson, M.A., Childers, W.E., Nicholson, A.W., MacKerell, A.D., Jr, Cooperman, B.S.,and Andrade, R.B. 2016. Ribosome-template azide-alkyne cycloadditions: synthesis of potent macrolide antibiotics by click chemistry. J. Am. Chem. Soc. 138:3136-3144.

Paudyal, S., Alfonso-Prieto, M., Redhu, S.K., Carnevale, V., Klein, M.L. and Nicholson, A.W. 2015. Combined computation and experimental analysis of a complex of ribonuclease III and the regulatory macrodomain protein, YmdB. Proteins 83:459-472.  doi: 10.1002/prot.24751

Nicholson, A.W. 2014. RNase III mechanisms of double-stranded RNA cleavage. Wiley Interdiscip. Rev. RNA 5:31-48.

Redhu, S.K., Castronovo, M., and Nicholson, A.W. 2013. Digital imprinting of RNA recognition and processing on a self-assembled nucleic acid matrix. Scientific Reports 3:2550  doi: 10.1038/srep02550.

Castronovo, M., Stopar, A., Coral, L., Redhu, S.K., Vidonis, M., Kumar, V., Del Ben, F., Grassi, M. and Nicholson, A.W. 2013. Effects of nanoscale confinement on the functionality of nucleic acids: implications for nanomedicine. Current Med. Chem. 20:3539-3557.

Nicholson, A.W. 2012. Dissecting human dicer: some assembly required. J. Mol. Biol. 422: 464-465.

Gone, S. and Nicholson, A.W. 2012.  Bacteriophage T7 protein kinase. Site of inhibitory autophosphorylation, and use of dephosphorylated enzyme for efficient modification of protein in vitro. Prot. Expr. Purif. 85:218-223.

Alla, N.R. and Nicholson, A.W. 2012. Evidence for a dual functional role of a conserved histidine in RNA-DNA heteroduplex cleavage by human RNase H1. FEBS J. 279:4492-4500.

Anzahaee, M.Y., Watts, J.K., Alla, N.R., Nicholson, A.W., and Damha, M.J. 2011 Energetically important C-H···F-C pseudohydrogen bonding in water: evidence and application to rational design of oligonucleotides with high binding affinity.  J. Am. Chem. Soc. 133:728-31.

Shi, Z., Nicholson, R.H. and Jaggi, R., and Nicholson, A.W. 2011. Characterization of Aquifex aeolicus ribonuclease III and the reactivity epitopes of its pre-ribosomal RNA substrates.  Nucleic Acids Res. 39:2756-2768. (Epub 2010 Dec 7)

Nathania, L. and Nicholson, A.W. 2010. Thermotoga maritima ribonuclease III. Characterization of thermostable biochemical behavior and analysis of conserved base-pairs that function as reactivity epitopes for the Thermotoga 23S rRNA precursor. Biochem. 49: 7164-7178.

Meng, W., Nicholson, R.H., Nathania, L., Pertzev, A. V. and Nicholson, A. W. 2008. New approaches to understanding double-stranded RNA processing by ribonuclease III.  Purification and assays of homodimeric and heterodimeric forms of RNase III from bacterial extremophiles and mesophiles. Methods Enzymol. 447, 119-129.

Meng, W. and Nicholson, A.W. 2008. Heterodimer-based analysis of subunit and domaincontributions to double-stranded RNA processing by Escherichia coli RNase III in vitro. Biochem. J. 410, 39-48.

Pertzev, A. and Nicholson. A. W.  2006. Characterization of RNA sequence determinants and antideterminants of processing reactivity for a minimal substrate of Escherichia coli ribonuclease III.  Nucleic Acids Res. 34, 3708-3721.

Sun, W., Pertzev, A. and Nicholson, A. W.  2005.  Catalytic mechanism of Escherichia coli ribonuclease III. Kinetic and inhibitor evidence for the involvement of two Mg2+ ions in phosphodiester hydrolysis.  Nucleic Acids Res. 33, 807-815.

Sun., W., Li, G., and Nicholson, A. W.  2004.  Mutational analysis of the nuclease domain of Escherichia coli ribonuclease III.  Identification of conserved acidic residues that are important for catalytic function in vitro.  Biochemistry 43, 13054-13062.

Zhang, Y., Calin-Jageman, I., Gurnon, J.R., Choi, T.J., Adams, B., Nicholson, A.W., and van Etten, J. L. 2003.  Characterization of a chlorella virus PBCV-1 encoded ribonuclease III.  Virology  317, 73-83.

Calin-Jageman, I. and Nicholson, A. W. 2003. Mutational analysis of an RNA internal loop as a reactivity epitope for Escherichia coli ribonuclease III substrates.  Biochemistry 42, 5025-5034.

Calin-Jageman, I. and Nicholson, A. W. 2003. RNA structure-dependent uncoupling of substrate binding and cleavage by Escherichia coli ribonuclease III.  Nucleic Acids Res. 31, 2381-2392.

Fortin, K. R., Nicholson, R.H. and Nicholson, A. W. 2002. Mouse ribonuclease III: cDNA structure, expression analysis, and chromosomal location. BMC Genomics 3, 26.

Nicholson, R. H. and Nicholson, A. W. 2002. Characterization and expression analysis of a mouse cDNA encoding Dicer, a ribonuclease III orthologue involved in RNA interference.  Mamm. Genome 13, 67-73.

Marchand, I., Nicholson, A. W. and Dreyfus, M. 2001.  Bacteriophage T7 protein kinase phosphorylates RNase E and stabilizes mRNAs synthesized by T7 RNA polymerase. Molecular Microbiology 42, 767-776.

Sun, W., Jun, E. and Nicholson, A. W. 2001. Intrinsic double-stranded RNA processing activity of Escherichia coli ribonuclease III lacking the double-stranded RNA-binding domain.  Biochemistry 40, 14976-14984.

Calin-Jageman, I., Amarasinghe, A. and Nicholson, A. W. 2001. Ethidium-dependent uncoupling of RNA binding and cleavage by Escherichia coli  ribonuclease III. Nucleic Acids Res. 29, 1915-1925.

Sun, W. and Nicholson, A. W. 2001. Mechanism of action of Escherichia coli ribonuclease III. Stringent chemical requirement for a glutamic acid side chain at position 117, and Manganese ion rescue of the Glu117Asp mutant.  Biochemistry 40, 5102-5110.

Marchand, I., Nicholson, A. W. and Dreyfus, M. 2001.  High-level autoenhanced expression of a single-copy gene in Escherichia coli. Overproduction of bacteriophage T7 protein kinase directed by T7 late genetic elements.   Gene 262, 231-238.

Nicholson, A.W. 1999. Structure, function and regulation of bacterial ribonucleases. FEMS Microbiol. Rev. 23, 371-390.

Zhang, K. and Nicholson, A.W. 1997. Regulation of ribonuclease III processing by double-helical sequence antideterminants. Proc. Natl. Acad. Sci. USA 94, 13437-13441.

Li, H. and Nicholson, A.W.  1996. Defining the enzyme binding domain of a ribonuclease III processing signal. Ethylation interference and hydroxyl radical footprinting using catalytically inactive RNase III mutants. EMBO J. 15, 101-113.

Nicholson, A.W. 1996.  “Structure, reactivity and biology of double-stranded RNA” Prog. Nucleic Acids Res. Mol. Biol. 52, 1-65.

Schweisguth, D.C., Chelladurai, B.S., Nicholson, A.W., and Moore, P.B. 1994. “Structural analysis of a ribonuclease III processing signal.” Nucleic Acids Res. 22, 604-612.

Robertson, E.S., Aggison, L.A. and Nicholson, A.W. 1994. “Elongation factor G and ribosomal protein S6 are phosphorylated in bacteriophage T7-infected Escherichia coli.”  Molecular Microbiol. 11, 1045-1057.

Chelladurai, B.S., Li, H., Zhang, K. and Nicholson, A.W. 1993. Mutational analysis of a ribonuclease III processing signal. Biochemistry 32, 7549-58.

Li, H., Chelladurai, B.S., Zhang, K. and Nicholson, A.W. 1993. “Ribonuclease III cleavage of a bacteriophage T7 processing signal.  Divalent cation specificity and specific anion effects.” Nucleic Acids Res. 21, 1919-25

Robertson, E.S. and Nicholson, A.W. 1992. Phosphorylation of Escherichia coli translation initiation factors by the bacteriophage T7 protein kinase. Biochemistry 31, 4822-4827.

Michalewicz, J. and Nicholson, A.W. 1992. “Molecular cloning and expression of the bacteriophage T7 0.7 (protein kinase) gene.” Virology 186, 452-462.

Nicholson, A.W. 1992. Accurate enzymatic cleavage in vitro of a 2′-deoxyribose-substituted ribonuclease III processing signal. Biochim. Biophys. Acta 1129, 318-322.

Chelladurai, B.S., Li, H. and Nicholson, A.W. 1991. A conserved sequence element in ribonuclease III processing signals is not required for accurate in vitro enzymatic cleavage. Nucleic Acids Res. 19, 1759-1766.

Michalewicz, J., Hsu, E., Larson, J. and Nicholson, A.W. 1991. Physical map and genetic early region of the T7-related coliphage BA14. Gene 98, 89-93.

Robertson, E.S. and Nicholson, A.W. 1990. Protein kinase of bacteriophage T7 induces the phosphorylation of only a small number of proteins in the infected cell. Virology 175, 525-534.

Nicholson, A.W., Niebling, K.R., McOsker, P.L. and Robertson, H.D. 1988. Accurate in vitro cleavage by RNase III of phosphorothioate-substituted RNA processing signals in bacteriophage T7 early mRNA.  Nucleic Acids Research 16, 1577-1591.

Larson, J.J., Nicholson, A.W. and Siegel, A. 1987. Field inversion of large DNA fragments using an inexpensive unit.  Biotechniques 5, 228-232.

Nicholson, A.W., Frankfort, H.M., Davis, N.G., Ferrari, S., Lamb, R.A. and Robertson, H.D.  1986.  Direct characterization of influenza viral NS1 mRNA and related sequences from infected HeLa cells and a cell-free transcription system. Biochim. Biophys. Acta 868, 153-163.

Olson, H.M., Nicholson, A.W., Cooperman, B.S. and Glitz, D.G.  1985.  Localization of sites of photoaffinity labeling of the large subunit of Escherichia coli ribosomes by an aryl azide derivative of puromycin.  J. Biol. Chem. 260: 10326-1033l.

Nicholson, A.W., Hall, C.C., Strycharz, W.A. and Cooperman, B.S.  1982.  Photoaffinity labeling of Escherichia coli ribosomes by an aryl azide analogue of puromycin.  I. Evidence for the functional site specificity of labeling.  Biochemistry 21: 3809-38l7.

Nicholson, A.W., Hall, C.C., Strycharz, W.A. and Cooperman, B.S.  1982.  “Photoaffinity Labeling of Escherichia coli ribosomes by an aryl azide analogue of puromycin.  II. On the identification of the major covalently labeled proteins and on the mechanism of photoincorporation.”  Biochemistry 21, 3797-3809.

Nicholson, A.W. and Cooperman, B.S.  1978.  Photoaffinity labeling of Escherichia coli ribosomes with an aryl azide analogue of puromycin.  FEBS Letters 90, 203-208.

Danforth, C., Nicholson, A.W., James, J.D. and Loudon, G.M. 1976. Steric acceleration of lactonization reactions: An analysis of `stereopopulation control’. J. Amer. Chem. Soc. 98, 4275-4281.