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James H. Hurley

Researcher at University of California, Berkeley

Publications -  254
Citations -  29991

James H. Hurley is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: ESCRT & Autophagy. The author has an hindex of 82, co-authored 223 publications receiving 26054 citations. Previous affiliations of James H. Hurley include California Institute for Quantitative Biosciences & University of California.

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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 (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

Molecular mechanism of multivesicular body biogenesis by ESCRT complexes

TL;DR: It is shown that ESCRT-0 forms domains of clustered cargo but does not deform membranes, which explains how the ESCRTs direct membrane budding and scission from the cytoplasmic side of the bud without being consumed in the reaction.
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Membrane budding and scission by the ESCRT machinery: it's all in the neck

TL;DR: The endosomal sorting complexes required for transport (ESCRTs) catalyse one of the most unusual membrane remodelling events in cell biology, which is crucial for many processes, including the biogenesis of multivesicular bodies, viral budding, cytokinesis and, probably, autophagy.
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Crystal structure of the Cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester

TL;DR: The structure of the second activator-binding domain of PKC delta has been determined in complex with phorbol 13-acetate, which binds in a groove between two pulled-apart beta strands at the tip of the domain, explaining how the activator promotes insertion of PKCs into membranes.