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Chris Williams

Researcher at University of Groningen

Publications -  36
Citations -  6520

Chris Williams is an academic researcher from University of Groningen. The author has contributed to research in topics: Peroxisome & Peroxisomal targeting signal. The author has an hindex of 18, co-authored 36 publications receiving 5921 citations. Previous affiliations of Chris Williams include University of Amsterdam & European Bioinformatics Institute.

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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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A Conserved Cysteine Is Essential for Pex4p-dependent Ubiquitination of the Peroxisomal Import Receptor Pex5p

Chris Williams, +3 more
- 03 Aug 2007 - 
TL;DR: The results strongly suggest that Pex4p-dependent ubiquitination of Pex5p occurs on a cysteine residue, which appears to be essential for both the Pex3-dependent and the overall function of PEx5p.
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Phosphorylation of Pex11p does not regulate peroxisomal fission in the yeast Hansenula polymorpha.

Ann S. Thomas, +3 more
- 23 Jun 2015 - 
TL;DR: Peroxisomal fission in H. polymorpha is not modulated by phosphorylation of Pex11p, and mutations to the phosphorylated site do not disturb the function of P Ex11p in peroxisome fission, nor do they alter the localization of PEx11p.
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Membrane curvature during peroxisome fission requires Pex11

Łukasz Opaliński, +4 more
- 05 Jan 2011 - 
TL;DR: It is demonstrated that maintaining the amphipathic properties of Pex11‐Amph in conjunction with retaining its α‐helical structure are crucial for its function, and it is shown that mutations abolishing the membrane remodelling activity of the PEx11‐amph domain also hamper the function of full‐length Pex 11 in peroxisome fission in vivo.
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Label-Free and Real-Time Detection of Protein Ubiquitination with a Biological Nanopore

Carsten Wloka, +6 more
- 29 Mar 2017 - 
TL;DR: This work reports a fast, single-molecule, and label-free method to probe the ubiquitination of proteins employing an engineered Cytolysin A (ClyA) nanopore, and shows that ionic currents can be used to recognize mono- and polyubiquitinated forms of native proteins under physiological conditions.