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Andreas Brech

Researcher at Oslo University Hospital

Publications -  135
Citations -  28972

Andreas Brech is an academic researcher from Oslo University Hospital. The author has contributed to research in topics: Endosome & Autophagy. The author has an hindex of 58, co-authored 126 publications receiving 25535 citations. Previous affiliations of Andreas Brech include University of Oslo.

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Guidelines for the use and interpretation of assays for monitoring autophagy

Daniel J. Klionsky, +1287 more
- 01 Apr 2012 - 
TL;DR: These guidelines are presented for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy 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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p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy

TL;DR: It is demonstrated that the previously reported aggresome-like induced structures containing ubiquitinated proteins in cytosolic bodies are dependent on p62 for their formation and p62 is required both for the formation and the degradation of polyubiquitin-containing bodies by autophagy.

p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates

TL;DR: In this article, the authors showed that the polyubiquitin-binding protein p62/SQSTM1 is degraded by autophagy by using a 22-residue sequence of p62 containing an evolutionarily conserved motif.
Journal ArticleDOI

p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death

TL;DR: In this article, the polyubiquitin-binding protein p62/SQSTM1 has been shown to be involved in linking polyUBiquitinated protein aggregates to the autophagy machinery.
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EEA1 links PI(3)K function to Rab5 regulation of endosome fusion

TL;DR: The identification of EEA1 as a direct Rab5 effector provides a molecular link between PI(3)K and Rab5, and its restricted distribution to early endosomes indicates that EEA 1 may confer directionality to Rab5-dependent endocytic transport.