Publications

 

Link to bibliography- https://www.ncbi.nlm.nih.gov/myncbi/michael.harris.1/bibliography/public/


  • Harris ME, Huynh L, Chamberlain A. (2023). Surveying the substrate specificity landscape of bacterial ribonuclease P. submitted.


  • Yoon S, Ollie E, York DM, Piccirilli JA, Harris ME. (2023). Rapid kinetics of pistol ribozyme: Insight into limits to RNA catalysis. Biochemistry DOI: 10.1021/acs.biochem.3c00160



  • Huang T, Snell KC, Kalia N, Gardezi S, Guo L, Harris ME. (2023). Kinetic analysis of RNA cleavage by coronavirus Nsp15 endonuclease: Evidence for acid base catalysis and substrate dependent metal ion activation. J Biol Chem.  299(6) 104787  



  • Weissman B, Ekesan Ş, Lin HC, Gardezi S, Li NS, Giese TJ, McCarthy E, Harris ME, York DM, Piccirilli JA. (2023). Dissociative Transition State in Hepatitis Delta Virus Ribozyme Catalysis. J Am Chem Soc. 145(5):2830-2839.


  • Zhu J, Wang W, Zhao J, Huynh L, Taylor DM, and Harris ME. (2022). Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P. Nat Commun. 13(1):5120.


  • Pritzlaff A, Ferrier G, Mulry E, Jafar N, Harris ME, and Eddy M. (2022). Atomic-Scale View of Protein-PEG Interactions that Redirect the Thermal Unfolding Pathway of PEGylated Human Galectin-3. Angwant Chem Intl Ed. 61(40) e202203784.


  • Yoon S and Harris ME. (2021). Beyond the Plateau: pL Dependence of Proton Inventories as a Tool for Studying Ribozyme and Ribonuclease Catalysis. Biochemistry 60(37):2810-2823.


  • Misko TA, Liu YT, Harris ME, Oleinick NL, Pink J, Lee HY, Dealwis CG. (2019) Structure-guided design of anti-cancer ribonucleotide reductase inhibitors. J Enzyme Inhib Med Chem 34(1):438-450.


  • Bevilacqua PC, Harris ME, Piccirilli JA, Gaines C, Ganguly A, Kostenbader K, Ekesan Ş, York DM. (2019). An Ontology for Facilitating Discussion of Catalytic Strategies of RNA-Cleaving Enzymes. ACS Chem Biol 14(6):1068-1076.


  • Zhao J, Harris ME. (2019). Distributive enzyme binding controlled by local RNA context results in 3′ to 5′ directional processing of dicistronic tRNA precursors by Escherichia coli ribonuclease P. Nucleic Acids Res 47(3):1451-1467.


Harris ME. (2020). “RNA-Protein Interactions” in Nucleic Acids in Chemical Biology, 4th Blackburn, et al. Eds.

Jun Lu J, Koo SC, Weissman BP, Harris ME, Li N-S and Piccirilli JA. (2018). Evidence that nucleophile deprotonation exceeds bond formation in the HDV ribozyme transition state. Biochemistry. 57(25):3465-3472.

Huff S, Ahmad MF, Yang M, Agrawal P, Pink J, Harris ME, Dealwis C, Viswanathan R (2018). Structure-Guided Synthesis and Mechanistic Studies Reveal Sweetspots on Naphthyl Salicyl Hydrazone Scaffold as Non-Nucleosidic Competitive, Reversible Inhibitors of Human Ribonucleotide Reductase. J Med Chem. 61(3):666-680.

Knappenberger AJ, Grandhi S, Sheth R, Ahmad MD, Viswanathan R, and Harris ME (2017). Phylogenetic sequence analysis and functional studies reveal compensatory amino acid substitutions in loop 2 of human ribonucleotide reductase. J Biol Chem. 292(40):16463-16476.

Harris ME, York DM, Piccirilli JA and Anderson VE. (2017). Kinetic isotope effect analysis of RNA 2’-O-transphosphorylation. Methods Enzymol. Vol 596, 433-457.

Niland CN, Anderson DR, Jankowsky E, and Harris ME. (2017). The contribution of the C5 protein subunit of Escherichia coli ribonuclease P to specificity for precursor tRNA is modulated by proximal 5’ leader sequences. RNA. 23(10):1502-1511.

Ahmad MF, Alam I, Huff SE, Pink J, Flanagan SA, Shewach D, Misko TA, Oleinick NL, Harte WE, Viswanathan R, Harris ME, and Dealwis CG. (2017). Potent competitive inhibition of human ribonucleotide reductase by a non-nucleoside small molecule. Proc Natl Acad Sci 114(31):8241-8246.

Jankowsky E and Harris ME. (2017). Mapping specificity landscapes of RNA-protein interactions by high throughput sequencing. Methods. S1046-2023(17)30099-3.

Jain N, Lin H-C, Harris ME and Tolbert B. (2017). Rules of RNA specificity of hnRNP A1 revealed by global and quantitative analysis of its affinity distribution. Proc Natl Acad Sci. 114(9):2206-2211.

Lin H-C, Zhao J, Niland CN, Tran B, Jankowsky E and Harris ME. (2016). Comprehensive analysis of the C5 protein specificity landscape reveals RNA structure and sequence preferences that direct ribonuclease P substrate specificity. Cell Chem Biol. 23(10):1271-1281.

Knappenberger AJ, Ahmad FM, Dealwis CG and Harris ME. (2016). Nucleotide effector analogs allosterically regulate human ribonucleotide reductase and identify chemical determinants of substrate specificity. Biochemistry. 55(41):5884–5896.

Vijayaraghavan J, Kramp K, Harris ME and van den Akker. (2016). Inhibition of activated soluble guanylyl cyclase by small molecules targeted to the catalytic domain. FEBS Lett. 590(20):3669-3680.

Niland CN, Jankowsky E and Harris ME. (2016). Optimization of High Throughput Sequencing Kinetics (HTS-Kin) for the simultaneous determination of enzymatic rate constants for thousands of RNA substrates. (2016). Anal Biochem. 510:1-10.

Niland CN, Zhao J, Lin H-C, Jankowsky E and Harris ME. (2016). The global specificity landscape for ribonuclease P processing of pre-tRNA 5’ leader sequences. ACS Chem Biol. 11(8):2285-92.

Mullins M, Malligarjunan R, Hernandez-Sanchez W, de la Fuente M, Biendarra S, Harris ME and Taylor, D. (2016). POT1-TPP1 binding to telomere DNA discriminates between G-quadruplex topologies. J Molec Biol. 428(13):2695-708.

Misko TA, Wijerathna SR, Radivoyevitch TJ, Berdis AJ, Ahmad MF, Harris ME and Dealwis CG. (2016). Inhibition of yeast ribonucleotide reductase by Sml1 depends on the allosteric state of the enzyme. FEBS Lett. 590(12):1704-12.

Zhang S, Gu H, Chen H, Strong E, Ollie EW, Kellerman D, Liang D, Miyagi M, Anderson VE, Piccirilli JA, York DM and Harris ME. (2016). Isotope effect analyses provide evidence for an altered transition state for RNA 2’-O-transphosphorylation catalyzed by Zn2+. Chem Comm. 52(24):4462-5.

Lee T-S, Radak BK, Harris ME and York DM. (2016). A two metal ion conformational switch pathway for HDV ribozyme activation. ACS Catalysis. 126, 1843-1853.

Harris ME. (2016). Theme and variation in 5’-tRNA processing endonucleases: Comparative analysis of ribonucleoprotein versus protein versions of ribonuclease P. J Molec Biol. 428(1):5-9.

Ahmad M, Huff S, Pink J, Alam I, Zhang A, Perry K, Harris ME, Misko T, Porwal SK, Oleinick NL, Viswanathan R, Miyagi M, Dealwis CG. (2015). Identification of non-nucleoside human ribonucleotide reductase inhibitors. J Med Chem. 58(24):9498-509.

Jankowsky E and Harris ME. (2015). Specificity and non-specificity in RNA-protein interactions. Nat Rev Molec Cell Biol. 16(9):533-44.

Weissman BP, Li N-S, York DM, Harris ME, and Piccirilli JA. (2015). Heavy atom labeled nucleotides for measurement of kinetic isotope effects. Biochim Biophys Acta 1854(11):1737-45.

Harris ME, Piccirilli JA and York DM. (2015). Integration of kinetic isotope effects in the analysis of ribonuclease mechanism. Biochim Biophys Acta 1854(11):1801-8.

Chen H, Piccirilli JA, Harris ME and York DM. (2015). Effect of Zn2+ binding and enzyme active site on the transition state for RNA 2′-O-transphosphorylation interpreted through kinetic isotope effects Biochim Biophys Acta 1854(11):1795-800.

Radak BK, Lee TS, Harris ME, York DM. (2015). Assessment of metal-assisted nucleophile activation in the hepatitis delta virus ribozyme from molecular simulation and 3D-RISM. RNA. (9):1566-1577.

Koo S, Lu J, Li, N-S, Leung E, Das S, Harris ME, and Piccirilli JA. (2015). Transition state features in the Hepatitis Delta Virus (HDV) ribozyme reaction revealed by atomic perturbations. J Am Chem Soc. 137(28):8973-82.

Mojica MF, Mahler GS, Bethel CR, Taracila MA, Kosmopoulou M, Papp-Wallace KM, Llarrull LI, Marshall SH, Wallace CJ, Villegas MV, Harris ME, Vila AJ, Spencer J, Bonomo RA. (2015). Exploring the role of residue 228 for substrate and inhibitor recognition by VIM metallo-β-lactamases. Biochemistry. 54 (20): 3183-96.

Kellerman DL, Simmons KS, Pedraza M, Piccirilli JA, York DM and Harris ME. (2015). Determination of HDV ribozyme N(-1) nucleobase and functional group modification using internal competition kinetics. Anal Biochem. 483: 12-20.

Dissanayake T, Swails J, Harris ME, Roitberg A, York DM. (2015). Interpretation of pH-activity profiles for acid-base catalysis from molecular simulations. Biochemistry. 54(6):1307-13.

Porwal SK, Furia E, Harris ME, Viswanathan R, and Devireddy L. (2015). Synthetic, potentiometric and spectroscopic studies of chelation between Fe(III) and 2,5-DHBA supports salicylate-mode of siderophore binding interactions. J Inorg Biochem. 145C:1-10.

Kellerman DL, York DM, Piccirilli JA and Harris ME. (2014). Altered (transition) states: Mechanisms and transition states of solution and enzyme catalyzed RNA 2’-O-transphosphorylation. Curr Opin Chem Biol. 21:96–102.

Lin H-C, Yandek LY, Germeni I and Harris ME. (2014). Determination of relative rate constants for in vitro RNA processing reactions by internal competition. Anal. Biochem. 467(2): 54-61.

Chen H, Giese TJ, Huang M, Wong K-Y, Harris ME and York DM. (2014). Mechanistic insights into RNA transphosphorylation from kinetic isotope effects and linear free energy relationships of model reactions. Chem Eur J. 20(44):14336-43.

Guenther U-P, Yandek LY, Niland CN, Campbell FE, Anderson D, Anderson VE, Harris ME and Jankowsky E. (2013). Hidden specificity in an apparently non-specific RNA-binding protein. Nature 502(7471):385-8.

Gu H, Zhang S, Wong K-Y, Radak BK, Dissanayake T, Kellerman D, Dai Q, Miyagi M, Anderson VE, York DM, Piccirilli JA and Harris ME. (2013). Experimental and computational analysis of the transition state for ribonuclease A catalyzed RNA 2’-O-transphosphorylaiton. Proc Natl Acad Sci USA 110(32):13002-13007.

Corriveau M, Mullins MR, Baus D, Harris ME and Taylor DJ (2013). Coordinated interactions of multiple POT1-TPP1 proteins with telomere DNA. J Biol Chem. 288(23):16361-70.

Yandek LE, Lin H-C and Harris ME. (2013). Alternative substrate kinetics of Escherichia coli ribonuclease P: Determination of relative rate constants by internal competition. J Biol Chem. 288(12):8342-54

Radak BK, Harris ME and York DM. (2013). Molecular simulations of RNA 2′-O-transesterification reaction models in solution. J Phys Chem. 117(1):94-103.

Harris ME. (2013). “Probing RNA solution structure by photocrosslinking: Incorporation of photoreactive groups at RNA termini and determination of crosslinked sites by primer extension”. in Handbook of RNA Biochemistry, 3rd ed. Hartmann RK, Bindereif A, Schön A, and Westhof E, eds. Wiley-VCH. ISBN: 978-3527327645

Harris ME. (2013). “Identification and Characterization of metal ion coordination interactions with RNA by quantitative analysis of thiophilic metal ion rescue of site-specific phosphorothioate modifications”. in Handbook of RNA Biochemistry, 3rd ed. Hartmann RK, Bindereif A, Schön A, and Westhof E, eds. Wiley-VCH. ISBN: 978-3527327645

Wong K-U, Gu H, Zhang S, Piccirilli JA, Harris ME and York D (2012). Characterization of the reaction path and transition states for RNA transphosphorylation from theory and experiment. Angew Chem Intl Ed. 51(3):823.

Papp-Wallace K, Senkfor B, Gatta J, Chai W, Taracila M, Shanmugasundaram M, Han S, Zaniewski R, Lacey B, Tomaras A, Skalweit M, Harris ME, Rice L,  Buynak J and Bonomo RA. (2012). Early insights into affinity of different β-lactam antibiotics and β-lactamase inhibitors against soluble forms of Acinetobacter spp. PBP1a and PBP3. Antimicrob Agents Chemother. 56(11):5687-92.

Levitt PS, Papp-Wallace KM, Taracila MA, Hujer AM, Winkler ML, Smith KM, Xu Y, Harris ME and Bonomo RA. (2012). Exploring the role of a conserved class a residue in the -loop of KPC-2 β-lactamase: A mechanism for ceftazidime hydrolysis. J Biol Chem. 287(38):31783-93.

Lee TS, Giambaşu G, Harris ME and York DM. (2011). Characterization of the structure and dynamics of the HDV ribozyme at different stages along the reaction path. J Phys Chem. 2(20):2538-2543.

Christian EL, Anderson VE, Carey PC and Harris ME (2011). Deconvolution of electrostatic, H-bonding, and inner-sphere coordination interactions and dimethyl phosphate in solution by Raman spectroscopy. J Inorg Biochem. 105(4):538-47.

Harris ME, Dai Q, Gu H, Kellerman DE, Piccirilli JA and Anderson VE (2010). Kinetic isotope effects for RNA cleavage by 2’-O-transphosphorylation: Nucleophilic activation by specific base. J Am Chem Soc. 132(33):11613-21.

Christian EL, Anderson VE, Carey PR and Harris ME. (2010). A quantitative Raman spectroscopic signal for metal-phosphodiester interactions in solution. Biochemistry. 49(13):2869-79.

Koutmou KS, Zahler NH, Kurz JC, Campbell FE, Harris ME and Fierke CA. (2010). Protein-precursor tRNA contact leads to sequence-specific recognition of 5′ leaders by bacterial ribonuclease P. J Mol Biol. 12;396(1):195-208.

Sun L, Campbell FE, Yandek LE and Harris ME. (2010). Binding of the C5 protein to P RNA enhances the rate constant for catalysis for P RNA processing of pre-tRNAs lacking a consensus G(1)-C(72) base pair. J Mol Biol. 395(5):1019-37.

Harris ME and Yandek LE. (2010). “Challenges in substrate recognition by RNase P: Facing up to the biological context” in Protein Reviews Volume 10: Ribonuclease P. pp 135-152. Altman S and Lui F, eds. Springer New York.  ISBN 978-1-4419-1141-4

Schroeder LA, Gries TJ, Saecker RM, Record MT Jr, Harris ME and DeHaseth PL. (2009). Evidence for a tyrosine-adenine stacking interaction and for a short-lived open intermediate subsequent to initial binding of Escherichia coli RNA polymerase to promoter DNA. J Mol Biol. 385(2):339-49.

Harris ME and Christian EL. (2009). “Understanding the role of meal ions in RNA folding and function: Lessons from RNase P, a ribonucleoprotein enzyme” in Non-Protein Coding RNAs. pp183-214. Walter NG, Woodson SA and Batey RT, eds. Springer-Verlag Berlin Heidelberg ISBN 0932-2353

Harris ME. (2009). “Catalytic Modes of Biological Ribozymes” Wiley Encyclopedia of Chemical Biology. Begley T. ed. Wiley. ISBN: 978-0-471-75477-0.

Christian EL and Harris ME. (2009). “RNA crosslinking methods” in Biophysical, Chemical, and Functional Probes of RNA Structure, Interactions and Folding: Part A Meth Enzymol 468:127-146. Herschlag, D. ed. Elsevier. ISBN: 978-0-12-374399-2

Harris ME and Cassano AG. (2008). Experimental analyses of the chemical dynamics of ribozyme catalysis. Curr Opin Chem Biol. 12(6):626-39.

Dai Q, Frederiksen JK, Anderson VE, Harris ME and Piccirilli JA. (2008). Efficient synthesis of [2′-18O]uridine and its incorporation into oligonucleotides: A new tool for mechanistic study of nucleotidyl transfer reactions by isotope effect analysis. J Org Chem. 73(1):309-11.

Zahler N and Harris ME. (2008). “Co- and Post-Transcriptional Incorporation of Specific Modifications Including Photoreactive Groups into RNA Molecules” in Handbook of RNA Biochemistry, 2nd ed. pp. 75-85. Hartmann RK, Bindereif A, Schön A, and Westhof E, eds. Wiley. ISBN: 9783527308262 

Harris ME and Christian EL. (2008). “Probing RNA Structure by Photoaffinity Crosslinking with 4-Thiouridine and 6-Thioguanosine” in Handbook of RNA Biochemistry, 2nd ed. pp 374-384. Hartmann RK, Bindereif A, Schön A, and Westhof E, eds. Wiley. ISBN: 9783527308262  

Cassano AG, Wang B, Anderson DR, Previs S, Harris ME and Anderson VE. (2007). Inaccuracies in selected ion monitoring determination of isotope ratios obviated by profile acquisition: nucleotide 18O/16O measurements. Anal Biochem. 367(1):28-39.

Sun L and Harris ME. (2007). Binding of C5 protein to the P RNA ribozyme increases catalytic rate by influencing active site metal ion affinity.  RNA. 34:1-11.

Anderson VE, Ruszczysky M and Harris ME. (2006). Nucleophilic activation in enzyme catalysis.  Chem Rev. 106(8):3236-51.

Sun L, Campbell FE and Harris ME. (2006). Substrate specific effects of C5 protein lead to uniformity in binding and catalysis by RNase P. EMBO J. 25(17):3998-4007.

Christian EL, Johnson K, Perrera N and Harris ME. (2006). The P4 metal binding site in RNase P RNA affects active site metal affinity through substrate positioning. RNA. 12(8):1463-7.

Guo X, Campbell FE, Christian EL, Anderson VE and Harris ME. (2006) RNA-dependent folding and stabilization of C5 protein during assembly of the E. coli RNase P holoenzyme. J Molec Biol. 360(1):190-203

Anderson VE, Harris ME and Cassano AG. (2006) “Nucleophile Isotope Effects” in Isotope Effects in Chemistry and Biology. CRC Press. Kohen A, Limbach H-H (eds)

Zahler NH, Sun L, Christian, EL and Harris ME (2005). The pre-tRNA nucleotide base and 2′-hydroxyl at N(-1) contribute to fidelity in tRNA processing by RNase P. J Molec Biol 345(5):969-85.

Cassano AG, Anderson, VE and Harris ME. (2004). Transition states of phopshodiester bond hydrolysis: Information from heavy atom isotope effects.  Biopolymers. 73, 110-129.

Cassano AG, Anderson VE and Harris ME. (2004). Analysis of solvent nucleophile isotope effects: Evidence for concerted mechanisms and nucleophilic activation by metal ion coordination in non-enzymatic and ribozyme catalyzed phosphodiester hydrolysis. Biochemistry. 43(32):10547-59.

Harris ME and Christian EL. (2004). “Probing RNA Structure by Photoaffinity Crosslinking With 4-Thiourine and 6-Thioguanosine” in Handbook of RNA Biochemistry, Wiley. Hartmann, Binderief, Shon and Westhof, eds.

Zahler, NH and Harris ME. (2004). “Site-Specific Modification of RNA” in Handbook of RNA Biochemistry, Wiley. Hartmann, Binderief, Shon and Westhof, eds.

Harris ME and Christian EL. (2003). Recent insights into the structure and function of the ribonucleoprotein enzyme RNase P. Curr Op Struct Biol. 13, 325-333.

Zahler NH, Christian EL and Harris ME. (2003). Recognition of the 5’ leader of pre-tRNA substrates by the active site of ribonuclease P. RNA. 9, 734-745.

Christian EL, Kaye NM, Zahler, NH and Harris ME. (2002). Analysis of substrate recognition by the ribonucleoprotein endonuclease RNase P. Methods. 28, 307-322.

Kaye NM, Zahler NH, Christian EL and Harris ME. (2002). Conserved helix structure contributes to functional metal ion interactions in the catalytic domain of ribonuclease P RNA. J Molec Biol. 324(3):429-442.

Cassano AG, Anderson VE and Harris ME. (2002). Evidence for direct attack by hydroxide in phosphodiester hydrolysis. J Am Chem Soc. 124(37):10964-5.

Christian EL, Kaye NM and Harris ME. (2002). Evidence for a polynuclear metal ion binding site in the catalytic domain of ribonuclease P RNA. EMBO J. 21, 2253-2262.

Kaye NM, Christian EL and Harris ME. (2002). NAIM and site-specific functional group modification analysis of the RNase P ribozyme: Magnesium dependent structure in the P1-P4 multi-helix junction contributes to catalysis. Biochemistry. 41, 4533-4545.

Campbell FE, Cassano AG, Anderson V and Harris ME. (2002). Pre-steady state and stopped flow fluorescence analysis of E. coli RNase III: Insights into mechanism and conformational changes associated with binding and catalysis. J Molec Biol. 317, 21-40.

Christian EL, Kaye NM and Harris ME. (2000). Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme. RNA. 6, 511-519.

Harris ME and Christian EL. (1999). Use of circularly permutation and end-modification to position photoaffinity probes for analysis of RNA structure. Methods. 18, 51-59.

Christian EL and Harris ME. (1999) The track of the pre-tRNA 5’ leader sequence in the ribonuclease P ribozyme-substrate complex. Biochemistry. 38, 12629-12638.

Siew D, Zahler N, Cassano A, Strobel S and Harris ME. (1999). Identification of individual adenosine chemical groups involved in substrate recognition by the ribonuclase P ribozyme. Biochemistry. 38, 1873-1883.

Christian EL, McPheeters DS and Harris ME. (1998). Identification of individual nucleotides in the bacterial ribonuclease P ribozyme adjacent to the pre-tRNA cleavage site by short-range photocrosslinking. Biochemistry. 37, 17618-17628.

Chen J-L, Nolan JM, Harris ME and Pace NR. (1998). Comparative photocross-linking analysis of the tertiary structures of Escherichia coli and Bacillis subtilis RNase P RNAs. EMBO J. 17, 1515-1525.

Harris ME, Kavansev A, Chen J-L and Pace NR (1997). Analysis of the tertiary structure of the ribonuclease P ribozyme-substrate complex by site-specific photoaffinity crosslinking. RNA. 3, 561-576.

Harris ME and Pace NR. (1996). Analysis of the tertiary structure of bacterial RNase P RNA. Molec Biol Reports. 22,115-123.

Piller KJ, Decker CJ, Rusche L, Harris ME, Hajduk SL and Sollner-Webb B. (1995). Editing domains of Trypanosoma brucei mitochondrial RNAs identified by secondary structure. Molec Cell Biol. 15, 2916-2924.

Harris ME and Pace NR. (1995). Identification of phosphates involved in catalysis by the ribozyme RNase P RNA. RNA. 1, 210-218.

Frank D, Harris ME and Pace NR. (1994). Rational design of self-cleaving pre-tRNA ribonuclease P RNA conjugates. Biochemistry. 33, 10800-10808.

Harris ME, Nolan JM, Malhotra A, Brown JW, Harvey SC and Pace NR. (1994). Use of photoaffinity crosslinking and molecular modeling to analyze the global architecture of ribonuclease P RNA. EMBO J. 13, 3953-3960.

Hajduk SL, Harris ME and Pollard VW. (1993). RNA editing in trypanosome mitochondria. FASEB J. 7, 54-63.

Hajduk SL, Adler B, Bertrand K, Hager K, Harris ME, Moore D, Priest J and Wood Z. (1992). Molecular biology of african trypanosomes: Development of new strategies to combat an old disease. Am. J. Med. Sci. 303, 258-270.

Pollard VW, Harris ME and Hajduk SL. (1992). Native RNA editing complexes from trypanosome mitochondria. EMBO J. 7, 4429-4438.

Michelotti EF, Harris ME, Adler BK, Torri A and Hajduk SL. (1992). Trypanosoma brucei mitochondrial ribosomal RNA synthesis, processing and developmentally regulated expression. Molec. Biochem. Parasitol. 54, 31-42.

Gabb HA, Harris ME, Pandey NB, Marzluff WF and Harvey SC. (1992). Molecular modeling to predict the structural and biological effects of mutations in a highly conserved histone mRNA loop sequence. J. Biomolec. Struc. and Dynam. 9, 1119-1130.

Harris ME and Hajduk SL. (1992). In vitro formation of gRNA/mRNA chimeras from synthetic substrate RNAs. Cell. 68, 1091-1099.

Harris ME, Decker C, Sollner-Webb B and Hajduk SL. (1992). Specific cleavage of pre-edited RNAs in extracts from trypanosome mitochondria. Molec. Cell. Biol. 6, 2591-2598.

Adler B, Harris ME, Bertrand KI and Hajduk SL. (1991). Modification of Trypanosoma brucei mitochondrial rRNA by post-transcriptional 3′ polyuridine tail formation. Molec. Cell. Biol. 12, 5878-5884.

Harris ME, Böhni R, Schneiderman MH, Ramamurthy L, Schümperli D and Marzluff WF. (1991). Regulation of histone mRNA in the unperturbed cell cycle: evidence suggesting two post-transcriptional steps. Molec. Cell. Biol. 5, 2416-2424.

Harris ME, Moore DR and Hajduk SL. (1990). Addition of uridines to edited RNAs in trypanosome mitochondria occurs independently of transcription. J. Biol. Chem. 265, 11368-11376.