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Peter J. Roach

Researcher at Indiana University

Publications -  213
Citations -  19123

Peter J. Roach is an academic researcher from Indiana University. The author has contributed to research in topics: Glycogen synthase & Glycogen. The author has an hindex of 66, co-authored 212 publications receiving 17904 citations. Previous affiliations of Peter J. Roach include Purdue University & Indiana University – Purdue University Indianapolis.

Papers
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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.
Journal ArticleDOI

Glycogen and its metabolism: some new developments and old themes.

Peter J. Roach, +3 more
- 01 Feb 2012 - 
TL;DR: Glycogen is a branched polymer of glucose that acts as a store of energy in times of nutritional sufficiency for utilization in time of need as mentioned in this paper, and much is known about its regulation by hormones such as insulin, glucagon and adrenaline (epinephrine).
Journal ArticleDOI

Glycogen and its Metabolism

Peter J. Roach
- 28 Feb 2002 - 
TL;DR: Though the number of enzymes directly involved in the metabolism of glycogen is quite small, many more proteins act indirectly in a regulatory capacity and, with some exceptions, mutations in the regulatory proteins appear to cause a more subtle phenotypic change.
Journal ArticleDOI

Multisite and hierarchal protein phosphorylation

Peter J. Roach
- 05 Aug 1991 - 
TL;DR: Multisite phosphorylation is a prevalent form of protein modification whose full implications are just beginning to be understood and allow more intricate regulatory circuits to operate.
Journal ArticleDOI

Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3.

C. J. Fiol, +4 more
- 15 Oct 1987 - 
TL;DR: The results provide a molecular basis to explain the synergistic action of casein kinase II and GSK-3 that is also observed with native glycogen synthase and emphasizes how protein recognition sites in some cellular targets may have to be formed post-translationally.