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Marius K. Lemberg

Researcher at Heidelberg University

Publications -  71
Citations -  9755

Marius K. Lemberg is an academic researcher from Heidelberg University. The author has contributed to research in topics: Endoplasmic reticulum & Signal peptide peptidase. The author has an hindex of 32, co-authored 64 publications receiving 8750 citations. Previous affiliations of Marius K. Lemberg include École Polytechnique Fédérale de Lausanne & Laboratory of Molecular Biology.

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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Identification of signal peptide peptidase, a presenilin-type aspartic protease.

TL;DR: Human SPP is identified as a polytopic membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases that promote intramembrane proteolysis to release biologically important peptides.
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Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets

TL;DR: Evidence is provided that after cleavage by signal peptidase, the signal peptide is further processed by the intramembrane‐cleaving protease SPP that promotes the release of core protein from the ER membrane, then free for subsequent trafficking to lipid droplets.
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The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking

TL;DR: In this article, it was shown that PARL cleaves human Pink1, which is implicated in Parkinson's disease, within its conserved membrane anchor, leading to accumulation of the Pink1 precursor.
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Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis.

TL;DR: It is proposed that signal peptides require flexibility in the lipid bilayer to exhibit an accessible peptide bond for intramembrane proteolysis.