T
Thomas Langer
Researcher at Max Planck Society
Publications - 253
Citations - 26029
Thomas Langer is an academic researcher from Max Planck Society. The author has contributed to research in topics: Mitochondrion & mitochondrial fusion. The author has an hindex of 82, co-authored 222 publications receiving 23219 citations. Previous affiliations of Thomas Langer include Heidelberg University & Ludwig Maximilian University of Munich.
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Journal ArticleDOI
Lipid signalling drives proteolytic rewiring of mitochondria by YME1L.
Thomas MacVicar,Yohsuke Ohba,Hendrik Nolte,Hendrik Nolte,Fiona Carola Mayer,Takashi Tatsuta,Hans-Georg Sprenger,Hans-Georg Sprenger,Barbara Lindner,Yue Zhao,Jiahui Li,Christiane J. Bruns,Marcus Krüger,Markus Habich,Jan Riemer,Robin Schwarzer,Manolis Pasparakis,Manolis Pasparakis,Sinika Henschke,Jens C. Brüning,Jens C. Brüning,Nicola Zamboni,Thomas Langer,Thomas Langer +23 more
TL;DR: The mTORC1–LIPIN1–YME1L axis is identified as a post-translational regulator of mitochondrial proteostasis at the interface between metabolism and mitochondrial dynamics under conditions such as hypoxia or starvation.
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Mitochondrial Proteases: Multifaceted Regulators of Mitochondrial Plasticity
TL;DR: Understanding the dual function of mitoproteases as regulatory and quality control enzymes will help unravel the role of mitochondrial plasticity in aging and disease.
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The Good and the Bad of Mitochondrial Breakups.
TL;DR: Recent advances in the field of mitochondrial dynamics are discussed, demonstrating cell- and tissue-specific effects of mitochondrial fragmentation on cellular metabolism, cell survival, and mitochondrial quality control.
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An Intersubunit Signaling Network Coordinates ATP Hydrolysis by m-AAA Proteases
Steffen Augustin,Florian Gerdes,Sukyeong Lee,Francis T.F. Tsai,Thomas Langer,Thomas Langer,Takashi Tatsuta +6 more
TL;DR: Coordinated ATP hydrolysis within m-AAA protease ring complexes, conserved AAA+ machines in the inner membrane of mitochondria, provides insight into how AAA+ proteins convert energy derived from ATP Hydrolysis into mechanical work.
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The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria.
TL;DR: Proteins of the Clp/Hsp100-family located in the cytosol and within mitochondria confer compartment-specific protection against heat damage to the cell, suggesting a conserved mode of action of the two proteins.