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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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Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides.

TL;DR: It is shown by crosslinking that the chaperone DnaJ binds nascent ribosome-bound polypeptide chains as short as 55 residues, which helps clarify the stage in its biogenesis at which the folding protein makes first contact with these components.
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The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m‐AAA protease

TL;DR: An overlapping substrate specificity of the subunits of the m‐AAA protease is revealed and this results explain the impaired assembly of respiratory chain complexes by defects in expression of intron‐containing genes in mitochondria lacking m‐ AAA protease.
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CerS6-Derived Sphingolipids Interact with Mff and Promote Mitochondrial Fragmentation in Obesity.

TL;DR: The experiments reveal an unprecedented specificity of sphingolipid signaling depending on specific synthesizing enzymes, provide a mechanistic link between hepatic lipid deposition and mitochondrial fragmentation in obesity, and define the CerS6-derived sphingoipid/Mff interaction as a therapeutic target for metabolic diseases.
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TRIAP1/PRELI Complexes Prevent Apoptosis by Mediating Intramitochondrial Transport of Phosphatidic Acid

TL;DR: A complex of the p53-regulated protein TRIAP1 (p53CSV) and PRELI in the mitochondrial intermembrane space (IMS) is identified, which ensures the accumulation of CL in mitochondria, highlighting the importance of the CL content of mitochondrial membranes in apoptosis.
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DNAJC19, a mitochondrial cochaperone associated with cardiomyopathy, forms a complex with prohibitins to regulate cardiolipin remodeling.

TL;DR: The experiments suggest that PHB/DNAJC19 membrane domains regulate cardiolipin remodeling by tafazzin and explain similar clinical symptoms in two inherited cardiomyopathies by an impaired cardiolIPin metabolism in mitochondrial membranes.