[14] M. Kaur*, D. Y. Travin*, M. Berger*, M. Jangra, M. Morici, H. A. Safdari, D. Klepacki, W. Wang, M. Cook, S. Chou, A. Guitor, K. Koteva, M. Xu, L. Ejim, L. Macneil, N. Vázquez-Laslop, A. S. Mankin, D. Wilson, and G. Wright, “A natural depsipeptide antibiotic binds the E-site of the bacterial ribosome”, Nature, vol. 655, pp. 737–746, 2026 (* – authors contributed equally)

[13] M. Jangra, D. Y. Travin, M. Kaur, D. Hackenberger, K. Koteva, Y. S. Polikanov, and G. D. Wright, “An acetyltransferase conferring self-resistance of the producer to lasso peptide antibiotic lariocidin”, ACS Infectious Diseases, vol. 12 no. 2, pp. 714-723, 2026

[12] M. Jangra*, D. Y. Travin*, E. V. Aleksandrova, M. Kaur, L. Darwish, K. Koteva, D. Klepacki, W. Wang, M. Tiffany, A. Sokaribo, B. K. Coombes, N. Vázquez-Laslop, Y. S. Polikanov, A. S. Mankin, and G. D. Wright, “A broad spectrum lasso peptide antibiotic targeting the bacterial ribosome.”, Nature, vol. 640, pp. 1022–1030, 2025 (* – authors contributed equally)

[11] D. Y. Travin#, R. Jouan, A. Vigouroux, S. Inaba-Inoue, J. Lachat, F. Haq, T. Timchenko, D. Sutormin, S. Dubiley, K. Beis, S. Moréra, K. Severinov, and P. Mergaert#, ”Dual-uptake mode of the antibiotic phazolicin prevents resistance acquisition by gram-negative bacteria.” mBio, e0021723., 2023 (# – corresponding authors)

[10] D. Y. Travin, D. Sutormin, P. Mergaert, and K. Severinov, “Complete genome sequences of two Rhizobium strains producing azol(in)e-modified antibiotics.” Microbiol. Resour. Announc., e0072222, 2022

[9] D. Sutormin, A. Galivondzhyan, D. Travin, O. Musharova, A. Rusanova, S. Borukhov, K. Severinov “The interaction between transcribing RNA polymerase and topoisomerase I prevents R-loop formation in E. coli.”, Nat. Commun., 13:4524, 2022

[8] Q. Nicoud, Q. Barrière, N. Busset, S. Dendene, D. Travin, M. Bourge, R. Le Bars, C. Boulogne, M. Lecroël, S. Jenei, A. Kereszt, E. Kondorosi, E. G. Biondi, T. Timchenko, B. Alunni, and P. Mergaert “Sinorhizobium meliloti functions required for resistance to antimicrobial NCR peptides and bacteroid differentiation.” mBio, 12:e00895-21, 2021

[7]   D. Y. Travin, K. Severinov, and S. Dubiley, “Natural Trojan horse inhibitors of aminoacyl-tRNA synthetases.” RSC Chem. Biol., vol. 2, no. 2, pp. 468–485, 2021

[6]   D. Y. Travin, D. Bikmetov, and K. Severinov, “Translation-targeting RiPPs and where to find them.” Front. Genet., 11:226, 2020

[5]   D. Y. Travin, Z. L. Watson, M. Metelev, F. R. Ward, I. A. Osterman, I. M. Khven, N. F. Khabibullina, M. Serebryakova, P. Mergaert, Y. S. Polikanov, J. H. D. Cate, and K. Severinov, “Structure of ribosome-bound azole-modified peptide phazolicin rationalizes its species-specific mode of bacterial translation inhibition.” Nat. Commun., 10:4563, 2019

[4]   D. Ghilarov, C. E. M. Stevenson, D. Y. Travin, J. Piskunova, M. Serebryakova, A. Maxwell, D. M. Lawson, and K. Severinov, “Architecture of microcin B17 synthetase: an octameric protein complex converting a ribosomally synthesized peptide into a DNA gyrase poison.” Mol. Cell, vol. 73, no. 4, pp. 749–762, 2019

[3]   D. Y. Travin*, M. Metelev*, M. Serebryakova, E. S. Komarova, I. A. Osterman, D. Ghilarov, and K. Severinov, “Biosynthesis of translation inhibitor klebsazolicin proceeds through heterocyclization and N-terminal amidine formation catalyzed by a single YcaO enzyme.” J. Am. Chem. Soc., vol. 140, no. 16, pp. 5625–5633, Apr. 2018pp. 1129–1136, 2017, (* – authors contributed equally)

[2]   D. Travin*, I. Popov*, A. T. Guler, D. Medvedev, S. van der Plas-Duivesteijn, M. Varela, I. C. R. M. Kolder, A. H. Meijer, H. P. Spaink, and M. Palmblad, “COMICS: cartoon visualization of omics data in spatial context using anatomical ontologies.” J. Proteome Res., vol. 17, no. 1, pp. 739–744, 2018, (* – authors contributed equally)

[1]   M. Metelev, I. A. Osterman, D. Ghilarov, N. F. Khabibullina, A. Yakimov, K. Shabalin, I. Utkina, D. Y. Travin, E. S. Komarova, M. Serebryakova, T. Artamonova, M. Khodorkovskii, A. L. Konevega, P. V Sergiev, K. Severinov, and Y. S. Polikanov, “Klebsazolicin inhibits 70S ribosome by obstructing the peptide exit tunnel.” Nat. Chem. Biol., vol. 13, no. 10, pp. 1129-1136, 2017