Cryo-EM structures of the human Elongator complex at work

Autor: Nour-el-Hana Abbassi, Marcin Jaciuk, David Scherf, Pauline Böhnert, Alexander Rau, Alexander Hammermeister, Michał Rawski, Paulina Indyka, Grzegorz Wazny, Andrzej Chramiec-Głąbik, Dominika Dobosz, Bozena Skupien-Rabian, Urszula Jankowska, Juri Rappsilber, Raffael Schaffrath, Ting-Yu Lin, Sebastian Glatt

Publikováno v: Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)

Abstract tRNA modifications affect ribosomal elongation speed and co-translational folding dynamics. The Elongator complex is responsible for introducing 5-carboxymethyl at wobble uridine bases (cm5U34) in eukaryotic tRNAs. However, the structure and

Externí odkaz: https://doaj.org/article/33775229bf0d422aa115354cb779786a

Functional Protein Composition in Femoral Glands of Sand Lizards (Lacerta agilis)

Autor: Alejandro Ibáñez, Bozena Skupien-Rabian, Urszula Jankowska, Sylwia Kędracka-Krok, Bartłomiej Zając, Maciej Pabijan

Publikováno v: Molecules, Vol 27, Iss 7, p 2371 (2022)

Proteins are ubiquitous macromolecules that display a vast repertoire of chemical and enzymatic functions, making them suitable candidates for chemosignals, used in intraspecific communication. Proteins are present in the skin gland secretions of ver

Externí odkaz: https://doaj.org/article/4a969eca97ea44b489c23d5ae9af4282

E2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation

Autor: Keerthiraju E Ravichandran, Lars Kaduhr, Bozena Skupien‐Rabian, Ekaterina Shvetsova, Mikołaj Sokołowski, Ros´cisław Krutyhołowa, Dominika Kwasna, Cindy Brachmann, Sean Lin, Sebastian Guzman Perez, Piotr Wilk, Manuel Kösters, Przemysław Grudnik, Urszula Jankowska, Sebastian A Leidel, Raffael Schaffrath, Sebastian Glatt

Publikováno v: Ravichandran, Keerthiraju E; Kaduhr, Lars; Skupien-Rabian, Bozena; Shvetsova, Ekaterina; Sokołowski, Mikołaj; Krutyhołowa, Ros Cisław; Kwasna, Dominika; Brachmann, Cindy; Lin, Sean; Guzman Perez, Sebastian; Wilk, Piotr; Kösters, Manuel; Grudnik, Przemysław; Jankowska, Urszula; Leidel, Sebastian A; Schaffrath, Raffael; Glatt, Sebastian (2022). E2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation. The EMBO journal, 41(20), e111318. EMBO Press 10.15252/embj.2022111318

Post-translational modifications by ubiquitin-like proteins (UBLs) are essential for nearly all cellular processes. Ubiquitin-related modifier 1 (Urm1) is a unique UBL, which plays a key role in tRNA anticodon thiolation as a sulfur carrier protein (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::743dd75f630b383ea5758a3f19ace983

Changes in the Cell Wall Proteome of Leaves in Response to High Temperature Stress in Brachypodium distachyon

Autor: Urszula Jankowska, Alexander Betekhtin, Artur Pinski, Bozena Skupien-Rabian, Robert Hasterok, Elisabeth Jamet

Publikováno v: International Journal of Molecular Sciences
Volume 22
Issue 13
International Journal of Molecular Sciences, MDPI, 2021, 22 (13), pp.6750. ⟨10.3390/ijms22136750⟩
International Journal of Molecular Sciences, Vol 22, Iss 6750, p 6750 (2021)

International audience; High temperature stress leads to complex changes to plant functionality, which affects, i.a., the cell wall structure and the cell wall protein composition. In this study, the qualitative and quantitative changes in the cell w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98b5b48c6fc64d4d5b6e355ac807597f

Analysis of a Nuclear Intrinsically Disordered Proteome

Autor: Bozena, Skupien-Rabian, Urszula, Jankowska, Sylwia, Kedracka-Krok

Publikováno v: Methods in molecular biology (Clifton, N.J.). 2175

Intrinsically disordered proteins (IDPs) play crucial roles in cell functioning, although they do not possess defined three-dimensional architecture. They are highly abundant in the cell nucleus, and the vast majority of transcription factors (TFs) c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::418fce7aa8efd7df5d28fd02187d9760
https://pubmed.ncbi.nlm.nih.gov/32681491