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Robert Layfield

Researcher at University of Nottingham

Publications -  142
Citations -  17888

Robert Layfield is an academic researcher from University of Nottingham. The author has contributed to research in topics: Ubiquitin & Ubiquitin binding. The author has an hindex of 45, co-authored 132 publications receiving 15092 citations. Previous affiliations of Robert Layfield include Queen's University & Nottingham Trent University.

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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

Disassociation between the effects of amino acids and insulin on signaling, ubiquitin ligases, and protein turnover in human muscle.

Paul L. Greenhaff, +10 more
- 01 Sep 2008 - 
TL;DR: Increasing AA and insulin availability causes changes in anabolic signaling and amounts of enzymes of the ubiquitin-proteasome pathway, which cannot be easily reconciled with observed effects on MPS or LPB.
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α-Synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome

George K. Tofaris, +2 more
- 30 Nov 2001 - 
TL;DR: It is found that in vitro, unmodified α‐synuclein can be directly degraded by the 20S proteasome, suggesting an ubiquitin‐independent mechanism of proteasomal degradation for α‐ synuclein and other natively unfolded proteins.