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Ingo Schmitz

Researcher at Otto-von-Guericke University Magdeburg

Publications -  113
Citations -  12723

Ingo Schmitz is an academic researcher from Otto-von-Guericke University Magdeburg. The author has contributed to research in topics: Apoptosis & Fas receptor. The author has an hindex of 39, co-authored 102 publications receiving 10925 citations. Previous affiliations of Ingo Schmitz include Ruhr University Bochum & University of Erlangen-Nuremberg.

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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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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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The Role of c-FLIP in Modulation of CD95-induced Apoptosis *

Carsten Scaffidi, +3 more
- 15 Jan 1999 - 
TL;DR: It is shown that c-FLIP is expressed in two isoforms, both of which, like FADD and caspase-8, are recruited to the CD95 DISC in a stimulation-dependent fashion and inhibits CD95-mediated apoptosis.
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Differential Modulation of Apoptosis Sensitivity in CD95 Type I and Type II Cells

Carsten Scaffidi, +5 more
- 06 Aug 1999 - 
TL;DR: It is shown that a number of apoptosis-inhibiting or -inducing stimuli only affect apoptosis in type II cells, indicating that they act on the mitochondrial branch of the CD95 pathway.
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Cellular FLICE-inhibitory Protein Splice Variants Inhibit Different Steps of Caspase-8 Activation at the CD95 Death-inducing Signaling Complex

Andreas Krueger, +4 more
- 08 Jun 2001 - 
TL;DR: Results indicate that c-FLIPL induces a conformation of procaspase-8 that allows partial but not complete proteolytical processing, whereas in contrast c- FLIPS even prevents partial procaspasing-8 activation at the DISC.