Johannes M. Herrmann
Kaiserslautern University of Technology
228 Papers
1.3K Citations
Johannes M. Herrmann is an academic researcher from Kaiserslautern University of Technology. The author has contributed to research in topics: Mitochondrion & Intermembrane space. The author has an hindex of 62, co-authored 187 publications. Previous affiliations of Johannes M. Herrmann include Schrödinger & Ludwig Maximilian University of Munich.
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Papers
Translocation of proteins into mitochondria.
TL;DR: This review summarizes the present knowledge on the import and sorting of mitochondrial precursor proteins, with a special emphasis on unresolved questions and topics of current research.
1.4K
A disulfide relay system in the intermembrane space of mitochondria that mediates protein import.
Nikola Mesecke,Nadia Terziyska,Christian Kozany,Frank Baumann,Walter Neupert,Kai Hell,Johannes M. Herrmann +6 more
TL;DR: It is suggested that the existence of a disulfide exchange system in the IMS is unexpected in view of the free exchange of metabolites between IMS and cytosol via porin channels, and reflects the evolutionary origin of the I MS from the periplasmic space of the prokaryotic ancestors of mitochondria.
577
COPII–cargo interactions direct protein sorting into ER-derived transport vesicles
TL;DR: The results indicate that cargo packaging signals and soluble cargo adaptors are recognized by a recruitment complex comprising Sar1–GTP and Sec23/24.
436
Quality control of the mitochondrial proteome.
TL;DR: To ensure proper mitochondrial function, cells use multiple mechanisms of quality control that survey mitochondrial protein biogenesis, import and folding, and allow mitochondria to adapt to the changing needs as well as to respond to stresses that compromise proteostasis.
323
AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria.
Klaus Leonhard,Johannes M. Herrmann,Rosemary A. Stuart,Gertrud Mannhaupt,Walter Neupert,Thomas Langer +5 more
TL;DR: Two AAA proteases with their catalytic sites on opposite membrane surfaces constitute a novel proteolytic system for the degradation of membrane proteins in mitochondria.
287