J
Johannes M. Herrmann
Researcher at Kaiserslautern University of Technology
Publications - 208
Citations - 12392
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 receiving 10940 citations. Previous affiliations of Johannes M. Herrmann include Schrödinger & Ludwig Maximilian University of Munich.
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Journal ArticleDOI
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.
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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.
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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.
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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.
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Oxa1p, an essential component of the N-tail protein export machinery in mitochondria
TL;DR: It is demonstrated here that imported nuclear encoded proteins physically interact with Oxa1p and depend on Oxa2p for efficient export of their N termini to the intermembrane space, including the fully synthesized pCoxII and CoxIII species.