Literature DB >> 34985692

Indirect Methods To Measure Unfolded Proteins In Living Cells Using Fluorescent Proteins.

Elisabet Navarro-Tapia1, Roberto Pérez-Torrado2.   

Abstract

In the study of the unfolded protein response pathway, it is essential to determine the amount of unfolded proteins that the cell is accumulating. Besides being essential it is one of the most challenging technique because of the difficulty to detect unfolded proteins without producing protein denaturation with the method itself. Thus, indirect methods became very useful as the use of fluorescent proteins. In this chapter, we present some of the most used methods to indirectly measure protein folding in living cells using fluorescent proteins.
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Endoplasmic reticulum stress; Fluorescent proteins; Indirect method; Unfolded protein response

Mesh:

Substances:

Year:  2022        PMID: 34985692     DOI: 10.1007/978-1-0716-1732-8_3

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  24 in total

1.  Tandem fluorescent protein timers for in vivo analysis of protein dynamics.

Authors:  Anton Khmelinskii; Philipp J Keller; Anna Bartosik; Matthias Meurer; Joseph D Barry; Balca R Mardin; Andreas Kaufmann; Susanne Trautmann; Malte Wachsmuth; Gislene Pereira; Wolfgang Huber; Elmar Schiebel; Michael Knop
Journal:  Nat Biotechnol       Date:  2012-06-24       Impact factor: 54.908

2.  IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA.

Authors:  Marcella Calfon; Huiqing Zeng; Fumihiko Urano; Jeffery H Till; Stevan R Hubbard; Heather P Harding; Scott G Clark; David Ron
Journal:  Nature       Date:  2002-01-03       Impact factor: 49.962

3.  Approaches to imaging unfolded secretory protein stress in living cells.

Authors:  Patrick Lajoie; Elena N Fazio; Erik L Snapp
Journal:  Endoplasmic Reticulum Stress Dis       Date:  2014-01-01

4.  Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions.

Authors:  Philip I Merksamer; Ala Trusina; Feroz R Papa
Journal:  Cell       Date:  2008-11-20       Impact factor: 41.582

5.  Homeostatic adaptation to endoplasmic reticulum stress depends on Ire1 kinase activity.

Authors:  Claudia Rubio; David Pincus; Alexei Korennykh; Sebastian Schuck; Hana El-Samad; Peter Walter
Journal:  J Cell Biol       Date:  2011-03-28       Impact factor: 10.539

6.  Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response.

Authors:  Sebastián Bernales; Kent L McDonald; Peter Walter
Journal:  PLoS Biol       Date:  2006-11       Impact factor: 8.029

7.  Development of a fluorescent reporter system for monitoring ER stress in Chinese hamster ovary cells and its application for therapeutic protein production.

Authors:  Gargi Roy; Shu Zhang; Lina Li; Eileen Higham; Herren Wu; Marcello Marelli; Michael A Bowen
Journal:  PLoS One       Date:  2017-08-23       Impact factor: 3.240

8.  Ethanol Effects Involve Non-canonical Unfolded Protein Response Activation in Yeast Cells.

Authors:  Elisabet Navarro-Tapia; Roberto Pérez-Torrado; Amparo Querol
Journal:  Front Microbiol       Date:  2017-03-07       Impact factor: 5.640

9.  Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response.

Authors:  Sebastian Schuck; William A Prinz; Kurt S Thorn; Christiane Voss; Peter Walter
Journal:  J Cell Biol       Date:  2009-11-09       Impact factor: 10.539

10.  A thiol probe for measuring unfolded protein load and proteostasis in cells.

Authors:  Moore Z Chen; Nagaraj S Moily; Jessica L Bridgford; Rebecca J Wood; Mona Radwan; Trevor A Smith; Zhegang Song; Ben Zhong Tang; Leann Tilley; Xiaohong Xu; Gavin E Reid; Mahmoud A Pouladi; Yuning Hong; Danny M Hatters
Journal:  Nat Commun       Date:  2017-09-07       Impact factor: 14.919

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