A bacterial nucleolus for cold adaptation.

Gut MJ, Dorner K, Abegg S, Qureshi NS, Ramachandran K, Loynton-Ferrand A, Prakapaite R, Schmidt A, Williams TA, Duss O, Hondele M

bioRxiv, 2026

doi:10.64898/2026.09.17.752289.

Mapping in-cell protein contact sites reveals hijacking of paraspeckles during influenza A virus infection.

Kotova I, Mühlberg L, Gilep K, Burtscher ML, Becher I, Yu D, Ziemianowicz D, Stanelle-Bertram S, Beck S, Baeg K, Grba A, Duss O, Gabriel G, Savitski MM, Liu F, Bogdanow B, Kosinski J

Nature microbiology, 2026

doi:10.1038/s41564-026-02416-1.

Paraspeckle condensation is controlled via TDP-43 polymerization and linked to neuroprotection.

Hodgson RE, Huang WP, Lang R, Kumar V, An H, Stender EGP, Chalakova ZP, Driver MD, Sanchez Avila A, Ellis BCS, Day E, Rayment JA, Baeg K, Strange A, Moll T, Wright GSA, van Vugt JJFA, Project MinE ALS Sequencing Consortium, Allen SP, Locker N, Pitout I, Fletcher S, Onck PR, Duss O, Cooper-Knock J, Shelkovnikova TA

Nature cell biology, 2026

doi:10.1038/s41556-026-01895-y.

Functional characterization of dynamic nascent RNA folding ensembles in real time.

Gor K, Geissen EM, Duss O

Science advances, 2026

doi:10.1126/sciadv.aec4037.

Functional coupling between ribosomal RNA transcription and processing guided by stable transcription factor binding.

Chaban A, Qureshi NS, Duss O

bioRxiv, 2026

doi:10.64898/2026.03.17.712431.

Real-time tracking of mRNP complex assembly reveals various mechanisms that synergistically enhance translation repression.

Payr M, Meyer J, Geissen EM, Hennig J, Duss O

Cell reports, 2025

doi:10.1016/j.celrep.2025.116492.

Snapshot of in-cell protein contact sites reveals new host factors and hijacking of paraspeckles during influenza A virus infection.

Kotova I, Mühlberg L, Gilep K, Yu D, Ziemianowicz D, Stanelle-Bertram S, Beck S, Baeg K, Duss O, Gabriel G , Liu F, Bogdanow B, Kosinski J

bioRxiv, 2025

doi:10.1101/2025.03.09.642134.

Structural and kinetic insights into tRNA promoter engagement by yeast general transcription factor TFIIIC.

Seifert-Dávila W, Chaban A, Baudin F, Girbig M, Hauptmann L, Hoffmann T, Duss O, Eustermann S, Müller CW

Nucleic acids research, 2025

doi:10.1093/nar/gkae1174.

Tracking transcription-translation coupling in real time.

Qureshi NS, Duss O

Nature, 2025

doi:10.1038/s41586-024-08308-w.

Exploring the dynamics of messenger ribonucleoprotein-mediated translation repression.

Meyer J, Payr M, Duss O, Hennig J

Biochemical Society transactions, 2024

doi:10.1042/BST20231240.

Tracking transcription-translation coupling in real-time.

Qureshi NS, Duss O

bioRxiv, 2023

doi:10.1101/2023.12.07.570708.

Interconnections between m6A RNA modification, RNA structure, and protein-RNA complex assembly.

Höfler S, Duss O

Life science alliance, 2023

doi:10.26508/lsa.202302240.

Co-transcriptional assembly mechanisms of protein-RNA complexes.

Qureshi NS, Duss O

FEBS letters, 2023

doi:10.1002/1873-3468.14758.

Decoding a ribosome uncertainty.

Duss O, Nikolay R, Kraushar ML

Trends in genetics : TIG, 2023

doi:10.1016/j.tig.2023.06.001.

Emerging quantitative biochemical, structural, and biophysical methods for studying ribosome and protein-RNA complex assembly.

Gor K, Duss O

Biomolecules, 2023

doi:10.3390/biom13050866.

Real-time tracking of transcription-translation coupling.

Qureshi N, Duss O

Biophysical journal, 2023

doi:10.1016/j.bpj.2022.11.2608.

Transient protein-RNA interactions guide nascent ribosomal RNA folding.

Duss O, Stepanyuk GA, Puglisi JD, Williamson JR

Cell, 2019

doi:10.1016/j.cell.2019.10.035.

An integrated cell-free assay to study translation regulation by small bacterial noncoding RNAs.

Michel E, Duss O, Allain FH

Methods in molecular biology (Clifton, N.J.), 2018

doi:10.1007/978-1-4939-7634-8_11.

Real-time assembly of ribonucleoprotein complexes on nascent RNA transcripts.

Duss O, Stepanyuk GA, Grot A, O'Leary SE, Puglisi JD, Williamson JR

Nature communications, 2018

doi:10.1038/s41467-018-07423-3.

Aromatic side-chain conformational switch on the surface of the RNA Recognition Motif enables RNA discrimination.

Diarra Dit Konté N, Krepl M, Damberger FF, Ripin N, Duss O, Šponer J, Allain FH

Nature communications, 2017

doi:10.1038/s41467-017-00631-3.

Combining NMR and EPR to determine structures of large RNAs and protein-RNA complexes in solution.

Duss O, Yulikov M, Allain FHT, Jeschke G

Methods in enzymology, 2015

doi:10.1016/bs.mie.2015.02.005.

Cut and paste RNA for nuclear magnetic resonance, paramagnetic resonance enhancement, and electron paramagnetic resonance structural studies.

Duss O, Diarra Dit Konté N, Allain FH

Methods in enzymology, 2015

doi:10.1016/bs.mie.2015.05.029.

Structural basis of the non-coding RNA RsmZ acting as a protein sponge.

Duss O, Michel E, Yulikov M, Schubert M, Jeschke G, Allain FH

Nature, 2014

doi:10.1038/nature13271.

EPR-aided approach for solution structure determination of large RNAs or protein-RNA complexes.

Duss O, Yulikov M, Jeschke G, Allain FH

Nature communications, 2014

doi:10.1038/ncomms4669.

Molecular basis for the wide range of affinity found in Csr/Rsm protein-RNA recognition.

Duss O, Michel E, Diarra dit Konté N, Schubert M, Allain FH

Nucleic acids research, 2014

doi:10.1093/nar/gku141.

Automated and assisted RNA resonance assignment using NMR chemical shift statistics.

Aeschbacher T, Schmidt E, Blatter M, Maris C, Duss O, Allain FH, Güntert P, Schubert M

Nucleic acids research, 2013

doi:10.1093/nar/gkt665.

Isotope labeling and segmental labeling of larger RNAs for NMR structural studies.

Duss O, Lukavsky PJ, Allain FH

Advances in experimental medicine and biology, 2012

doi:10.1007/978-94-007-4954-2_7.

Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy.

Dominguez C, Schubert M, Duss O, Ravindranathan S, Allain FH

Progress in nuclear magnetic resonance spectroscopy, 2011

doi:10.1016/j.pnmrs.2010.10.001.

How to study the structure and dynamics of protein-RNA complexes by NMR spectroscopy.

Schubert M, Dominguez C, Duss O, Ravindranathan S, Allain FH

2011

doi:10.3233/978-1-60750-695-9-249.

A fast, efficient and sequence-independent method for flexible multiple segmental isotope labeling of RNA using ribozyme and RNase H cleavage.

Duss O, Maris C, von Schroetter C, Allain FH

Nucleic acids research, 2010

doi:10.1093/nar/gkq756.

Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA.

Schubert M, Lapouge K, Duss O, Oberstrass FC, Jelesarov I, Haas D, Allain FH

Nature structural & molecular biology, 2007

doi:10.1038/nsmb1285.