Hans-Joachim Wieden



  • Roberts, L. and Wieden, H.-J.* (2018) Viruses, IRESs, and A Universal Translation Initiation Mechanism. Biotechnol. Genet. Eng. Rev. 34(1): 60-75. DOI: 10.1080/02648725.2018.1471567 (IF: 0.929)
  • Tanzawa, T., Kato, K., Girodat, D., Kumakura, Y., Wieden, H.-J., Uchiumi, T., Tanaka, I., and Yao, M.* (2018) The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion. Nucl. Acids Res.  46(6): 3232-3244. DOI: 10.1093/nar/gky115 (IF: 10.162)
  • Tillault, A.-S., Schultz, S.K., Wieden, H.-J., and Kothe, U.* (2018) Molecular determinants for 23S rRNA recognition and modification by the E. coli pseudouridine synthase RluE. J. Mol. Biol. 430(9): 1284-1294. DOI: 10.1016/j.jmb.2018.03.011 (IF: 4.632)


  • Hudson, A.J., Glaister, G.D., and Wieden, H.-J.* (2017) The Emergency Medical Service Microbiome. Appl. Environ. Microbiol. 84(5): e02098-17. DOI: 10.1128/AEM.02098-17 (IF: 3.807)
  • Fernandes, D.D., Bamrah, J., Kailasam, S., Gomes, G.-N.W., Li, Yi, Wieden, H.-J., and Gradinaru, C.C.* (2017) Characterization of Fluorescein Arsenical Hairpin (FlAsH) as a Probe for Single-Molecule Fluorescence Spectroscopy. Sci. Rep. 7: 13063. (IF: 4.847)
  • Smith, D.D., Girodat, D., Wieden, H.-J.* and Selinger, L.B.* (2017) Streamlined purification of fluorescently labeled Escherichia coli phosphate-binding protein (PhoS) suitable for rapid-kinetics applications. Anal. Biochem. 537: 106-113.. DOI: 10.1016/j.ab.2017.09.012 (IF: 2.219)
  • Dubé, S., Orr, D., Dempsey, B., and Wieden, H.-J.* (2017) A Synthetic Biology Approach to Integrative High School STEM Training. Nature Biotechnol. 35: 591-595. DOI: 10.1038/nbt.3896. (IF: 43.113)
  • Gzyl, K.E. and Wieden, H.-J.* (2017) Tetracycline Does Not Directly Inhibit the Function of Bacterial Elongation Factor Tu. PLoS ONE 12(5): e0178523. DOI: 10.1371/journal.pone.0178523. (IF: 3.057)
  • Heller, J.L.E., Kamalampeta, R., and Wieden, H.-J.* (2017) Taking a step back from back-translocation: An integrative view of LepA/EF4’s cellular function. Mol. Cell. Biol. 37(12): 100653-16. DOI: 10.1128/MCB.00653-16. (IF: 4.427)
  • Vigar, J., and Wieden, H.-J.* (2017) Engineering bacterial translation initiation - Do we have all the tools we need? Biochim. Biophys. Acta. In Press. DOI: 10.1016/j.bbagen.2017.03.008 (IF: 5.083)
  • Chao, Y., Li, L., Girodat, D., Förstner, K.U., Said, N., Corcoran, C., Śmiga, M., Papenfort, K., Reinhardt, R., Wieden, H.-J., Luisi, B., and Vogel, J.* (2017) A global in vivo cleavage map reveals a central role for RNase E in small RNA biogenesis. Mol. Cell. 65(1): 39-51. DOI: 10.1016/j.molcel.2016.11.002 (IF: 13.958)


  • De Laurentiis, E.I., Mercier, E., and Wieden, H.-J. (2016) The C-terminal Helix of Pseudomonas aeruginosa Elongation Factor Ts Tunes EF-Tu Dynamics to Modulate Nucleotide Exchange. J. Biol. Chem. 291: 23136-48. DOI: 10.1074/jbc.M116.740381 (IF: 4.258)
  • De Laurentiis, E.I., Girodat, D., Mercier, E., Wieden, H.-J. (2016) Using Rapid Kinetics and Molecular Dynamics Simulations to Study Biomolecular Information Processing and Design. Biomath Communications 3. DOI: 10.11145/bmc.2016.04.167 (IF:NA)
  • Beal, J.*, Haddock-Angelli, T., Gershater, M., de Mora, K., Lizarazo, M., Hollenhorst, J., Rettberg, R., iGEM Interlab Study Contributors. (2016) Reproducibility of Fluorescent Expression from Engineered Biological Constructs in E. coli. PLoS One 11(6): e0157255. DOI: 10.1371/journal.pone.0150182 (IF: 3.23)
  • Thakor, N., Smith, M.D., Roberts, L. Patel, H., Wieden, H.-J., Cate, J.C.D., and Holcik, M. (2016) Cellular mRNA recruits the ribosome via eIF3-PABP bridge to initiate internal translation. RNA Biol. DOI: 10.1080/15476286.2015.1137419 (IF: 4.97)
  • Coatham, M.L., Brandon, H.E., Fischer, J.J., Schummer, T., and Wieden, H.-J. (2016) The conserved GTPase HflX is a ribosome splitting factor that binds to the E-site of the bacterial ribosome. Nucl. Acids Res. 44(4): 1952-61. DOI: 10.1093/nar/gkv1524 (IF: 9.11)


  • Brandon, H.E., Friedt, J.R., Glaister, G.D., Kharey, S.K., Smith, D.D., Stinson Z.K., and Wieden, H.-J. (2015) A New Part Class Utilizing Programmed Ribosomal Frameshifts. Translation 3: e1112458. DOI: 10.1080/21690731.2015.1112458 (IF:NA)
  • Rosler, K.S., Mercier, E., Andrews, I.C., and Wieden, H.-J., (2015) Histidine 114 is critical for ATP hydrolysis by the universally conserved ATPase YchF. J. Biol. Chem. 290: 18650-61. DOI: 10.1074/jbc.M114.598227 (IF: 4.60)
  • Tillault, A.S., Fourmann, J.B., Loegler, C., Wieden, H.-J., Kothe, U., and Charpentier, B., (2015) Contribution of two conserved histidines to the dual activity of archaeal RNA guide-dependent and -independent pseudouridine synthase Cbf5. RNA 21: 1233-9. DOI: 10.1261/rna.051425.115 (IF: 4.622)
  • De Laurentiis, E.I., and Wieden, H.-J. (2015) Identification of two structural elements important for ribosome stimulated GTPase activity of Elongation Factor 4 (EF4/LepA). Sci. Rep. 5: 8573. DOI: 10.1038/srep08573 (IF: 5.58) 
  • Mercier, E., Girodat, D., and Wieden, H.-J. (2015) A conserved P-loop anchor limits the structural dynamics that mediate nucleotide dissociation in EF-Tu. Sci. Rep. 8:7677. DOI: 10.1038/srep07677 (IF: 5.228)


  • Boël, G., Smith, P.C., Ning, W., Englander, M.T., Chen, B., Hashem, Y., Testa, A.J., Fischer, J.J., Wieden, H.-J., Frank, J., Gonzalez, R.L. Jr., Hunt, J.F. (2014) The ABC-F protein EttA gates ribosome entry into the translation elongation cycle. Nat. Struct. Mol. Biol. 21: 143-51. DOI: 10.1038/nsmb.2740 (IF: 11.633)
  • Friedt, J., Leavens, F.M., Mercier, E., Wieden, H.-J., Kothe, U. (2014) An arginine-aspartate network in the active site of bacterial TruB is critical for catalyzing pseudouridine formation. Nucleic Acids Res. 42: 3857-70. DOI: 10.1093/nar/gkt1331 (IF: 8.808)


  • Chen, X.L., Serrano, D., Mayhue, M., Wieden, H.-J., Stankova, J., Boulay, G., Ilangumaran, S., Ramanathan, S. (2013) GTPase of the immune-associated nucleotide-binding protein 5 (GIMAP5) regulates calcium influx in T-lymphocytes by promoting mitochondrial calcium accumulation. Biochem J. 449(2): 353-64. DOI: 10.1042/BJ20120516 (IF: 4.779)


  • Becker, M., Gzyl, K., Altamirano A.M., Vuong, A., Urban, K., Wieden, H.-J. (2012) The 70S ribosome modulates the ATPase activity of Escherichia coli YchF. RNA Biol9: 1288-1301. DOI: 10.4161/rna.22131 (IF: 5.377)
  • Fischer, J.J., Coatham, M.L., Eagle Bear, S., Brandon, H.E., De Laurentiis, E.I., Shields, M.J., Wieden, H.-J. (2012) The ribosome modulates the structural dynamics of the conserved GTPase HflX and triggers tight nucleotide binding. Biochimie 94(8): 1647-59. DOI: 10.1016/j.biochi.2012.04.016 (IF: 3.123)
  • Gruninger R.J., Dobing, S., Smith, A.D., Bruder LM, Selinger, L.B., Wieden, H.-J., Mosimann, S.C. (2012) Substrate binding in protein tyrosine phosphatase-like inositol polyphosphatases. J. Biol. Chem. 287: 9722-30. DOI: 10.1074/jbc.M111.309872 (IF: 4.6)


  • Delaurentiis, E.I., Mo, F., and Wieden, H.-J. (2011) Construction of a fully active Cys-less Elongation Factor Tu: Functional role of the conserved Cysteine 81. Biochim. Biophys. Acta. 1814: 684-92. DOI: 10.1016/j.bbapap.2011.02.007 (IF: 3.191)


  • Wieden, H.-J., Mercier, E., Gray, J., Steed, B., Yawney, D. (2010) A combined molecular dynamics and rapid kinetics approach to identify conserved 3 dimensional communication networks in Elongation Factor Tu. Biophys J99: 3735-43. DOI: 10.1016/j.bpj.2010.10.013 (IF: 3.832)