Professor Dr. Dagmar Klostermeier

• 2025
• 2023
• 2022
• 2021
• 2020
• 2019
• 2018
• 2017
• 2016
• 2015
• 2014
• 2013
• 2012
• 2011
• 2010
• 2009
• 2008
• 2007
• 2006
• 2005
• 2004
• 2002
• 2001
• 2000
• 1999
• 1998
• 1997

2025

• Donsbach, P., Kwas, C., Steimer, L., Samatanga, B., Andreou, A. Z. und Klostermeier, D., 2025. Inter-domain communication in the dimeric DEAD-box helicase Hera from T. thermophilus and implications for the mechanism of RNA unwinding. Nucleic Acids Research. 53(4), S. gkaf080. ISSN 0305-1048. doi: 10.1093/nar/gkaf080.
• Willing, F., Mhaindarkar, V. P., Hirsch, J., Lanz, M. A., Mitton-Fry, M. J., Gubaev, A. und Klostermeier, D., 2025. Different propensities for gate opening in gyrases and topoisomerase IV. Nucleic Acids Research. 53(8), S. gkaf330. ISSN 0305-1048. doi: 10.1093/nar/gkaf330.

2023

• Krause L., Chakraborty A., Andreou, A. und Klostermeier, D., 2023. Linking translation factor conformational dynamics with translation efficiencies and gene expression. Biophysical Journal. 121(3), S. 338a–339a. ISSN 0006-3495.
• Mhaindarkar, V., Rasche, R., Kümmel, D., Rudolph, M. und Klostermeier, D., 2023. Structure of reverse gyrase with a minimal latch that supports ATP-dependent positive supercoiling without specific interactions with the topoisomerase domain. Acta Crystallographica Section D: Structural Biology. 79(6). ISSN 0907-4449. doi: 10.1107/S2059798323002565.

2022

• Klostermeier, D., 2022. Analysis of the conformational space and dynamics of RNA helicases by single-molecule FRET in solution and on surfaces. Methods in Enzymology. 673, S. 251–310. ISSN 0076-6879. doi: 10.1016/bs.mie.2022.03.043.
• Krause, L., Willing, F., Andreou, A. und Klostermeier, D., 2022. The domains of yeast eIF4G, eIF4E and the cap fine-tune eIF4A activities through an intricate network of stimulatory and inhibitory effects. Nucleic Acids Research. 50(11), S. 6497–6510. ISSN 0305-1048. doi: 10.1093/nar/gkac437.
• Chakraborty, A., Krause, L. und Klostermeier, D., 2022. Determination of rate constants for conformational changes of RNA helicases by single-molecule FRET TIRF microscopy. Methods. 204, S. 428–441. ISSN 1046-2023. doi: 10.1016/j.ymeth.2022.03.004.

2021

• Hirsch, J. und Klostermeier, D., 2021. What makes a type IIA topoisomerase a gyrase or a Topo IV?. Nucleic Acids Res .. 2021. doi: 10.1093/nar/gkab270.
• Klostermeier, D., 2021. Towards Conformation-Sensitive Inhibition of Gyrase: Implications of Mechanistic Insight for the Identification and Improvement of Inhibitors. Molecules .. 26(5). doi: 10.3390/molecules26051234..
• Donsbach, P. und Klostermeier, D., 2021. Regulation of RNA helicase activity: principles and examples. Biol Chem .. 2021. doi: 10.1515/hsz-2020-0362.
• Krause, L. und Klostermeier, D., 2021. Probing RNA Helicase Conformational Changes by Single-Molecule FRET Microscopy. Methods Mol Biol. 2209, S. 119–132. doi: 10.1007/978-1-0716-0935-4_8.
• Klostermeier, D., 2021. Highlight: RNA helicases–structure, function, mechanism and regulation. Biological Chemistry Hoppe-Seyler. 402(5), S. 527–528. ISSN 0177-3593. doi: 10.1515/hsz-2021-0194.
• Romanovska, A., Keil, J., Tophoven, J., Furkan Oruc, M., Schmidt, M., Breisch, M., Sengstock*, C. und Weidlich, D.Klostermeier* D. Tiller* J., 2021. Conjugates of ciprofloxacin and amphiphilic block copoly (2-alkyl-2-oxazolines) s overcome efflux pumps and are active against CIP-resistant bacteria. Molecular pharmaceutics. 18(9), S. 3532–3543. ISSN 1543-8384. doi: 10.1021/acs.molpharmaceut.1c00430.

2020

• Donsbach, P., Yee, BA., Sanchez-Hevia, D., Berenguer, J., Aigner, S., Yeo, GW. und Klostermeier, D., 2020. The Thermus thermophilus DEAD-box protein Hera is a general RNA binding protein and plays a key role in tRNA metabolism. RNA .. 11, S. 1557–1574. doi: 10.1261/rna.075580.120.
• Collin, F., Weisslocker-Schaetzel, M. und Klostermeier, D., 2020. A β-hairpin is a Minimal Latch that Supports Positive Supercoiling by Reverse Gyrase. J Mol Biol. 432(16), S. 4762–4771. doi: 10.1016/j.jmb.2020.06.018.
• Leemans, M., Galicia, C., Deyaert, E., Daems, E., Krause, L., Paesmans, J., Pardon, E., Steyaert, J., Kortholt, A., Sobott, F., Klostermeier, D. und Versées, W., 2020. Allosteric modulation of the GTPase activity of a bacterial LRRK2 homolog by conformation-specific Nanobodies. Biochem J .. 477(7), S. 1203–1218. doi: 10.1042/BCJ20190843.
• Weidlich, D. und Klostermeier, D., 2020. Functional interactions between gyrase subunits are optimized in a species-specific manner. J Biol Chem .. 295(8), S. 2299–2312. doi: 10.1074/jbc.RA119.010245.

2019

• Andreou, AZ., Harms, U. und Klostermeier, D., 2019. Single-stranded regions modulate conformational dynamics and ATPase activity of eIF4A to optimize 5'-UTR unwinding. Nucleic Acids Res .. 47(10), S. 5260–5275. doi: 10.1093/nar/gkz254.

2018

• Stelljes, J., Weidlich, D., Gubaev, A. und Klostermeier, D., 2018. Gyrase containing a single C-terminal domain catalyzes negative supercoiling of DNA by decreasing the linking number in steps of two. Nucleic Acids Research. 46(13), S. 6773–6784. ISSN 0305-1048. doi: 10.1093/nar/gky470.
• Klostermeier, Dagmar, 2018. Why Two? On the Role of (A-)Symmetry in Negative Supercoiling of DNA by Gyrase. Int. J. Mol. Sci.. 19. doi: 10.3390/ijms19051489.

2017

• Hartmann, S., Gubaev, A. und Klostermeier, D., 2017. Binding and hydrolysis of a single ATP is sufficient for negative supercoiling of DNA by gyrase. J. Mol. Biol.. 429(23), S. 3717–3729. doi: 10.1016/j.jmb.2017.10.005.
• Samantanga, B., Andreou, A.Z. und Klostermeier, D., 2017. Allosteric regulation of helicase core activities of the DEAD-box helicase YxiN by RNA binding to its RNA recognitation motif. Nuc. Acids Res.. 45(4), S. 1994–2006. doi: 10.1093/nar/gkx014.
• Klostermeier, D. und Rudolph, M.G., 2017. Biophysical Chemistry. o. O.: unbekannt / n.a. / unknown ISBN 9781482252231.
• Andreou, A., Harms, U. und Klostermeier, D., 2017. eIF4B stimulates eIF4A ATPase and unwinding activities by direct interaction through its 7-repeats region. RNA Biol.. 14(1), S. 113–123. doi: 10.1080/15476286.2016.1259782.

2016

• Hartmann, S., Weidlich, D. und Klostermeier, D., 2016. Single-Molecule Confocal FRET Microscopy to Dissect Conformational Changes in the Catalytic Cycle of DNA Topoisomerases. Methods Enzymol. 581, S. 317–351. doi: 10.1016/bs.mie.2016.08.013.
• Gubaev, A., Weidlich, D. und Klostermeier, D., 2016. DNA gyrase with a single catalytic tyrosine can catalyze DNA supercoiling by a nicking-closing mechanism. Nucl. Acids Res.. 44(21), S. 10354–10366. doi: 10.1093/nar/gkw740.
• Heininger, A.U., Hackert, P., Andreou, A.Z., Boon, K.L., Memet, I., Prior, M., Clancy, A., Schmidt, B., Urlaub, H., Schleiff, E., Sloan, K.E., Deckers, M., Lührmann, R., Enderlein, J., Klostermeier, D., Rehling, P. und Bohnsack, M.T., 2016. Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways. RNA Biol. 13(3), S. 320–330. doi: 10.1080/15476286.2016.1142038.

2015

• Nianios, D., Thierbach, S., Steimer, L., Lulchev, P., Klostermeier, D. und Fetzner, S., 2015. Nickel quercetinase, a "promiscuous metalloenzyme: metal incorporation and metal ligand substitution studies. BMC Biochem. 16(10). doi: 10.1186/s12858-015-0039-4.
• Rudolph, M.G. und Klostermeier, D., 2015. When core competence is not enough: functional interplay of the DEAD-box helicase core with ancillary domains and auxilliary factors in RNA binding and unwinding. Biol. Chem.. 396(8), S. 849–865. doi: 10.1515/hsz-2014-0277.

2014

• Samatanga, B. und Klostermeier, D., 2014. DEAD-box RNA helicase domains exhibit a continuum between complete functional independence and high thermodynamic coupling in nucleotide and RNA duplex recognition. Nucl. Acids Res. 42(16), S. 10644–10654.
• Del Toro Duany, Y., Ganguly, A. und Klostermeier, D., 2014. Differential contributions of the latch in Thermotoga maritima reverse gyrase to binding of single-stranded DNA before and after ATP hydrolysis. Biol. Chem.. 395(1), S. 83–93. doi: 10.1515/hsz-2013-0177.
• Andreou, A.Z. und Klostermeier, D., 2014. eIF4B and eIF4G jointly stimulate eIF4A ATPase and unwinding activities by modulation of the eIF4A conformational cycle. J. Mol. Biol.. 426(1), S. 51–61. doi: 10.1016/j.jmb.2013.09.027.
• Lanz, M.A., Farhat, M. und Klostermeier, D., 2014. The acidic C-terminal tail of the GyrA subunit moderates the DNA supercoiling activity of Bacillus subtilis gyrase. J. Biol. Chem.. 289(18), S. 12275–12285. doi: 10.1074/jbc.M114.547745.
• Gubaev, A. und Klostermeier, D., 2014. The mechanism of negative DNA supercoiling: a cascade of DNA-induced conformational changes prepares gyrase for strand passage. DNA Repair. 16, S. 23–24. ISSN 1568-7864. doi: 10.1016/j.dnarep.2014.01.011.
• Harms, U., Andreou, A.Z., Gubaev, A. und Klostermeier, D., 2014. eIF4B, eIF4G and RNA regulate eIF4A activity in translation initiation by modulating the eIF4A conformational cycle. Nucl. Acids Res.. 42(12), S. 7911–7922. doi: 10.1093/nar/gku440.
• Lulchev, P. und Klostermeier, D., 2014. Reverse gyrase-recent advances and current mechanistic understanding of positive DNA supercoiling. Nucl. Acids Res.. 42, S. 8200–8213. doi: 10.1093/nar/gku589.
• Andreou, A.Z. und Klostermeier, D., 2014. Fluorescence Methods in the Investigation of the DEAD-Box Helicase Mechanism. Experienta Supplementum. 105, S. 161–192. doi: 10.1007/978-3-0348-0856-9_8.

2013

• Klostermeier, D., 2013. Rearranging RNA structures at 75°C? Towards the physiologic function of the DEAD-box helicase Hera from Thermus thermophilus”, for the Biopolymers Special Issue “Nucleic acids. Biopolymers. 99(12), S. 1137–1146. doi: 10.1002/bip.22316.
• Gubaev, A. und Klostermeier, D., 2013. Single molecule FRET reveals DNA- and nucleotide-induced conformational changes in DNA gyrase preceding the strand passage reaction, for the DNA repair Special Issue “Single molecule approaches: watching DNA repair one molecule at a time. DNA repair.. doi: 10.1042/BST0390611.
• Del Toro Duany, Y., Ganguly, A. und Klostermeier, D., 2013. Differential contributions of the latch in Thermotoga maritima reverse gyrase to binding of single-stranded DNA before and after ATP hydrolysis. Biol. Chem.. 394. doi: 10.1515/hsz-2013-0177.
• Andreou, A. Z. und Klostermeier, D., 2013. eIF4B and eIF4G jointly stimulate eIF4A ATPase and unwinding activities by modulation of the eIF4A conformational cycle. J. Mol. Biol.. 2013. doi: 10.1016/j.jmb.2013.09.027..
• Steimer, L., Wurm, J.P., Linden, M.H., Rudolph, M.G., Wöhnert, J. und Klostermeier, D., 2013. Recognition of two distinct elements in the RNA substrate by the RNA-binding domain of the T. thermophilus DEAD box helicase Hera. Nucl. Acids Res.. 41(12), S. 6259–6272. doi: 10.1093/nar/gkt323.
• Rudolph, M.G. und Klostermeier, D., 2013. Mapping the Spectrum of Conformational States of the DNA- and C-Gates in Bacillus subtilis Gyrase. J. Mol. Biol.. 2013.
• Klostermeier, D., 2013. Lifelong companions: RNA helicases and their roles in RNA metabolism. RNA Biol.. 10(1), S. 2–3.
• Rudolph, M.G., del Toro Duany, Y., Jungblut, S.P., Ganguly, A. und Klostermeier, D., 2013. Crystal structures of Thermotoga maritima reverse gyrase: inferences for the mechanism of positive DNA supercoiling. Nucl. Acids Res.. 41(2), S. 1058–1070. doi: 10.1093/nar/gks1073.
• Ganguly, A., del Toro Duany, Y. und Klostermeier, D., 2013. Reverse gyrase transiently unwinds double-stranded DNA in an ATP-dependent reaction. J. Mol. Biol.. 425(1), S. 32–40.

2012

• Andreou, A.Z. und Klostermeier, D., 2012. DEAD-box helicase conformational changes monitored by single molecule fluorescence resonance energy transfer”, in “RNA Helicases: Analysis of Molecular Mechanisms and Biological Functions. Methods in Enzymology. 511, S. 75–109.
• Steimer, L. und Klostermeier, D., 2012. RNA helicases in infection and disease”, Special Issue on “RNA and Disease. RNA Biology. 9(6), S. 751–771.
• Andreou, A.Z. und Klostermeier, D., 2012. The DEAD box helicase eIF4A: paradigm or special case?” for the RNA Biology Special Issue on “RNA helicases. RNA Biology. 10(1), S. 19–32.
• Andreou, A. und Klostermeier, D., 2012. Conformational changes of DEAD-box helicases monitored by single molecule fluorescence resonance energy transfer. Methods Enzymol.. 511, S. 75–109.
• Lanz, M. und Klostermeier, D., 2012. The GyrA-box determines the geometry of DNA bound to gyrase and couples DNA binding to the nucleotide cycle. Nucleic Acids Res.. 40(21), S. 10893–10903.
• Andreou, A. und Klostermeier, D., 2012. The DEAD-box helicase elF4A: Paradigm or the odd one out?. RNA Biol.. 10(1), S. 1–14.
• Ganguly, A., Del Toro Duany, Y. und Klostermeier, D., 2012. Reverse Gyrase Transiently Unwinds Double-Stranded DNA in an ATP-Dependent Reaction. J. Mol. Biol.. 425(1), S. 32–40.
• Rudolph, MG., Del Toro Duany, Y., Jungblut, SP., Ganguly, A. und Klostermeier, D., 2012. Crystal structures of Thermotoga maritima reverse gyrase: inferences for the mechanism of positive DNA supercoiling. Nucleic Acids Res.. 2012, S. 1–13.
• Gubaev, A. und Klostermeier, D., 2012. Potassium ions are required for nucleotide-induced closure of gyrase N-gate. J. Biol. Chem. 287(14), S. 10916–10921.

2011

• Klostermeier, D., 2011. Highlight: Mechanisms of RNA-mediated regulation. Biological Chemistry. 392(4), S. 275. ISSN 1431-6730. doi: 10.1515/BC.2011.047.
• Hammann, C., Hartmann, RK., Helm, M., Klostermeier, D., Marchfelder, A., Suess, B. und Vörtler, S., 2011. Regulatory RNAs and beyond. EMBO Reports. 12(8), S. 751–753. ISSN 1469-221X. doi: 10.1038/embor.2011.150.
• Ganguly, A., del, Toro Duany Y, Rudolph, MG. und Klostermeier, D., 2011. The latch modulates nucleotide and DNA binding to the helicase-like domain of Thermotoga maritima reverse gyrase and is required for positive DNA supercoiling. Nucleic Acids Research. 39(5), S. 1789–1800. ISSN 0305-1048. doi: 10.1093/nar/gkq1048.
• Strohmeier, J., Hertel, I., Diederichsen, U., Rudolph, M.G. und Klostermeier, D., 2011. Changing nucleotide specificity of the DEAD-box helicase Hera abrogates communication between the Q-motif and the P-loop. Biological Chemistry. 329(4), S. 357–369. ISSN 1431-6730. doi: 10.1515/BC.2011.034.
• Klostermeier, D., 2011. Single-molecule FRET reveals nucleotide-driven conformational changes in molecular machines and their link to RNA unwinding and DNA supercoiling. Biochemical Society Transactions. 39(2), S. 611–616. ISSN 0300-5127. doi: 10.1042/BST0390611.
• del, Toro Duany Y und Klostermeier, D., 2011. Nucleotide-driven conformational changes in the reverse gyrase helicase-like domain couple the nucleotide cycle to DNA processing. Physical Chemistry Chemical Physics., S. Paper. ISSN 1463-9076. doi: 10.1039/C0CP02859B.
• Gubaev, Ayrat Klostermeier Dagmar, 2011. DNA-induced narrowing of the gyrase N-gate coordinates T-segment capture and strand passage. Proceedings of the National Academy of Sciences of the United States of America 108(34), S. 14085–14090. ISSN 0027-8424. doi: 10.1073/pnas.1102100108.
• Lanz, Martin A. und Klostermeier, Dagmar, 2011. Guiding strand passage: DNA-induced movement of the gyrase C-terminal domains defines an early step in the supercoiling cycle.. Nucleic Acids Research., S. 1–14. ISSN 0305-1048. doi: 10.1093/nar/gkr680.
• Del Toro Duany, Y., Klostermeier, D. und Rudolph, M.G., 2011. The conformational flexibility of the helicase-like domain from Thermotoga maritima reverse gyrase is restricted by the topoisomerase domain. Biochemistry. 50(26), S. 5816–5823. ISSN 0006-2960.
• Hilbert, M., Kebbel, F., Gubaev, A. und Klostermeier, D., 2011. eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism. Nucl. Acids Res.. 2011(39(6)), S. 2260–2270.

2010

• Karow, AR. und Klostermeier, D., 2010. A Structural Model for the DEAD Box Helicase YxiN in Solution: Localization of the RNA Binding Domain. Journal of Molecular Biology. 402(4), S. 629–637. ISSN 0022-2836. doi: 10.1016/j.jmb.2010.07.049.

2009

• Rudolph, M.G. und Klostermeier, D., 2009. The Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase core. RNA. 15(11), S. 1993–2001. ISSN 1355-8382. doi: 10.1261/rna.1820009.
• Karow, A.R. und Klostermeier, D., 2009. A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN. Nucleic Acids Research. 37(13), S. 4464–4471. ISSN 0305-1048. doi: 10.1093/nar/gkp397.
• Rudolph, M.G., Wittmann, J.G. und and, Klostermeier D., 2009. Crystallization and preliminary characterization of the Thermus thermophilus RNA helicase Hera C-terminal domain. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 65(3), S. 248–252. ISSN 17443091. doi: 10.1107/S1744309108043145.
• Klostermeier, D. und Rudolph, 2009. A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility. Nucleic Acids Research. 37(2), S. 421–430. ISSN 0305-1048. doi: 10.1093/nar/gkn947.
• Gubaev, A., Hilbert, M. und Klostermeier, D., 2009. The DNA-gate of Bacillus subtilis gyrase is predominantly in the closed conformation during the DNA supercoiling reaction. Proceedings of the National Academy of Sciences of the United States of America. 106(32), S. 13278–13283. ISSN 0027-8424. doi: 10.1073/pnas.0902493106.
• Aregger, R. und Klostermeier, D., 2009. The DEAD Box Helicase YxiN Maintains a Closed Conformation during ATP Hydrolysis. Biochemistry. 48(45), S. 10679–10681. ISSN 0006-2960. doi: 10.1021/bi901278p.
• Hilbert, M., Karow, A.R. und Klostermeier, D., 2009. The mechanism of ATP-dependent RNA unwinding by DEAD-box proteins. Biological Chemistry. 390(12), S. 1237–1250. ISSN 1431-6730. doi: 10.1515/BC.2009.135.
• Klostermeier, Dagmar, Guzy, Lidia und Mihr and Rajah Scheepers, Anja, Hrsg., 2009. Wohin mit uns? – Wissenschaftlerinnen und Wissenschaftler der Zukunft. Lausanne: Peter Lang. ISBN 978-3-631-58114-8.

2008

• Linden, M.L., Hartmann, R.K. und Klostermeier, D., 2008. The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity. Nucleic Acids Research. 36(18), S. 5800–5811. ISSN 0305-1048. doi: 10.1093/nar/gkn581.
• Del, Toro Duany Y., Jungblut, S.P., Schmidt, A.S. und Klostermeier, D., 2008. The reverse gyrase helicase-like domain is a nucleotide-dependent switch that is attenuated by the topoisomerase domain. Nucleic Acids Research. 36(18), S. 5882–5895. ISSN 0305-1048. doi: 10.1093/nar/gkn587.
• Theissen, B., Karow, A.R., Köhler, J., Gubaev, A. und Klostermeier, D., 2008. RNA and ATP cooperatively induce a conformational change in a DEAD box helicase. Proceedings of the National Academy of Sciences of the United States of America. 105(2), S. 548–553. ISSN 0027-8424. doi: 10.1073/pnas.0705488105.

2007

• Jungblut, S.P. und Klostermeier, D., 2007. Adenosine 5′-O-(3-thio)triphosphate (ATPγS) Promotes Positive Supercoiling of DNA by T. maritima Reverse Gyrase. Journal of Molecular Biology. 371(1), S. 197–209. ISSN 0022-2836. doi: 10.1016/j.jmb.2007.05.031.
• Göttler, T. und Klostermeier, D., 2007. Dissection of the Nucleotide Cycle of B. subtilis DNA Gyrase and its Modulation by DNA. Journal of Molecular Biology. 367(5), S. 1392–1404. ISSN 0022-2836. doi: 10.1016/j.jmb.2007.01.055.
• Karow, A., Theissen, B. und Klostermeier, D., 2007. Authentic interdomain communication in an RNA helicase reconstituted by expressed protein ligation of two helicase domains. The FEBS Journal. 274(2), S. 463–473. ISSN 1742-464X. doi: 10.1111/j.1742-4658.2006.05593.x.

2006

• Rudolph, M.G., Heissmann, R., Wittmann, J.G. und Klostermeier, D., 2006. Crystal Structure and Nucleotide Binding of the Thermus thermophilus RNA Helicase Hera N-terminal Domain. Journal of Molecular Biology. 361(4), S. 731–743. ISSN 0022-2836.

2005

• Pljevjalcic, G., Klostermeier, D. und Millar, D.P., 2005. The tertiary structure of the hairpin ribozyme is formed through a slow conformational search. Biochemistry. 44(12), S. 4870–4876. ISSN 0006-2960. doi: 10.1021/bi047772i.

2004

• Klostermeier, D., Sears, P., Wong, C.-H., Millar, D.P. und Williamson, J.R., 2004. A three-fluorophore FRET assay for high-throughput screening of small-molecule inhibitors of ribosome assembly. Nucleic Acids Research. 32(9), S. 2707–2715. ISSN 0305-1048. doi: 10.1093/nar/gkh588.
• Dumitru, G. L., Deuerling, E., Groemping, Y., Klostermeier, D., Restle, T. und Reinstein, J., 2004. DafA cycles between the DnaK chaperone system and translational machinery. Journal of Molecular Biology. 339(5), S. 1179–1189. ISSN 0022-2836. doi: 10.1016/j.jmb.2004.04.052.

2002

• Klostermeier, D. und Millar, D.P., 2002. Energetics of hydrogen bond networks in RNA: Hydrogen bonds surrounding G+1 and U42 are the major determinants for the tertiary structure stability of the hairpin ribozyme. Biochemistry. 41(48), S. 14095–14102. ISSN 0006-2960. doi: 10.1021/bi025551b.

2001

• Klostermeier, D. und Millar, D.P., 2001. Time-resolved fluorescence resonance energy transfer: A versatile tool for the analysis of nucleic acids. Biopolymers. 61(3), S. 159–179. ISSN 0006-3525. doi: 10.1002/bip.10146.
• Ryder, S.P., Oyelere, A.K., Padilla, J., Klostermeier, D., Millar, D.P. und Strobel, S.A., 2001. Investigation of adenosine base ionization in the hairpin ribozyme by nucleotide analog interference mapping. RNA. 7(10), S. 1454–1463. ISSN 1355-8382.
• Klostermeier, D. und Millar, D.P., 2001. RNA conformation and folding studied with fluorescence resonance energy transfer. Methods. 23(3), S. 240–254. ISSN 1046-2023. doi: 10.1006/meth.2000.1135.
• Klostermeier, D. und Millar, D.P., 2001. Tertiary structure stability of the hairpin ribozyme in its natural and minimal forms: Different energetic contributions from a ribose zipper motif. Biochemistry. 40(37), S. 11211–11218. ISSN 0006-2960. doi: 10.1021/bi010773f.
• Brehmer, D., Ruediger, S., Gaessler, C., Klostermeier, D., Packschies, L., Reinstein, J., Mayer., M.P. und Bukau, B., 2001. Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange. Nature Structural Biology. 8(5), S. 427–432. ISSN 1072-8368. doi: 10.1038/87588.
• Grömping, Y., Klostermeier, D., Herrmann, C., Veit, T., Seidel, R. und Reinstein, J., 2001. Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE. Journal of Molecular Biology. 305(5), S. 1173–1183. ISSN 0022-2836. doi: 10.1006/jmbi.2000.4373.

2000

• Klostermeier, D. und Millar, D.P., 2000. Helical junctions as determinants for RNA folding: Origin of tertiary structure stability of the hairpin ribozyme. Biochemistry. 39(42), S. 12970–12978. ISSN 0006-2960. doi: 10.1021/bi0014103.

1999

• Laufen T., Mayer, M.P., Beisel C., Klostermeier D., Mogk A. und Reinstein J., Bukau B., 1999. Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones. Proceedings of the National Academy of Sciences of the United States of America. 96(10), S. 5452–5457. ISSN 0027-8424. doi: 10.1073/pnas.96.10.5452.
• Klostermeier, D., Seidel, R. und Reinstein, J., 1999. The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system. Journal of Molecular Biology. 287(3), S. 511–525. ISSN 0022-2836. doi: 10.1006/jmbi.1999.2636.

1998

• Klostermeier, D., Seidel, R. und Reinstein, J., 1998. Functional properties of the molecular chaperone DnaK from Thermus thermophilus. Journal of Molecular Biology. 279(4), S. 841–853. ISSN 0022-2836. doi: 10.1006/jmbi.1998.1816.

1997

• Klostermeier, D., Bayer, P., Kraft, M., Frank, R.W. und Rösch, P., 1997. Spectroscopic investigations of HIV-1 trans-activator and related peptides in aqueous solutions. Biophysical Chemistry. 63(2-3), S. 87–96. ISSN 0301-4622. doi: 10.1016/S0301-4622(96)02243-0.