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Matthias Gaestel

Researcher at Hannover Medical School

Publications -  294
Citations -  31016

Matthias Gaestel is an academic researcher from Hannover Medical School. The author has contributed to research in topics: Protein kinase A & Kinase. The author has an hindex of 75, co-authored 281 publications receiving 28369 citations. Previous affiliations of Matthias Gaestel include Martin Luther University of Halle-Wittenberg & Tufts University.

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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

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

Small heat shock proteins are molecular chaperones

Ursula Jakob, +3 more
- 25 Jan 1993 - 
TL;DR: It is shown that all sHsps investigated act as molecular chaperones in these folding reactions and at stoichiometric amounts they maximally prevent the aggregation of citrate synthase and alpha-glucosidase under heat shock conditions and stabilize the proteins.
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The p38 MAP kinase pathway signals for cytokine-induced mRNA stabilization via MAP kinase-activated protein kinase 2 and an AU-rich region-targeted mechanism

Reinhard Winzen, +9 more
- 15 Sep 1999 - 
TL;DR: Findings indicate that the p38 MAP kinase pathway contributes to cytokine/stress‐induced gene expression by stabilizing mRNAs through an MK2‐dependent, ARE‐targeted mechanism.
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Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation

Monika Ehrnsperger, +3 more
- 15 Jan 1997 - 
TL;DR: The task of sHsps in this context is to efficiently trap a large number of unfolding proteins in a folding‐competent state and thus create a reservoir of non‐native proteins for an extended period of time, allowing refolding after restoration of physiological conditions in cooperation with other chaperones.