Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolution

Autor: Eva S. Cunha, Xiaorui Chen, Marta Sanz-Gaitero, Deryck J. Mills, Hartmut Luecke

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-8 (2021)

Infection by Helicobacter pylori is associated with peptic ulcers and gastric cancer. H. pylori urease is required for colonization of the stomach and thus an attractive antimicrobial drug target. Cryo-EM analyses of the H. pylori urease with inhibit

Externí odkaz: https://doaj.org/article/69b0a175c71544c4a7319b5dccd61e00

High resolution analysis of proteolytic substrate processing

Autor: Jasmin Schillinger, Michelle Koci, Kenny Bravo-Rodriguez, Geronimo Heilmann, Farnusch Kaschani, Markus Kaiser, Christine Beuck, Hartmut Luecke, Robert Huber, Doris Hellerschmied, Steven G. Burston, Michael Ehrmann

Proteolysis is a key catalytic event in protein and thus cellular homeostasis. Despite the importance and wide implications of proteolytic processing and degradation, methods describing the degradation of folded proteins at high temporal and spatial

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6e1a8f5a84e6a4dd124d2c8969f22e16
https://doi.org/10.1101/2022.03.24.485615

Cryo-EM structure ofHelicobacter pyloriurease with a novel inhibitor in the active site at 2.0 Å resolution

Autor: Hartmut Luecke, Xiaorui Chen, Marta Sanz Gaitero, Deryck J. Mills, Eva S. Cunha

Infection of the human stomach byHelicobacter pyloriremains a worldwide problem and greatly contributes to peptic ulcer disease and gastric cancer. Without active intervention approximately 50% of the world population will continue to be infected wit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::17be64dc5ccc14e1194b1c2f15ece98a
https://doi.org/10.1101/2020.09.14.290999

RNA Editing TUTase 1: structural foundation of substrate recognition, complex interactions and drug targeting

Autor: Rommie E. Amaro, Takuma Suematsu, Ruslan Aphasizhev, Hartmut Luecke, Özlem Demir, Paola Munoz-Tello, Jason R. Stagno, Lional Rajappa-Titu, Inna Aphasizheva, Marius Long, Kevin Cheng, Stéphane Thore

Publikováno v: Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2016, 44 (22), pp.10862-10878. ⟨10.1093/nar/gkw917⟩
Rajappa-Titu, Lional; Suematsu, Takuma; Munoz-Tello, Paola; Long, Marius; Demir, Özlem; Cheng, Kevin J; et al.(2016). RNA Editing TUTase 1: structural foundation of substrate recognition, complex interactions and drug targeting. Nucleic Acids Research, 44(22), 10862-10878. doi: 10.1093/nar/gkw917. UC Irvine: Institute for Clinical and Translational Science. Retrieved from: http://www.escholarship.org/uc/item/1hj8d1c1

Terminal uridyltransferases (TUTases) execute 3′ RNA uridylation across protists, fungi, metazoan and plant species. Uridylation plays a particularly prominent role in RNA processing pathways of kinetoplastid protists typified by the causative agen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f5ee582301067b1eef7d03d8194e131
https://hal.archives-ouvertes.fr/hal-02472380

Structures of oncogenic, suppressor and rescued p53 core-domain variants: mechanisms of mutant p53 rescue

Autor: Ying Wang, Vira Tretyachenko-Ladokhina, Hartmut Luecke, Martha Tan, Brad D. Wallentine, Donald F. Senear

Publikováno v: Acta crystallographica. Section D, Biological crystallography, vol 69, iss Pt 10

To gain insights into the mechanisms by which certain second-site suppressor mutations rescue the function of a significant number of cancer mutations of the tumor suppressor protein p53, X-ray crystallographic structures of four p53 core-domain vari

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::524a44815ef85651eb6752e0b6fbb4cc
https://doi.org/10.1107/s0907444913020830