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Jeroen Roelofs

Researcher at University of Kansas

Publications -  50
Citations -  10157

Jeroen Roelofs is an academic researcher from University of Kansas. The author has contributed to research in topics: Proteasome & Ubiquitin. The author has an hindex of 28, co-authored 43 publications receiving 8574 citations. Previous affiliations of Jeroen Roelofs include Kansas State University & Harvard 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.
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A proteomics approach to understanding protein ubiquitination

TL;DR: A proteomics approach to enrich, recover, and identify ubiquitin conjugates from Saccharomyces cerevisiae lysate provides a general tool for the large-scale analysis and characterization of protein ubiquitination.
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

Assembly, structure, and function of the 26S proteasome

TL;DR: The recent identification of four molecular chaperones, in addition to five previously identified chaperone, have provided mechanistic insight into how this cellular megastructure is assembled in the cell.
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Chaperone-mediated pathway of proteasome regulatory particle assembly

TL;DR: It is shown that in the yeast Saccharomyces cerevisiae three proteins are found associated with RP but not with the RP–CP holoenzyme: Nas6, Rpn14 and Hsm3 are RP chaperones, and it is shown in an accompanying study that RP assembly is templated through the Rpt C termini, apparently by their insertion into binding pockets in the CP.