Publications of W. Wintermeyer

Mercier, E.; Wintermeyer, W.; Rodnina, M. V.: Co‐translational insertion and topogenesis of bacterial membrane proteins monitored in real time. EMBO Journal 39 (15), e104054 (2020)

Rodnina, M. V.; Peske, F.; Peng, B. Z.; Belardinelli, R.; Wintermeyer, W.: Converting GTP hydrolysis into motion: Versatile translational elongation factor G. Biological Chemistry 401 (1), pp. 131 - 142 (2019)

Zaghouania, M.; Bögeholz, L. A. K.; Mercier, E.; Wintermeyer, W.; Roche, S. P.: Total synthesis of (±)-fumimycin and analogues for biological evaluation as peptide deformylase inhibitors. Tetrahedron 75 (24), pp. 3216 - 3230 (2019)

Draycheva, A.; Lee, S.; Wintermeyer, W.: Cotranslational protein targeting to the membrane: Nascent-chain transfer in a quaternary complex formed at the translocon. Scientific Reports 8 (1), 9922 (2018)

Mercier, E.; Holtkamp, W.; Rodnina, M. V.; Wintermeyer, W.: Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence. Nucleic Acids Research 45 (20), pp. 11858 - 11866 (2017)

Ranjan, A.; Mercier, E.; Bhatt, A.; Wintermeyer, W.: Signal recognition particle prevents N-terminal processing of bacterial membrane proteins. Nature Communications 8, 15562 (2017)

Draycheva, A.; Bornemann, T.; Ryazanov, S.; Lakomek, N. A.; Wintermeyer, W.: The bacterial SRP receptor, FtsY, is activated on binding to the translocon. Molecular Microbiology 102 (1), pp. 152 - 167 (2016)

Lakomek, N. A.; Draycheva, A.; Bornemann, T.; Wintermeyer, W.: Electrostatics and intrinsic disorder drive translocon binding of the SRP receptor FtsY. Angewandte Chemie International Edition 55 (33), pp. 9544 - 9547 (2016)

Rodnina, M. V.; Wintermeyer, W.: Protein elongation, co-translational folding and targeting. Journal of Molecular Biology 428 (10, P. B), pp. 2165 - 2185 (2016)

Belardinelli, R.; Sharma, H.; Caliskan, N.; da Cunha, C. E. L.; Peske, F.; Wintermeyer, W.; Rodnina, M. V.: Choreography of molecular movements during ribosome progression along mRNA. Nature Structural and Molecular Biology 23 (4), pp. 342 - 348 (2016)

Belardinelli, R.; Sharma, H.; Peske, F.; Wintermeyer, W.; Rodnina, M. V.: Translocation as continuous movement through the ribosome. RNA Biology 13 (12), pp. 1197 - 1203 (2016)

Kuhn, P.; Draycheva, A.; Vogt, A.; Petriman, N. A.; Sturm, L.; Drepper, F.; Warscheid, B.; Wintermeyer, W.; Koch, H. G.: Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon. Journal of Cell Biology 211 (1), pp. 91 - 104 (2015)

Adio, S.; Senyushkina, T.; Peske, F.; Fischer, N.; Wintermeyer, W.; Rodnina, M. V.: Fluctuations between multiple EF-G-induced chimeric tRNA states during translocation on the ribosome. Nature Communications 6, 7442 (2015)

Ge, Y.; Draycheva, A.; Bornemann, T.; Rodnina, M. V.; Wintermeyer, W.: Lateral opening of the bacterial translocon on ribosome binding and signal peptide insertion. Nature Communications 5, 5263 (2014)

Holtkamp, W.; Wintermeyer, W.; Rodnina, M. V.: Synchronous tRNA movements during translocation on the ribosome are orchestrated by elongation factor G and GTP hydrolysis. BioEssays 36 (10), pp. 908 - 918 (2014)

Bornemann, T.; Holtkamp, W.; Wintermeyer, W.: Interplay between trigger factor and other protein biogenesis factors on the ribosome. Nature Communications 5, 4180 (2014)

Holtkamp, W.; da Cunha, C. E. L.; Peske, F.; Konevega, A. L.; Wintermeyer, W.; Rodnina, M. V.: GTP hydrolysis by EF‐G synchronizes tRNA movement on small and large ribosomal subunits. EMBO Journal 33 (9), pp. 1073 - 1085 (2014)

Peske, F.; Kuhlenkötter, S.; Rodnina, M. V.; Wintermeyer, W.: Timing of GTP binding and hydrolysis by translation termination factor RF3. Nucleic Acids Research 42 (3), pp. 1812 - 1820 (2014)

da Cunha, C. E. L.; Belardinelli, R.; Peske, F.; Holtkamp, W.; Wintermeyer, W.; Rodnina, M. V.: Dual use of GTP hydrolysis by elongation factor G on the ribosome. Translation 1 (1), e24315 (2013)

Holtkamp, W.; Lee, S.; Bornemann, T.; Senyushkina, T.; Rodnina, M. V.; Wintermeyer, W.: Dynamic switch of the signal recognition particle from scanning to targeting. Nature Structural and Molecular Biology 19 (12), pp. 1332 - 1337 (2012)