Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Kamila B Franke"'
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:
Sander J. Tans, Kamila B. Franke, Mario J. Avellaneda, Vanda Sunderlikova, Axel Mogk, Bernd Bukau
Publikováno v:
Nature. 578:317-320
The ability to reverse protein aggregation is vital to cells1,2. Hsp100 disaggregases such as ClpB and Hsp104 are proposed to catalyse this reaction by translocating polypeptide loops through their central pore3,4. This model of disaggregation is app
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f5c0c80d25894406aaca4ca84006ded8
https://doi.org/10.1038/s41586-020-1964-y
https://doi.org/10.1038/s41586-020-1964-y
Autor:
Mario J, Avellaneda, Kamila B, Franke, Vanda, Sunderlikova, Bernd, Bukau, Axel, Mogk, Sander J, Tans
Publikováno v:
Nature. 578(7794)
The ability to reverse protein aggregation is vital to cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6155dd4c72822d4e4f9b533feb3a3ed6
https://pubmed.ncbi.nlm.nih.gov/32034316
https://pubmed.ncbi.nlm.nih.gov/32034316
Publikováno v:
Journal of Molecular Biology. 428:4378-4391
Escherichia coli ClpB and Saccharomyces cerevisiae Hsp104 are members of the Hsp100 family of ring-forming hexameric AAA+ chaperones that promote the solubilization of aggregated proteins and the propagation of prions. ClpB and Hsp104 cooperate with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0462434f573bd13bc64137c77cf3e081
https://doi.org/10.1016/j.jmb.2016.09.003
https://doi.org/10.1016/j.jmb.2016.09.003
Autor:
Kamila B. Franke, Axel Mogk, Vanda Sunderlikova, Mario J. Avellaneda, Sander J. Tans, Bernd Bukau
Publikováno v:
Nature. 578:E23-E23
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ac8a369defc064a859788fffccd4a205
https://doi.org/10.1038/s41586-020-2017-2
https://doi.org/10.1038/s41586-020-2017-2
Autor:
Lothar Jänsch, Shady Mansour Kamal, Hyunhee Kim, Kamila B. Franke, Jasmin Jäger, Manfred Nimtz, Ute Römling, Bernd Bukau, Heinrich Lünsdorf, Janja Trček, Changhan Lee, Axel Mogk
Publikováno v:
Proceedings of the National Academy of Sciences. 115
AAA+ disaggregases solubilize aggregated proteins and confer heat tolerance to cells. Their disaggregation activities crucially depend on partner proteins, which target the AAA+ disaggregases to protein aggregates while concurrently stimulating their
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bbb3b0d885fe55837617b3f1b18b22a
https://doi.org/10.1073/pnas.1712051115
https://doi.org/10.1073/pnas.1712051115
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
Publikováno v:
Frontiers in Molecular Biosciences
The members of the hexameric AAA+ disaggregase of E. coli and S. cerevisiae, ClpB and Hsp104, cooperate with the Hsp70 chaperone system in the solubilization of aggregated proteins. Aggregate solubilization relies on a substrate threading activity of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5df3e933521b51d53640584ba5d08c00
https://pubmed.ncbi.nlm.nih.gov/28275610
https://pubmed.ncbi.nlm.nih.gov/28275610
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
Autor:
Femke I. Kraas, Mattia Bosello, Thomas A. Knappe, Mohamed A. Marahiel, Xiulan Xie, Tobias W. Giessen, Kamila B. Franke, Uwe Linne
Publikováno v:
Journal of Natural Products. 75:905-914
In this study we report the isolation, structure elucidation, and biosynthesis of mirubactin (1), a siderophore containing an unprecedented chemical functionality in natural products, namely, an O-acyl hydroxamic acid ester. Mirubactin represents the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5271176954a25887b359d9db4f37eed
https://doi.org/10.1021/np300046k
https://doi.org/10.1021/np300046k