
Gottfried J. Palm
Articles
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Nov 3, 2024 |
nature.com | Carlos Moreno-Yruela |Sabrina Schulze |Gottfried J. Palm |Nancy Wang |Dianna Hocking |Leila Jebeli | +5 more
AbstractClassical Zn2+-dependent deac(et)ylases play fundamental regulatory roles in life and are well characterized in eukaryotes regarding their structures, substrates and physiological roles. In bacteria, however, classical deacylases are less well understood. We construct a Generalized Profile (GP) and identify thousands of uncharacterized classical deacylases in bacteria, which are grouped into five clusters.
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Nov 3, 2024 |
nature.com | Carlos Moreno-Yruela |Sabrina Schulze |Gottfried J. Palm |Nancy Wang |Dianna Hocking |Leila Jebeli | +5 more
AbstractClassical Zn2+-dependent deac(et)ylases play fundamental regulatory roles in life and are well characterized in eukaryotes regarding their structures, substrates and physiological roles. In bacteria, however, classical deacylases are less well understood. We construct a Generalized Profile (GP) and identify thousands of uncharacterized classical deacylases in bacteria, which are grouped into five clusters.
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Jul 1, 2024 |
onlinelibrary.wiley.com | Thomas E. Bayer |Gottfried J. Palm |Leona Berndt |Hannes Meinert
Since the introduction of synthetic polymers, plastics have set application benchmarks as high-performing materials in almost all aspects of everyday life—from food containers and clothing to medical appliances and construction.1 While advantages including (chemical) resistance, durability, and low cost raised mass production from 1.5 million tons in 1950 to 390 million tons in 2021,2 these features contribute to today's failing disposal and recycling plans for synthetic polymers.3-6 In 2015,...
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Jun 27, 2024 |
mdpi.com | Felix Potlitz |Gottfried J. Palm |Michael Lammers |Anja Bodtke
All articles published by MDPI are made immediately available worldwide under an open access license. No special permission is required to reuse all or part of the article published by MDPI, including figures and tables. For articles published under an open access Creative Common CC BY license, any part of the article may be reused without permission provided that the original article is clearly cited. For more information, please refer to https://www.mdpi.com/openaccess.
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Feb 22, 2024 |
nature.com | Sabrina Schulze |Gottfried J. Palm |Susanne Sievers |Ulrich Baumann |Karin Schnetz
AbstractThe Escherichia coli TetR-related transcriptional regulator RutR is involved in the coordination of pyrimidine and purine metabolism. Here we report that lysine acetylation modulates RutR function. Applying the genetic code expansion concept, we produced site-specifically lysine-acetylated RutR proteins. The crystal structure of lysine-acetylated RutR reveals how acetylation switches off RutR-DNA-binding. We apply the genetic code expansion concept in E.
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