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Overlap of NatA and IAP substrates implicates N-terminal acetylation in protein stabilization

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Müller,  Franziska
Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Friese,  Alexandra
Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Pathe,  Claudio
Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Cardoso da Silva,  Richard
Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Bravo Rodriguez,  Kenny
Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Musacchio,  Andrea
Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Bange,  Tanja
Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Müller, F., Friese, A., Pathe, C., Cardoso da Silva, R., Bravo Rodriguez, K., Musacchio, A., et al. (2021). Overlap of NatA and IAP substrates implicates N-terminal acetylation in protein stabilization. Science Advances, 7(3): eabc8590, pp. 1-13. doi:10.1126/sciadv.abc8590.


Cite as: https://hdl.handle.net/21.11116/0000-0007-E781-2
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