Recognition and catalytic mechanism of tRNA m3C methyltransferase METTL6.

Aupic J, Hollmer I, Tengo L, Sehr P, Kowalinski E, Magistrato A

bioRxiv, 2025

doi:10.1101/2025.06.25.660299.

Structural basis of Spliced Leader RNA recognition by the Trypanosoma brucei cap-binding complex.

Bernhard H, Petržílková H, Popelářová B, Ziemkiewicz K, Bartosik K, Warmiński M, Tengo L, Gröger H, Dolce LG, Mackereth CD, Micura R, Jemielity J, Kowalinski E

Nature communications, 2025

doi:10.1038/s41467-024-55373-w.

Structural basis of tRNA recognition by the m3C RNA methyltransferase METTL6 in complex with SerRS seryl-tRNA synthetase.

Throll P, G Dolce L, Rico-Lastres P, Arnold K, Tengo L, Basu S, Kaiser S, Schneider R, Kowalinski E

Nature structural & molecular biology, 2024

doi:10.1038/s41594-024-01341-3.

Concerted structural rearrangements enable RNA channeling into the cytoplasmic Ski238-Ski7-exosome assembly.

Keidel A, Kögel A, Reichelt P, Kowalinski E, Schäfer IB, Conti E

Molecular cell, 2023

doi:10.1016/j.molcel.2023.09.037.

Structural basis for guide RNA selection by the RESC1-RESC2 complex.

Dolce LG, Nesterenko Y, Walther L, Weis F, Kowalinski E

Nucleic acids research, 2023

doi:10.1093/nar/gkad217.

Structural basis for sequence-independent substrate selection by eukaryotic wobble base tRNA deaminase ADAT2/3.

Dolce LG, Zimmer AA, Tengo L, Weis F, Rubio MAT, Alfonzo JD, Kowalinski E

Nature communications, 2022

doi:10.1038/s41467-022-34441-z.

METTLing in the right place: METTL8 is a mitochondrial tRNA-specific methyltransferase.

Kowalinski E, Alfonzo JD

Molecular cell, 2021

doi:10.1016/j.molcel.2021.11.009.

Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition.

Koliopoulos MG, Lethier M, van der Veen AG, Haubrich K, Hennig J, Kowalinski E, Stevens RV, Martin SR, Reis E Sousa C, Cusack S, Rittinger K

Nature communications, 2018

doi:10.1038/s41467-018-04214-8.

The cryo-EM structure of a ribosome-Ski2-Ski3-Ski8 helicase complex

Schmidt C, Kowalinski E, Shanmuganathan V, Defenouillère Q, Braunger K, Heuer A, Pech M, Namane A, Berninghausen O, Fromont-Racine M, Jacquier A, Conti E, Becker T, Beckmann R

Science (New York, N.Y.), 2016

doi:10.1126/science.aaf7520.

Structure of a Cytoplasmic 11-Subunit RNA Exosome Complex

Kowalinski E, Kögel A, Ebert J, Reichelt P, Stegmann E, Habermann B, Conti E

Molecular cell, 2016

doi:10.1016/j.molcel.2016.05.028.

Saccharomyces cerevisiae Ski7 Is a GTP-Binding Protein Adopting the Characteristic Conformation of Active Translational GTPases

Kowalinski E, Schuller A, Green R, Conti E

Structure (London, England : 1993), 2015

doi:10.1016/j.str.2015.04.018.

RIG-I Self-Oligomerization Is Either Dispensable or Very Transient for Signal Transduction

Louber J, Kowalinski E, Bloyet LM, Brunel J, Cusack S, Gerlier D

PloS one, 2014

doi:10.1371/journal.pone.0108770.

[RIG-I: a viral RNA detector molecular switch]

Kowalinski E, Louber J, Gerlier D, Cusack S

Medecine sciences : M/S, 2012

doi:10.1051/medsci/2012282006.

Structural analysis of specific metal chelating inhibitor binding to the endonuclease domain of influenza pH1N1 (2009) polymerase

Kowalinski E, Zubieta C, Wolkerstorfer A, Szolar OH, Ruigrok RW, Cusack S

PLoS pathogens, 2012

doi:10.1371/journal.ppat.1002831.

Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA

Kowalinski E, Lunardi T, McCarthy AA, Louber J, Brunel J, Grigorov B, Gerlier D, Cusack S

Cell, 2011

doi:10.1016/j.cell.2011.09.039.

D-ribose-5-phosphate isomerase B from Escherichia coli is also a functional D-allose-6-phosphate isomerase, while the Mycobacterium tuberculosis enzyme is not

Roos AK, Mariano S, Kowalinski E, Salmon L, Mowbray SL

Journal of molecular biology, 2008

doi:10.1016/j.jmb.2008.06.090.

Arx1 functions as an unorthodox nuclear export receptor for the 60S preribosomal subunit

Bradatsch B, Katahira J, Kowalinski E, Bange G, Yao W, Sekimoto T, Baumgärtel V, Boese G, Bassler J, Wild K, Peters R, Yoneda Y, Sinning I, Hurt E

Molecular cell, 2007

doi:10.1016/j.molcel.2007.06.034.

The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions

Kowalinski E, Bange G, Bradatsch B, Hurt E, Wild K, Sinning I

FEBS letters, 2007

doi:10.1016/j.febslet.2007.08.024.

Expression, purification, crystallization and preliminary crystallographic analysis of the proliferation-associated protein Ebp1

Kowalinski E, Bange G, Wild K, Sinning I

Acta crystallographica. Section F, Structural biology and crystallization communications, 2007

doi:10.1107/s1744309107038985.