Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
-
Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation ; volume:16 ; number:7 ; year:2020 ; extent:23
Molecular systems biology ; 16, Heft 7 (2020) (gesamt 23)
- Creator
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Bienvenut, Willy V.
Brünje, Annika
Boyer, Jean‐Baptiste
Mühlenbeck, Jens S.
Bernal, Gautier
Lassowskat, Ines
Dian, Cyril
Linster, Eric
Trinh, Dinh-Van
Konert, Minna
Jung, Vincent
Seidel, Julian
Schyrba, Laura K.
Ivanauskaite, Aiste
Eirich, Jürgen
Hell, Rüdiger
Schwarzer, Dirk
Mulo, Paula
Wirtz, Markus
Meinnel, Thierry
Giglione, Carmela
Finkemeier, Iris
- DOI
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10.15252/msb.20209464
- URN
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urn:nbn:de:101:1-2022062810280163876131
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
01.08.2025, 7:22 AM CEST
Data provider
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Bienvenut, Willy V.
- Brünje, Annika
- Boyer, Jean‐Baptiste
- Mühlenbeck, Jens S.
- Bernal, Gautier
- Lassowskat, Ines
- Dian, Cyril
- Linster, Eric
- Trinh, Dinh-Van
- Konert, Minna
- Jung, Vincent
- Seidel, Julian
- Schyrba, Laura K.
- Ivanauskaite, Aiste
- Eirich, Jürgen
- Hell, Rüdiger
- Schwarzer, Dirk
- Mulo, Paula
- Wirtz, Markus
- Meinnel, Thierry
- Giglione, Carmela
- Finkemeier, Iris
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N-terminal acetylation can stabilize proteins independent of their ubiquitination
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Methylene blue decreases mitochondrial lysine acetylation in the diabetic heart
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Spotlight on protein N-terminal acetylation
Lysine acetylation modulates mouse sperm capacitation
Proteomics profiling asthma induced-lysine acetylation
The role of lysine acetylation in photosynthesis
Versatility of ARD1/NAA10-mediated protein lysine acetylation
Acetylproteomics analyses reveal critical features of lysine-ε-acetylation in Arabidopsis and a role of 14-3-3 protein acetylation in alkaline response
Regulation of epithelial-mesenchymal transition by protein lysine acetylation
Characterization of a novel lysine acetylation site in the N-terminal domain of the centromeric histone variant Cse4 in Saccharomyces cerevisiae
N-terminal acetylation can stabilize proteins independent of their ubiquitination
The biology of lysine acetylation integrates transcriptional programming and metabolism
Methylene blue decreases mitochondrial lysine acetylation in the diabetic heart
Histone H3 lysine 27 acetylation is altered in colon cancer
Spotlight on protein N-terminal acetylation
Lysine acetylation modulates mouse sperm capacitation
Proteomics profiling asthma induced-lysine acetylation
The role of lysine acetylation in photosynthesis
Versatility of ARD1/NAA10-mediated protein lysine acetylation
Acetylproteomics analyses reveal critical features of lysine-ε-acetylation in Arabidopsis and a role of 14-3-3 protein acetylation in alkaline response
Regulation of epithelial-mesenchymal transition by protein lysine acetylation
Characterization of a novel lysine acetylation site in the N-terminal domain of the centromeric histone variant Cse4 in Saccharomyces cerevisiae
N-terminal acetylation can stabilize proteins independent of their ubiquitination
The biology of lysine acetylation integrates transcriptional programming and metabolism
Methylene blue decreases mitochondrial lysine acetylation in the diabetic heart