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Sequestration of Proteins in Stress Granules Relies on the In-Cell but Not the <i>In Vitro</i> Folding Stability

Nirnay Samanta, Sara S. Ribeiro, Mailin Becker, Émeline Laborie, Roland Pollak, Štěpán Timr, Fabio Sterpone, Simon Ebbinghaus

2021Journal of the American Chemical Society28 citationsDOI

Abstract

experiments however suggest that the increased flexibility of the unfolded state constitutes only a minor driving force to associate with the dynamic biomolecular network of the condensate. Specific protein-protein interactions in the cytoplasm in comparison to SGs determine the partitioning of folding states between the respective phases during HS.

Topics & Concepts

ChemistryProtein foldingFolding (DSP implementation)OrganelleBiophysicsCytoplasmProtein stabilityProtein aggregationUnfolded protein responseIn vitroSOD1Intrinsically disordered proteinsFunction (biology)Cell biologyBiochemistrySuperoxide dismutaseEndoplasmic reticulumEnzymeBiologyEngineeringElectrical engineeringRNA Research and SplicingHeat shock proteins researchEndoplasmic Reticulum Stress and Disease
Sequestration of Proteins in Stress Granules Relies on the In-Cell but Not the <i>In Vitro</i> Folding Stability | Litcius