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Jörg Höhfeld

Researcher at University of Bonn

Publications -  62
Citations -  16059

Jörg Höhfeld is an academic researcher from University of Bonn. The author has contributed to research in topics: Chaperone (protein) & Ubiquitin ligase. The author has an hindex of 38, co-authored 62 publications receiving 14150 citations. Previous affiliations of Jörg Höhfeld include University of Rochester.

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Journal ArticleDOI

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

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.
Journal ArticleDOI

CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation.

TL;DR: It is demonstrated that CHIP is a bona fide ubiquitin ligase and indicated that U-box-containing proteins may comprise a new family of E3s, and a major target of the ubiquit in ligase activity ofCHIP is Hsc70 itself.
Journal ArticleDOI

Chaperone-assisted selective autophagy is essential for muscle maintenance

TL;DR: The findings reveal the importance of chaperone-assisted degradation for the preservation of cellular structures and identify muscle as a tissue that highly relies on an intact proteostasis network, thereby shedding light on diverse myopathies and aging.
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Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors.

TL;DR: Functional convergence has allowed proteins with different architectures to trigger a conserved conformational shift in Hsp70 that leads to nucleotide exchange.