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Reinhild Prange

Researcher at University of Mainz

Publications -  48
Citations -  7338

Reinhild Prange is an academic researcher from University of Mainz. The author has contributed to research in topics: Hepatitis B virus & Endoplasmic reticulum. The author has an hindex of 26, co-authored 46 publications receiving 6750 citations. Previous affiliations of Reinhild Prange include Max Planck Society.

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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.
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Novel transmembrane topology of the hepatitis b virus envelope proteins

TL;DR: It is demonstrated that all envelope proteins synthesized in transfected cells or in a cell‐free system adopt more than one transmembrane orientation.
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Hepatitis B Virus Maturation Is Sensitive to Functional Inhibition of ESCRT-III, Vps4, and γ2-Adaptin

TL;DR: It is demonstrated that HBV exploits the MVB machinery with the aid of γ2-adaptin, and the effects of its overexpression in virus-replicating cells are examined, hinting at different export routes used by viral and subviral particles.
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The ras-related mouse ypt1 protein can functionally replace the YPT1 gene product in yeast.

TL;DR: It is suggested that different parts of the yeast YPT1 protein are required for the interaction with cellular targets and that these essential parts are conserved in the mammalian ypt1 protein.
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A carboxyl-terminal cysteine residue is required for palmitic acid binding and biological activity of the ras-related yeast YPT1 protein.

TL;DR: The Saccharomyces cerevisiae YPT1 gene codes for a ras‐like, guanine nucleotide‐binding protein which is essential for cell viability and it was found that as long as one of the cysteines was retained, the protein was fully functional.