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Dieter Willbold

Researcher at Forschungszentrum Jülich

Publications -  461
Citations -  21144

Dieter Willbold is an academic researcher from Forschungszentrum Jülich. The author has contributed to research in topics: Peptide & Medicine. The author has an hindex of 48, co-authored 426 publications receiving 17245 citations. Previous affiliations of Dieter Willbold include University of Düsseldorf & Leibniz Institute for Neurobiology.

Papers
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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

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.
Journal ArticleDOI

Fibril structure of amyloid-β(1-42) by cryo-electron microscopy.

Lothar Gremer, +18 more
- 06 Oct 2017 - 
TL;DR: The complete structure of an Aβ(1–42) fibril composed of two intertwined protofilaments determined by cryo–electron microscopy (cryo-EM) and provides a structural basis for understanding the effect of several disease-causing and disease-preventing mutations.
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Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease.

Heinrich Sticht, +7 more
- 01 Oct 1995 - 
TL;DR: A similar secondary structure is suggested for the aggregation part of prions, the postulated causative agents of the transmissible spongiform encephalopathy, to be remarkably similar to the sequence of the helical part of human A4-(1-40)-peptide.