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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AAA proteases: cellular machines for degrading membrane proteins.
TL;DR: AAA proteases are a conserved class of ATP-dependent proteases that mediate the degradation of membrane proteins in bacteria, mitochondria and chloroplasts and form a membrane-integrated quality-control system.
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Mitochondrial lipid trafficking.
TL;DR: The recent identification of membrane-tethering complexes and lipid-transfer proteins in mitochondria now provides the first insight into the mechanisms of these transport processes, which are of fundamental importance for mitochondrial activities and cell homeostasis.
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Intramitochondrial Transport of Phosphatidic Acid in Yeast by a Lipid Transfer Protein
Melanie Connerth,Takashi Tatsuta,Mathias Haag,Till Klecker,Benedikt Westermann,Thomas Langer,Thomas Langer +6 more
TL;DR: Intramitochondrial lipid trafficking may involve a regulatory feedback mechanism that limits the accumulation of cardiolipin in mitochondria and is identified as a lipid transfer protein that can shuttle phosphatidic acid between mitochondrial membranes.
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Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease
TL;DR: It is shown that Yme1 senses the folding state of solvent-exposed domains and specifically degrades unfolded membrane proteins and suggests that the AAA domains of other AAA proteins may have a similar function.
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Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface.
Klaus Leonhard,Bernard Guiard,Giovanna Pellecchia,Alexander Tzagoloff,Walter Neupert,Thomas Langer +5 more
TL;DR: It is demonstrated that a model substrate polypeptide containing hydrophilic domains at both sides of the membrane can be completely degraded by either of the AAA proteases, if solvent-exposed domains are in an unfolded state.