scispace - formally typeset
C

Carsten Sachse

Researcher at Ernst Ruska Centre

Publications -  86
Citations -  11217

Carsten Sachse is an academic researcher from Ernst Ruska Centre. The author has contributed to research in topics: Autophagy & Protein structure. The author has an hindex of 36, co-authored 76 publications receiving 9117 citations. Previous affiliations of Carsten Sachse include University of Jena & Howard Hughes Medical Institute.

Papers
More filters
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 (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

An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation

Florian K. M. Schur, +10 more
- 29 Jul 2016 - 
TL;DR: Improved cryo-electron tomography and subtomogram averaging show how HIV maturation inhibitor drugs may work and suggest that MIs prevent CA-SP1 cleavage by stabilizing the structure, and MI resistance develops by destabilizing CA- SP1.
Journal ArticleDOI

Aβ(1-40) Fibril Polymorphism Implies Diverse Interaction Patterns in Amyloid Fibrils

Jessica Meinhardt, +6 more
- 27 Feb 2009 - 
TL;DR: The observed fibril polymorphism implies that amyloid formation can lead, for the same polypeptide sequence, to many different patterns of inter- or intra-residue interactions.
Journal ArticleDOI

Comparison of Alzheimer Aβ(1–40) and Aβ(1–42) amyloid fibrils reveals similar protofilament structures

Matthias Schmidt, +5 more
- 24 Nov 2009 - 
TL;DR: A model for the arrangement of peptides within the Aβ(1–42) fibril is described, revealing that they share an axial twofold symmetry and a similar protofilament structure.