Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Sebastian Gremer"'
Autor:
Marta Carroni, Kamila B Franke, Michael Maurer, Jasmin Jäger, Ingo Hantke, Felix Gloge, Daniela Linder, Sebastian Gremer, Kürşad Turgay, Bernd Bukau, Axel Mogk
Publikováno v:
eLife, Vol 6 (2017)
Ring-forming AAA+ chaperones exert ATP-fueled substrate unfolding by threading through a central pore. This activity is potentially harmful requiring mechanisms for tight repression and substrate-specific activation. The AAA+ chaperone ClpC with the
Externí odkaz:
https://doaj.org/article/6a24907a82f9431ea0dc97334b3de121
Autor:
Jasmin Jäger, Bernd Bukau, Kamila B. Franke, Sebastian Gremer, Daniela Linder, Marta Carroni, Ingo Hantke, Michael Maurer, Axel Mogk, Felix Gloge, Kürşad Turgay
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f9f107d70fb42b2a8af497288e08e0b5
https://doi.org/10.7554/elife.30120.036
https://doi.org/10.7554/elife.30120.036
Autor:
Bernd Bukau, Sebastian Gremer, Axel Mogk, Gabrielle Taylor, Michael Maurer, Daniela Linder, Jasmin Jäger, Matthias P. Mayer, Felix Gloge, Laura Le Breton, Kamila B. Franke, Eilika Weber-Ban, Marta Carroni
Publikováno v:
Cell Chemical Biology. 26:1169-1179.e4
ATP-driven bacterial AAA+ proteases have been recognized as drug targets. They possess an AAA+ protein (e.g., ClpC), which threads substrate proteins into an associated peptidase (e.g., ClpP). ATPase activity and substrate selection of AAA+ proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56a245d6bac95dabf83bb2ea41757a0c
https://doi.org/10.1016/j.chembiol.2019.05.008
https://doi.org/10.1016/j.chembiol.2019.05.008