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Laura Segatori

Researcher at Rice University

Publications -  59
Citations -  8761

Laura Segatori is an academic researcher from Rice University. The author has contributed to research in topics: Proteostasis & Unfolded protein response. The author has an hindex of 24, co-authored 54 publications receiving 7189 citations. Previous affiliations of Laura Segatori include University of Texas at Austin & University of Pittsburgh.

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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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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.
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Chemical and biological approaches synergize to ameliorate protein-folding diseases.

Ting Wei Mu, +6 more
- 05 Sep 2008 - 
TL;DR: In this paper, small molecule proteostasis regulators are used to enhance the capacity of the innate cellular protein homeostasis to fold mutated enzymes that would otherwise misfold and be degraded.
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Antioxidant Properties of Cerium Oxide Nanocrystals as a Function of Nanocrystal Diameter and Surface Coating

Seung Soo Lee, +7 more
- 21 Oct 2013 - 
TL;DR: This work examines the effect of nanocrystal diameter and surface coating on the reactivity of cerium oxide nanocrystals with H2O2 both in chemical solutions and in cells, suggesting that their redox cycling behavior can be preserved even when stabilized.
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Preparative expression of secreted proteins in bacteria : status report and future prospects

George Georgiou, +1 more
- 01 Oct 2005 - 
TL;DR: The expression of heterologous secreted proteins in Escherichia coli is widely employed for laboratory and preparative purposes and protein design and directed evolution approaches are beginning to be exploited for engineering of the cellular protein folding machinery to achieve further improvements in protein expression.