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Matthias Peter

Researcher at ETH Zurich

Publications -  202
Citations -  24583

Matthias Peter is an academic researcher from ETH Zurich. The author has contributed to research in topics: Ubiquitin ligase & Cullin. The author has an hindex of 75, co-authored 192 publications receiving 21916 citations. Previous affiliations of Matthias Peter include ISREC & Swiss Institute of Bioinformatics.

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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.
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Global Mapping of the Yeast Genetic Interaction Network

Amy Hin Yan Tong, +49 more
- 06 Feb 2004 - 
TL;DR: Because digenic interactions are common in yeast, similar networks may underlie the complex genetics associated with inherited phenotypes in other organisms.
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Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis.

Marzena Bienko, +11 more
- 16 Dec 2005 - 
TL;DR: In this article, the identification of two ubiquitin (Ub)-binding domains (UBM and UBZ), which are evolutionarily conserved in all Y-family TLS polymerases (pols), is described.
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Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease.

Claudine Kraft, +3 more
- 06 Apr 2008 - 
TL;DR: It is shown that mature ribosomes are rapidly degraded by autophagy upon nutrient starvation in Saccharomyces cerevisiae, and a link between ubiquitination and the regulated degradation of mature Ribosome-associated proteins by Autophagy is suggested.
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Bni1p, a Yeast Formin Linking Cdc42p and the Actin Cytoskeleton During Polarized Morphogenesis

Marie Evangelista, +7 more
- 04 Apr 1997 - 
TL;DR: The Saccharomyces cerevisiae BNI1 gene product (Bni1p) is a member of the formin family of proteins, which participate in cell polarization, cytokinesis, and vertebrate limb formation.