Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Markus Deckers"'
Autor:
Karthik Mohanraj, Michal Wasilewski, Cristiane Benincá, Dominik Cysewski, Jaroslaw Poznanski, Paulina Sakowska, Zaneta Bugajska, Markus Deckers, Sven Dennerlein, Erika Fernandez‐Vizarra, Peter Rehling, Michal Dadlez, Massimo Zeviani, Agnieszka Chacinska
Publikováno v:
EMBO Molecular Medicine, Vol 11, Iss 5, Pp 1-21 (2019)
Abstract Nuclear and mitochondrial genome mutations lead to various mitochondrial diseases, many of which affect the mitochondrial respiratory chain. The proteome of the intermembrane space (IMS) of mitochondria consists of several important assembly
Externí odkaz:
https://doaj.org/article/03dc98b418614bc6bc41907e2c528d8b
Publikováno v:
Cell Stress, Vol 2, Iss 8, Pp 184-199 (2018)
Mitochondrial bioenergetics require the coordination of two different and independent genomes. Mutations in either genome will affect mitochondrial functionality and produce different sources of cellular stress. Depending on the kind of defect and st
Externí odkaz:
https://doaj.org/article/7c50b05ecbdc4268b99398193fb9a78a
Autor:
Sven Dennerlein, Silke Oeljeklaus, Daniel Jans, Christin Hellwig, Bettina Bareth, Stefan Jakobs, Markus Deckers, Bettina Warscheid, Peter Rehling
Publikováno v:
Cell Reports, Vol 12, Iss 10, Pp 1644-1655 (2015)
Cytochrome c oxidase, the terminal enzyme of the respiratory chain, is assembled from mitochondria- and nuclear-encoded subunits. The MITRAC complex represents the central assembly intermediate during this process as it receives imported subunits and
Externí odkaz:
https://doaj.org/article/63e3135124194e46bfbc60d22d254cc0
Autor:
Henning Urlaub, Sylvie Callegari, Anusha Valpadashi, Piotr Neumann, Peter Rehling, Andreas Linden, Ralf Ficner, Markus Deckers
Publikováno v:
FEBS Letters
The majority of mitochondrial proteins are nuclear encoded and imported into mitochondria as precursor proteins via dedicated translocases. The translocase of the inner membrane 22 (TIM22) is a multisubunit molecular machine specialized for the trans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c50994e81e45aea39d9546f83ab1919d
https://doi.org/10.1002/1873-3468.13978
https://doi.org/10.1002/1873-3468.13978
Autor:
Bettina Homberg, Piotr Neumann, Markus Deckers, Iwan Parfentev, Henning Urlaub, Peter Rehling, Ralf Pflanz, Ralf Ficner, Andreas Linden
Publikováno v:
Molecular and Cellular Proteomics
Molecular & Cellular Proteomics : MCP
Molecular & Cellular Proteomics : MCP
Protein interactions in mitochondria isolated from S. cerevisiae grown on glycerol or glucose medium were analyzed by XL-MS. The non-cleavable cross-linker BS3 proved suitable for elucidating differences in protein-protein interactions under both con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f92e791754840510ba595958dd2d3b9a
https://doi.org/10.1074/mcp.ra120.002028
https://doi.org/10.1074/mcp.ra120.002028
Autor:
Maya Schuldiner, Wolfgang Girzalsky, Chakraborty A, Ralf Erdmann, Radke J, Markus Deckers, Einat Zalckvar, Shirisha Nagotu
SummaryCells can regulate the abundance and composition of peroxisomes to adapt to environmental changes. In the baker’s yeast, S. cerevisiae, peroxisomes represent the only site for degradation of fatty acids. Hence, it is not surprising that grow
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0613884a98cba0b1085352655793da14
https://doi.org/10.1101/2021.05.31.446392
https://doi.org/10.1101/2021.05.31.446392
Autor:
Silke Oeljeklaus, Sven Dennerlein, Bettina Warscheid, David Pacheu-Grau, Agnieszka Chacinska, Michał Wasilewski, Ivan Bogeski, Margarita Chudenkova, Abhishek Aich, Peter Rehling, Christine S Gibhardt, Markus Deckers
Publikováno v:
Journal of Molecular Biology
The mitochondrial cytochrome c oxidase, the terminal enzyme of the respiratory chain, contains heme and copper centers for electron transfer. The conserved COX2 subunit contains the CuA site, a binuclear copper center. The copper chaperones SCO1, SCO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cedc5d1eb74a47b4e1f81912c8fe99e
https://hdl.handle.net/21.11116/0000-0005-B6AE-A21.11116/0000-0005-B6B0-6
https://hdl.handle.net/21.11116/0000-0005-B6AE-A21.11116/0000-0005-B6B0-6
Publikováno v:
Cell Stress, Vol 2, Iss 8, Pp 184-199 (2018)
Cell Stress
Cell Stress
Mitochondrial bioenergetics require the coordination of two different and independent genomes. Mutations in either genome will affect mitochondrial functionality and produce different sources of cellular stress. Depending on the kind of defect and st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4df89ac7e9f55e8871da5db2edc0ef2
https://doi.org/10.15698/cst2018.07.147
https://doi.org/10.15698/cst2018.07.147
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1868:119133
The respiratory chain, embedded in the inner mitochondrial membrane, is organized as a network of individual complexes, as well as large supercomplex structures. In the yeast S. cerevisiae, these supercomplexes consist of a dimeric cytochrome bc1-com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7343329a5ac15df52d6b64f7922cd0b2
https://doi.org/10.1016/j.bbamcr.2021.119133
https://doi.org/10.1016/j.bbamcr.2021.119133
Autor:
Christof Lenz, Markus Deckers, Peter Rehling, Daniel C. Jans, Christian Schulz, Tobias Müller, Sylvie Callegari, Henning Urlaub, Stefan Jakobs, Felipe Opazo, Mirjam Wissel, Silvio O. Rizzoli
Publikováno v:
Journal of Molecular Biology
Mitochondrial membrane proteins with internal targeting signals are inserted into the inner membrane by the carrier translocase (TIM22 complex). For this, precursors have to be initially directed from the TOM complex in the outer mitochondrial membra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9f99ecdc8868e14f501f499e7ac182a
https://hdl.handle.net/21.11116/0000-0003-A038-921.11116/0000-0003-E3CA-921.11116/0000-0003-E3CB-821.11116/0000-0003-E3CC-7
https://hdl.handle.net/21.11116/0000-0003-A038-921.11116/0000-0003-E3CA-921.11116/0000-0003-E3CB-821.11116/0000-0003-E3CC-7