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.
Papers
More filters
Journal ArticleDOI
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
TL;DR: The main stress proteins of Escherichia coli function in an ordered protein-folding reaction and this sequential mechanism of chaperone action may represent an important pathway for the folding of newly synthesized polypeptides.
Journal ArticleDOI
Mitochondrial Dynamics and Metabolic Regulation.
Timothy Wai,Thomas Langer +1 more
TL;DR: The ways in which metabolic alterations convey changes in mitochondrial morphology and how disruption of mitochondrial morphology impacts cellular and organismal metabolism are reviewed.
Journal ArticleDOI
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
TL;DR: Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro and might represent a general mechanism for the formation of protein structure in vivo.
Journal ArticleDOI
SLP‐2 is required for stress‐induced mitochondrial hyperfusion
Daniel Tondera,Stéphanie Grandemange,Alexis A. Jourdain,Mariusz Karbowski,Yves Benoît Mattenberger,Sébastien Herzig,Sandrine Da Cruz,Pascaline Clerc,Ines Raschke,Carsten Merkwirth,Sarah Ehses,Frank Krause,David C. Chan,Christiane Alexander,Christoph Ruediger Bauer,Richard J. Youle,Thomas Langer,Jean-Claude Martinou +17 more
TL;DR: It is reported that mitochondria hyperfuse and form a highly interconnected network in cells exposed to selective stresses and represents a novel adaptive pro‐survival response against stress.
Journal ArticleDOI
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.
TL;DR: The protein repair function of DnaK, GrpE and, in particular, DnaJ is likely to be part of the role of these proteins in regulation of the heat shock response.