Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Ines Lassowskat"'
Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation
Autor:
Willy V Bienvenut, Annika Brünje, Jean‐Baptiste Boyer, Jens S Mühlenbeck, Gautier Bernal, Ines Lassowskat, Cyril Dian, Eric Linster, Trinh V Dinh, Minna M Koskela, Vincent Jung, Julian Seidel, Laura K Schyrba, Aiste Ivanauskaite, Jürgen Eirich, Rüdiger Hell, Dirk Schwarzer, Paula Mulo, Markus Wirtz, Thierry Meinnel, Carmela Giglione, Iris Finkemeier
Publikováno v:
Molecular Systems Biology, Vol 16, Iss 7, Pp n/a-n/a (2020)
Abstract Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and ε‐lysine acetylation (KA) are known to be catalyzed by distinct families o
Externí odkaz:
https://doaj.org/article/d26b41bab41445bf8117bc4fba9d0b24
Autor:
Magdalena Füßl, Ines Lassowskat, Guillaume Née, Minna M. Koskela, Annika Brünje, Priyadarshini Tilak, Jonas Giese, Dario Leister, Paula Mulo, Dirk Schwarzer, Iris Finkemeier
Publikováno v:
Frontiers in Plant Science, Vol 9 (2018)
The reversible acetylation of lysine residues is catalyzed by the antagonistic action of lysine acetyltransferases and deacetylases, which can be considered as master regulators of their substrate proteins. Lysine deacetylases, historically referred
Externí odkaz:
https://doaj.org/article/18de750a09c44f868dc962cf01cbde3d
Publikováno v:
Proteomes, Vol 1, Iss 3, Pp 254-274 (2013)
Phosphorylation is an important post-translational protein modification with regulatory roles in diverse cellular signaling pathways. Despite recent advances in mass spectrometry, the detection of phosphoproteins involved in signaling is still challe
Externí odkaz:
https://doaj.org/article/fcb201dae5e8400aadc61c787f28cf8c
Autor:
José Luis Carrasco, María José Castelló, Kai Naumann, Ines Lassowskat, Marisa Navarrete-Gómez, Dierk Scheel, Pablo Vera
Publikováno v:
PLoS ONE, Vol 9, Iss 3, p e90734 (2014)
Arabidopsis thaliana DBP1 belongs to the plant-specific family of DNA-binding protein phosphatases. Although recently identified as a novel host factor mediating susceptibility to potyvirus, little is known about DBP1 targets and partners and the mol
Externí odkaz:
https://doaj.org/article/9507fb0dfc1e4e8ba3c1784c5a99cf70
Autor:
Martin H. Spalding, Amanda P. Cavanagh, Christopher M. Harvey, Donald R. Ort, Vijayata Singh, Steven C. Huber, Sang Yeol Kim, Jonas Giese, Iris Finkemeier, Ines Lassowskat
Publikováno v:
Proceedings of the National Academy of Sciences. 116:18723-18731
Arabidopsis Rubisco activase (Rca) is phosphorylated at threonine-78 (Thr78) in low light and in the dark, suggesting a potential regulatory role in photosynthesis, but this has not been directly tested. To do so, we transformed an rca -knockdown mut
Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation
Autor:
Julian Seidel, Annika Brünje, Gautier Bernal, Dirk Schwarzer, Iris Finkemeier, Laura K Schyrba, Eric Linster, Thierry Meinnel, Ines Lassowskat, Paula Mulo, Jürgen Eirich, Jens Stephan Mühlenbeck, Minna M. Koskela, Aiste Ivanauskaite, Jean-Baptiste Boyer, Markus Wirtz, Trinh V. Dinh, Carmela Giglione, Willy V. Bienvenut, Vincent A. Jung, Cyril Dian, Rüdiger Hell
Publikováno v:
Molecular Systems Biology
Molecular Systems Biology, 2020, 16 (7), pp.e9464. ⟨10.15252/msb.20209464⟩
Molecular Systems Biology, EMBO Press, 2020, 16 (7), pp.e9464. ⟨10.15252/msb.20209464⟩
Molecular Systems Biology, Vol 16, Iss 7, Pp n/a-n/a (2020)
Molecular Systems Biology, 2020, 16 (7), pp.e9464. ⟨10.15252/msb.20209464⟩
Molecular Systems Biology, EMBO Press, 2020, 16 (7), pp.e9464. ⟨10.15252/msb.20209464⟩
Molecular Systems Biology, Vol 16, Iss 7, Pp n/a-n/a (2020)
Protein acetylation is a highly frequent protein modification. However, comparatively little is known about its enzymatic machinery. N‐α‐acetylation (NTA) and ε‐lysine acetylation (KA) are known to be catalyzed by distinct families of enzymes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ce91c5e79b99a8e8008cc1856cb5060
https://hal.science/hal-02900691/file/MSB-16-e9464.pdf
https://hal.science/hal-02900691/file/MSB-16-e9464.pdf
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2139
Acetylation of lysine side chains at their ε-amino group is a reversible posttranslational modification (PTM), which can affect diverse protein functions. Lysine acetylation was first described on histones, and nowadays gains more and more attention
Publikováno v:
Methods in Molecular Biology ISBN: 9781071605271
Acetylation of lysine side chains at their e-amino group is a reversible posttranslational modification (PTM), which can affect diverse protein functions. Lysine acetylation was first described on histones, and nowadays gains more and more attention
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a1cd94001ad0c16b09998ef58b6a2a17
https://doi.org/10.1007/978-1-0716-0528-8_18
https://doi.org/10.1007/978-1-0716-0528-8_18
Autor:
Iris Finkemeier, Ines Lassowskat, Fabian Hosp, Matthew A. Hannah, Sven Christian, David De Vleesschauwer, Henning Redestig, Valeria Santoro, Matthias Mann, Daniela Fliegner
Publikováno v:
Mitochondrion
Cellular signaling pathways are regulated in a highly dynamic fashion in order to quickly adapt to distinct environmental conditions. Acetylation of lysine residues represents a central process that orchestrates cellular metabolism and signaling. In
Autor:
Sang Yeol, Kim, Christopher M, Harvey, Jonas, Giese, Ines, Lassowskat, Vijayata, Singh, Amanda P, Cavanagh, Martin H, Spalding, Iris, Finkemeier, Donald R, Ort, Steven C, Huber
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 116(37)
Arabidopsis Rubisco activase (Rca) is phosphorylated at threonine-78 (Thr78) in low light and in the dark, suggesting a potential regulatory role in photosynthesis, but this has not been directly tested. To do so, we transformed an rca-knockdown muta