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Thorsten Hoppe

Researcher at University of Cologne

Publications -  97
Citations -  12682

Thorsten Hoppe is an academic researcher from University of Cologne. The author has contributed to research in topics: Proteostasis & Ubiquitin ligase. The author has an hindex of 37, co-authored 88 publications receiving 10626 citations. Previous affiliations of Thorsten Hoppe include Max Planck Society & Ludwig Maximilian University of Munich.

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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.
Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Daniel J. Klionsky, +2983 more
- 08 Feb 2021 - 
TL;DR: In this article, the authors present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes.
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A Novel Ubiquitination Factor, E4, Is Involved in Multiubiquitin Chain Assembly

Manfred Koegl, +5 more
- 05 Mar 1999 - 
TL;DR: It is shown that efficient multiubiquitination needed for proteasomal targeting of a model substrate requires an additional conjugation factor, named E4, which defines a novel protein family that includes two human members and the regulatory protein NOSA from Dictyostelium required for fruiting body development.
Journal ArticleDOI

Activation of a Membrane-Bound Transcription Factor by Regulated Ubiquitin/Proteasome-Dependent Processing

Thorsten Hoppe, +5 more
- 01 Sep 2000 - 
TL;DR: Intriguingly, proteasome-dependent processing of SPT23 is regulated by fatty acid pools, suggesting that the precursor itself or interacting partners are sensors of membrane composition or fluidity.
Journal ArticleDOI

Mobilization of Processed, Membrane-Tethered SPT23 Transcription Factor by CDC48UFD1/NPL4, a Ubiquitin-Selective Chaperone

Michael Rape, +5 more
- 30 Nov 2001 - 
TL;DR: It is shown that SPT23 dimerizes prior to processing and that the processed molecule, p90, retains its ubiquitin modification and initially remains tethered to its unprocessed, membrane-bound SPT 23 partner.