BETA: Related publications
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| Zuber PK, Said N, Hilal T, et al. (2024) Concerted transformation of a hyper-paused transcription complex and its reinforcing protein. Nature Communications. 15: 3040 |
| Zuber PK, Daviter T, Heißmann R, et al. (2022) Structural and thermodynamic analyses of the β-to-α transformation in RfaH reveal principles of fold-switching proteins. Elife. 11 |
| Washburn RS, Zuber PK, Sun M, et al. (2020) Escherichia coli NusG Links the Lead Ribosome with the Transcription Elongation Complex. Iscience. 23: 101352 |
| Dudenhoeffer BR, Borggraefe J, Schweimer K, et al. (2020) NusA directly interacts with antitermination factor Q from phage λ. Scientific Reports. 10: 6607 |
| Galaz-Davison P, Molina JA, Silletti S, et al. (2019) Differential Local Stability Governs the Metamorphic Fold Switch of Bacterial Virulence Factor RfaH. Biophysical Journal |
| Dudenhoeffer BR, Schneider H, Schweimer K, et al. (2019) SuhB is an integral part of the ribosomal antitermination complex and interacts with NusA. Nucleic Acids Research |
| Artsimovitch I, Knauer SH. (2019) Ancient Transcription Factors in the News. Mbio. 10 |
| Zuber PK, Schweimer K, Rösch P, et al. (2019) Reversible fold-switching controls the functional cycle of the antitermination factor RfaH. Nature Communications. 10: 702 |
| Zuber PK, Hahn L, Reinl A, et al. (2018) Structure and nucleic acid binding properties of KOW domains 4 and 6-7 of human transcription elongation factor DSIF. Scientific Reports. 8: 11660 |
| Zuber PK, Artsimovitch I, NandyMazumdar M, et al. (2018) The universally-conserved transcription factor RfaH is recruited to a hairpin structure of the non-template DNA strand. Elife. 7 |